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Conserved domains on  [gi|767960106|ref|XP_011517800|]
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myosin-IIIa isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
352-1041 0e+00

class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


:

Pssm-ID: 276830 [Multi-domain]  Cd Length: 633  Bit Score: 1279.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  352 NTVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISG 431
Cdd:cd01379     1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  432 ESGAGKTENAHLLVQQLTVLGKANNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLL 511
Cdd:cd01379    81 ESGAGKTESANLLVQQLTVLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  512 EKSRVIHQAIGEKNFHIFYYIYAGLAEKKKLAHYKLPENKPPRYLQNDHLrTVQDIMNNSFYKSQYELIEQCFKVIGFTM 591
Cdd:cd01379   161 EKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAKYKLPENKPPRYLQNDGL-TVQDIVNNSGNREKFEEIEQCFKVIGFTK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  592 EQLGSIYSILAAILNVGNIEFSSVATEHQIDKSH-ISNHTALENCASLLCIRADELQEALTSHCVVTRGETIIRPNTVEK 670
Cdd:cd01379   240 EEVDSVYSILAAILHIGDIEFTEVESNHQTDKSSrISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVEE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  671 ATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSgnGDELSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVF 750
Cdd:cd01379   320 ATDARDAMAKALYGRLFSWIVNRINSLLKPDRSAS--DEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIF 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  751 AWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNLKSQYFWRPKRMELSFGIH 830
Cdd:cd01379   398 AWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNIKSKYYWRPKSNALSFGIH 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  831 HYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRqlvnhpltktgnlphsktknvinyqmrtseklinlakgdtge 910
Cdd:cd01379   478 HYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR------------------------------------------ 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  911 atrharettnmktQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGFSH 990
Cdd:cd01379   516 -------------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSH 582
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767960106  991 RILFANFIKRYYLLCYKSSEEPRMSPDTCATILEKAGLDNWALGKTKVFLK 1041
Cdd:cd01379   583 RILFADFLKRYYFLAFKWNEEVVANRENCRLILERLKLDNWALGKTKVFLK 633
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
2-287 0e+00

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 649.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    2 FPLIGKTIIFDNFPDPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVRF 81
Cdd:cd06638     1 FPLSGKTIIFDSFPDPSDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   82 YGIYFKKDKVNGDKLWLVLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTE 161
Cdd:cd06638    81 YGMYYKKDVKNGDQLWLVLELCNGGSVTDLVKGFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  162 GGVKLVDFGVSAQLTSTRHRRNTSVGTPFWMAPEVIACEQQLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFK 241
Cdd:cd06638   161 GGVKLVDFGVSAQLTSTRLRRNTSVGTPFWMAPEVIACEQQLDSTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFK 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767960106  242 IPRNPPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06638   241 IPRNPPPTLHQPELWSNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
MBD_Myo3a cd21956
MORN4 binding domain (MBD) found in Myosin-IIIa and similar proteins; Myosin-IIIa, also called ...
1409-1456 7.27e-23

MORN4 binding domain (MBD) found in Myosin-IIIa and similar proteins; Myosin-IIIa, also called Myo3a, is a probable actin-based motor with ATPase and kinase activities. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Myosin-IIIa is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. It is required for normal cochlear hair bundle development and hearing, and plays an important role in the early steps of cochlear hair bundle morphogenesis. Mutations in human myosin-IIIA are responsible for progressive nonsyndromic hearing loss. This model corresponds to the MORN4 binding domain (MBD) in the tail of myosin-IIIa. MORN4 and its Drosophila ortholog retinophilin (RTP) are binding partners/cargos of class III myosins.


:

Pssm-ID: 439318 [Multi-domain]  Cd Length: 49  Bit Score: 92.91  E-value: 7.27e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 767960106 1409 KDNKDSKATSEREACGLAIFSKQISKLSEEYFILQKKLNEMILSQQLK 1456
Cdd:cd21956     1 KDRKDLKATSEKEACDLAIFSKQISKLSEKYLILQKKLNEMILSHQLK 48
 
Name Accession Description Interval E-value
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
352-1041 0e+00

class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276830 [Multi-domain]  Cd Length: 633  Bit Score: 1279.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  352 NTVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISG 431
Cdd:cd01379     1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  432 ESGAGKTENAHLLVQQLTVLGKANNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLL 511
Cdd:cd01379    81 ESGAGKTESANLLVQQLTVLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  512 EKSRVIHQAIGEKNFHIFYYIYAGLAEKKKLAHYKLPENKPPRYLQNDHLrTVQDIMNNSFYKSQYELIEQCFKVIGFTM 591
Cdd:cd01379   161 EKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAKYKLPENKPPRYLQNDGL-TVQDIVNNSGNREKFEEIEQCFKVIGFTK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  592 EQLGSIYSILAAILNVGNIEFSSVATEHQIDKSH-ISNHTALENCASLLCIRADELQEALTSHCVVTRGETIIRPNTVEK 670
Cdd:cd01379   240 EEVDSVYSILAAILHIGDIEFTEVESNHQTDKSSrISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVEE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  671 ATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSgnGDELSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVF 750
Cdd:cd01379   320 ATDARDAMAKALYGRLFSWIVNRINSLLKPDRSAS--DEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIF 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  751 AWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNLKSQYFWRPKRMELSFGIH 830
Cdd:cd01379   398 AWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNIKSKYYWRPKSNALSFGIH 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  831 HYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRqlvnhpltktgnlphsktknvinyqmrtseklinlakgdtge 910
Cdd:cd01379   478 HYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR------------------------------------------ 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  911 atrharettnmktQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGFSH 990
Cdd:cd01379   516 -------------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSH 582
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767960106  991 RILFANFIKRYYLLCYKSSEEPRMSPDTCATILEKAGLDNWALGKTKVFLK 1041
Cdd:cd01379   583 RILFADFLKRYYFLAFKWNEEVVANRENCRLILERLKLDNWALGKTKVFLK 633
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
337-1053 0e+00

Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.


Pssm-ID: 214580 [Multi-domain]  Cd Length: 677  Bit Score: 765.55  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    337 LKDVDDLATLEILDENTVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQ 416
Cdd:smart00242    5 FEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIADNAYR 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    417 SMITYNSDQCIVISGESGAGKTENAHLLVQQLTVLGKAN--NRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMK 494
Cdd:smart00242   85 NMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNteVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKFIEIH 164
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    495 FTSSGAVVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGL--AEKKKLaHYKLPENKppRYLQNDHLRTVqDIMNNsf 572
Cdd:smart00242  165 FDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGAseELKKEL-GLKSPEDY--RYLNQGGCLTV-DGIDD-- 238
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    573 yKSQYELIEQCFKVIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQIdkSHISNHTALENCASLLCIRADELQEALTS 652
Cdd:smart00242  239 -AEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAA--STVKDKEELSNAAELLGVDPEELEKALTK 315
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    653 HCVVTRGETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDsspsgNGDELSIGILDIFGFENFKKNSFEQL 732
Cdd:smart00242  316 RKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFK-----DGSTYFIGVLDIYGFEIFEVNSFEQL 390
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    733 CINIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNL 812
Cdd:smart00242  391 CINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQHH 470
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    813 K--SQYFWRPKRMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNHPLTKTGnlphSKTKNvi 890
Cdd:smart00242  471 KkhPHFSKPKKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAG----SKKRF-- 544
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    891 nyqmrtseklinlakgdtgeatrharettnmktQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLL 970
Cdd:smart00242  545 ---------------------------------QTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLH 591
                           650       660       670       680       690       700       710       720
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    971 QLRYTGILETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRMSP-DTCATILEKAGLDN--WALGKTKVFLKYYHVEQ 1047
Cdd:smart00242  592 QLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAkKACEALLQSLGLDEdeYQLGKTKVFLRPGQLAE 671

                    ....*.
gi 767960106   1048 LNLMRK 1053
Cdd:smart00242  672 LEELRE 677
Myosin_head pfam00063
Myosin head (motor domain);
340-1041 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 650.50  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   340 VDDLATLEILDENTVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMI 419
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   420 TYNSDQCIVISGESGAGKTENAHLLVQQLTVLGKANNR----TLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKF 495
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAgnvgRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   496 TSSGAVVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGLA--EKKKLahyKLPENKPPRYLQNDHLRTVqDIMNNSfy 573
Cdd:pfam00063  161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASaqLKKEL---RLTNPKDYHYLSQSGCYTI-DGIDDS-- 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   574 kSQYELIEQCFKVIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQidkSHISNHTALENCASLLCIRADELQEALTSH 653
Cdd:pfam00063  235 -EEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQ---AVPDDTENLQKAASLLGIDSTELEKALCKR 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   654 CVVTRGETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGNgdelSIGILDIFGFENFKKNSFEQLC 733
Cdd:pfam00063  311 RIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKAS----FIGVLDIYGFEIFEKNSFEQLC 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   734 INIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNL- 812
Cdd:pfam00063  387 INYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTFLDKLYSTFs 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   813 KSQYFWRPK-RMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNHPLTKtgnlphsktknvin 891
Cdd:pfam00063  467 KHPHFQKPRlQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETA-------------- 532
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   892 yqmrtSEKLINLAKGDTGEATRHARETtnmktqTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQ 971
Cdd:pfam00063  533 -----ESAAANESGKSTPKRTKKKRFI------TVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQ 601
                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767960106   972 LRYTGILETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRMSPDT-CATILEKAGLDN--WALGKTKVFLK 1041
Cdd:pfam00063  602 LRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKGDAKKgCEAILQSLNLDKeeYQFGKTKIFFR 674
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
2-287 0e+00

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 649.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    2 FPLIGKTIIFDNFPDPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVRF 81
Cdd:cd06638     1 FPLSGKTIIFDSFPDPSDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   82 YGIYFKKDKVNGDKLWLVLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTE 161
Cdd:cd06638    81 YGMYYKKDVKNGDQLWLVLELCNGGSVTDLVKGFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  162 GGVKLVDFGVSAQLTSTRHRRNTSVGTPFWMAPEVIACEQQLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFK 241
Cdd:cd06638   161 GGVKLVDFGVSAQLTSTRLRRNTSVGTPFWMAPEVIACEQQLDSTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFK 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767960106  242 IPRNPPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06638   241 IPRNPPPTLHQPELWSNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
COG5022 COG5022
Myosin heavy chain [General function prediction only];
315-1345 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 619.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  315 EKARRERIHTKKGNFNRPLISNLK--DVDDLATLEILDENTVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHS 392
Cdd:COG5022    41 KKEDGESVSVKKKVLGNDRIKLPKfdGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDII 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  393 KLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGKTENAHLLVQQLTVLGKANN---RTLQEKILQVNNL 469
Cdd:COG5022   121 QSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTveiSSIEKQILATNPI 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  470 VEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGL-AEKKKLAHYKLP 548
Cdd:COG5022   201 LEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDpEELKKLLLLQNP 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  549 ENKppRYLQNDHLRTVQDIMNnsfyKSQYELIEQCFKVIGFTMEQLGSIYSILAAILNVGNIEFSsvatEHQIDKSHISN 628
Cdd:COG5022   281 KDY--IYLSQGGCDKIDGIDD----AKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFK----EDRNGAAIFSD 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  629 HTALENCASLLCIRADELQEALTSHCVVTRGETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGng 708
Cdd:COG5022   351 NSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASN-- 428
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  709 delSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQK-PMGLL 787
Cdd:COG5022   429 ---FIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKKnPLGIL 505
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  788 SLLDEESRFPKATDQTLVEKFEGNL---KSQYFWRPKRMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDN 864
Cdd:COG5022   506 SLLDEECVMPHATDESFTSKLAQRLnknSNPKFKKSRFRDNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTN 585
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  865 SVIRQLVnhpltktgnlPHSKTKNvinyqmrtseklinlakgdtgeatrharetTNMKTQTVASYFRYSLMDLLSKMVVG 944
Cdd:COG5022   586 EFVSTLF----------DDEENIE------------------------------SKGRFPTLGSRFKESLNSLMSTLNST 625
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  945 QPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGFSHRILFANFIKRYYLLCYKSSEE-----PRMSPDTC 1019
Cdd:COG5022   626 QPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTgeytwKEDTKNAV 705
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106 1020 ATILEKAGLD--NWALGKTKVFLKYYHVEQLNLMRKEAIDKL-ILIQACVRAFLCSRRYQKIQEKRKEsaiiIQSAARGH 1096
Cdd:COG5022   706 KSILEELVIDssKYQIGNTKVFFKAGVLAALEDMRDAKLDNIaTRIQRAIRGRYLRRRYLQALKRIKK----IQVIQHGF 781
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106 1097 LVRKQRKEivDMKNTAVTTIQTS-------DQEFDYKKNFENTRESFVKKQAENAISANERFISAPNNKGSV--SVVKTS 1167
Cdd:COG5022   782 RLRRLVDY--ELKWRLFIKLQPLlsllgsrKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFgrSLKAKK 859
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106 1168 TFKPEEETTNAVESNNRVYQTPKKMnNVYEEEVKQEFYLvgpevspKQKSVKDLEENSNLRKVEKEEAMIQSY------- 1240
Cdd:COG5022   860 RFSLLKKETIYLQSAQRVELAERQL-QELKIDVKSISSL-------KLVNLELESEIIELKKSLSSDLIENLEfktelia 931
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106 1241 -YQRYTEERNCEESKAAYLERKAISERpsypvpwLAENETSFKKTLEptlsqrsIYQNANSMEKEKKTSVVTQRAPI--- 1316
Cdd:COG5022   932 rLKKLLNNIDLEEGPSIEYVKLPELNK-------LHEVESKLKETSE-------EYEDLLKKSTILVREGNKANSELknf 997
                        1050      1060      1070
                  ....*....|....*....|....*....|....*
gi 767960106 1317 ----CSQEEGRGRLRHET--VKERQVEPVTQAQEE 1345
Cdd:COG5022   998 kkelAELSKQYGALQESTkqLKELPVEVAELQSAS 1032
PTZ00014 PTZ00014
myosin-A; Provisional
362-1103 1.40e-126

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 416.35  E-value: 1.40e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  362 YSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYigsKRTAS----PPHIFAMADLGYQSMITYNSDQCIVISGESGAGK 437
Cdd:PTZ00014  120 YLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRY---RDAKDsdklPPHVFTTARRALENLHGVKKSQTIIVSGESGAGK 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  438 TENAHLLVQQ-LTVLGKANNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLLEKSRV 516
Cdd:PTZ00014  197 TEATKQIMRYfASSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRV 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  517 IHQAIGEKNFHIFYYIYAGLAEKKKlAHYKLPENKPPRYLqNDHLRTVQDIMNnsfyKSQYELIEQCFKVIGFTMEQLGS 596
Cdd:PTZ00014  277 VTQEDDERSYHIFYQLLKGANDEMK-EKYKLKSLEEYKYI-NPKCLDVPGIDD----VKDFEEVMESFDSMGLSESQIED 350
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  597 IYSILAAILNVGNIEFSSVATEHQIDKSHIS--NHTALENCASLLCIRADELQEALTSHCVVTRGETIIRPNTVEKATDV 674
Cdd:PTZ00014  351 IFSILSGVLLLGNVEIEGKEEGGLTDAAAISdeSLEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEML 430
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  675 RDAMAKTLYGRLFSWIVNCINSLLKhdssPSGnGDELSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVFAWEQ 754
Cdd:PTZ00014  431 KDSLSKAVYEKLFLWIIRNLNATIE----PPG-GFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERES 505
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  755 NEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNLKSQYFWRPKR--MELSFGIHHY 832
Cdd:PTZ00014  506 KLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKvdSNKNFVIKHT 585
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  833 AGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVnhpltktgnlphsktknvinyqmrtseklinlaKGDTGEAT 912
Cdd:PTZ00014  586 IGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLF---------------------------------EGVEVEKG 632
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  913 RHArettnmKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGFSHRI 992
Cdd:PTZ00014  633 KLA------KGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRR 706
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  993 LFANFIKRYYLLCYKSSEEPRMSP-DTCATILEKAGL--DNWALGKTKVFLKyyhveqlnlmrKEAIDKLILIQ-ACVRA 1068
Cdd:PTZ00014  707 TFAEFLSQFKYLDLAVSNDSSLDPkEKAEKLLERSGLpkDSYAIGKTMVFLK-----------KDAAKELTQIQrEKLAA 775
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....*
gi 767960106 1069 F--LCS--------RRYQKIQEKRKESAIIIQSAARGHLVRKQRK 1103
Cdd:PTZ00014  776 WepLVSvlealilkIKKKRKVRKNIKSLVRIQAHLRRHLVIAEIK 820
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
21-287 6.83e-87

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 284.04  E-value: 6.83e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106     21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDID--EEIEAEYNILKALsDHPNVVRFYGIYFKKDKvngdkLWL 98
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKdrERILREIKILKKL-KHPNIVRLYDVFEDEDK-----LYL 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106     99 VLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST 178
Cdd:smart00220   75 VMEYCEGGDLFDL----LKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPG 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    179 rHRRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQPE-LWS 257
Cdd:smart00220  151 -EKLTTFVGTPEYMAPEVLLGKG-----YGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEwDIS 224
                           250       260       270
                    ....*....|....*....|....*....|
gi 767960106    258 AEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:smart00220  225 PEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
21-283 2.14e-55

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 201.39  E-value: 2.14e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEA----EYNILKALsDHPNVVRFYGiYFkkdkVNGDKL 96
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARErfrrEARALARL-NHPNIVRVYD-VG----EEDGRP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:COG0515    83 YLVMEYVEGESLADL----LRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRH-RRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQ--P 253
Cdd:COG0515   159 GATLtQTGTVVGTPGYMAPEQARGEP-----VDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSElrP 233
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767960106  254 ELwSAEFNDFISKCLTKDYEKRP-TVSELLQ 283
Cdd:COG0515   234 DL-PPALDAIVLRALAKDPEERYqSAAELAA 263
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
22-284 1.17e-48

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 174.22  E-value: 1.17e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    22 EITETIGKGTYGKVF----KVLNKKNGQKAAVKILDPIHDID--EEIEAEYNILKALsDHPNVVRFYGIYfkkdkVNGDK 95
Cdd:pfam07714    2 TLGEKLGEGAFGEVYkgtlKGEGENTKIKVAVKTLKEGADEEerEDFLEEASIMKKL-DHPNIVKLLGVC-----TQGEP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    96 LWLVLELCSGGSVTDlvkgFL-KRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:pfam07714   76 LYIVTEYMPGGDLLD----FLrKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRD 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   175 LTSTRHRRNTSVGT--PFWMAPEVIAceqqlDTTYDARCDTWSLGITAIEL-GDGDPPLADLHPMRALFKIPRNppPKLR 251
Cdd:pfam07714  152 IYDDDYYRKRGGGKlpIKWMAPESLK-----DGKFTSKSDVWSFGVLLWEIfTLGEQPYPGMSNEEVLEFLEDG--YRLP 224
                          250       260       270
                   ....*....|....*....|....*....|...
gi 767960106   252 QPELWSAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:pfam07714  225 QPENCPDELYDLMKQCWAYDPEDRPTFSELVED 257
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
27-303 3.08e-37

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 144.58  E-value: 3.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDPIHD--IDEEIEAEYNILKALsDHPNVVRFYGIYfkkdKVNGDkLWLVLELCS 104
Cdd:PLN00034   82 IGSGAGGTVYKVIHRPTGRLYALKVIYGNHEdtVRRQICREIEILRDV-NHPNVVKCHDMF----DHNGE-IQVLLEFMD 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  105 GGSVtdlvkgflkRGERM-SEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRRN 183
Cdd:PLN00034  156 GGSL---------EGTHIaDEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMDPCN 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  184 TSVGTPFWMAPEVIACEQQlDTTYDARC-DTWSLGITAIELGDGDPPL--------ADLhpMRAlfkIPRNPPPKlrQPE 254
Cdd:PLN00034  227 SSVGTIAYMSPERINTDLN-HGAYDGYAgDIWSLGVSILEFYLGRFPFgvgrqgdwASL--MCA---ICMSQPPE--APA 298
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767960106  255 LWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQIEGKDVMLQKQLTE 303
Cdd:PLN00034  299 TASREFRHFISCCLQREPAKRWSAMQLLQHPFILRAQPGQGQGGPNLHQ 347
MBD_Myo3a cd21956
MORN4 binding domain (MBD) found in Myosin-IIIa and similar proteins; Myosin-IIIa, also called ...
1409-1456 7.27e-23

MORN4 binding domain (MBD) found in Myosin-IIIa and similar proteins; Myosin-IIIa, also called Myo3a, is a probable actin-based motor with ATPase and kinase activities. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Myosin-IIIa is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. It is required for normal cochlear hair bundle development and hearing, and plays an important role in the early steps of cochlear hair bundle morphogenesis. Mutations in human myosin-IIIA are responsible for progressive nonsyndromic hearing loss. This model corresponds to the MORN4 binding domain (MBD) in the tail of myosin-IIIa. MORN4 and its Drosophila ortholog retinophilin (RTP) are binding partners/cargos of class III myosins.


Pssm-ID: 439318 [Multi-domain]  Cd Length: 49  Bit Score: 92.91  E-value: 7.27e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 767960106 1409 KDNKDSKATSEREACGLAIFSKQISKLSEEYFILQKKLNEMILSQQLK 1456
Cdd:cd21956     1 KDRKDLKATSEKEACDLAIFSKQISKLSEKYLILQKKLNEMILSHQLK 48
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
22-283 7.08e-16

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 82.92  E-value: 7.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKILDPihDI--DEEIEA----EynilkALS----DHPNVVRFY------GIY 85
Cdd:NF033483   10 EIGERIGRGGMAEVYLAKDTRLDRDVAVKVLRP--DLarDPEFVArfrrE-----AQSaaslSHPNIVSVYdvgedgGIP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   86 FkkdkvngdklwLVLELCSGgsvTDLvKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVK 165
Cdd:NF033483   83 Y-----------IVMEYVDG---RTL-KDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  166 LVDFG----VSAQ-LTSTrhrrNTSVGTPFWMAPeviacEQQLDTTYDARCDTWSLGITAIEL--G----DGDPPLADLH 234
Cdd:NF033483  148 VTDFGiaraLSSTtMTQT----NSVLGTVHYLSP-----EQARGGTVDARSDIYSLGIVLYEMltGrppfDGDSPVSVAY 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  235 -----PMralfkiprnPPPKLRQPELwSAEFNDFISKCLTKDYEKRP-TVSELLQ 283
Cdd:NF033483  219 khvqeDP---------PPPSELNPGI-PQSLDAVVLKATAKDPDDRYqSAAEMRA 263
 
Name Accession Description Interval E-value
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
352-1041 0e+00

class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276830 [Multi-domain]  Cd Length: 633  Bit Score: 1279.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  352 NTVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISG 431
Cdd:cd01379     1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  432 ESGAGKTENAHLLVQQLTVLGKANNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLL 511
Cdd:cd01379    81 ESGAGKTESANLLVQQLTVLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  512 EKSRVIHQAIGEKNFHIFYYIYAGLAEKKKLAHYKLPENKPPRYLQNDHLrTVQDIMNNSFYKSQYELIEQCFKVIGFTM 591
Cdd:cd01379   161 EKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAKYKLPENKPPRYLQNDGL-TVQDIVNNSGNREKFEEIEQCFKVIGFTK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  592 EQLGSIYSILAAILNVGNIEFSSVATEHQIDKSH-ISNHTALENCASLLCIRADELQEALTSHCVVTRGETIIRPNTVEK 670
Cdd:cd01379   240 EEVDSVYSILAAILHIGDIEFTEVESNHQTDKSSrISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVEE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  671 ATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSgnGDELSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVF 750
Cdd:cd01379   320 ATDARDAMAKALYGRLFSWIVNRINSLLKPDRSAS--DEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIF 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  751 AWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNLKSQYFWRPKRMELSFGIH 830
Cdd:cd01379   398 AWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNIKSKYYWRPKSNALSFGIH 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  831 HYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRqlvnhpltktgnlphsktknvinyqmrtseklinlakgdtge 910
Cdd:cd01379   478 HYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR------------------------------------------ 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  911 atrharettnmktQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGFSH 990
Cdd:cd01379   516 -------------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSH 582
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767960106  991 RILFANFIKRYYLLCYKSSEEPRMSPDTCATILEKAGLDNWALGKTKVFLK 1041
Cdd:cd01379   583 RILFADFLKRYYFLAFKWNEEVVANRENCRLILERLKLDNWALGKTKVFLK 633
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
352-1041 0e+00

Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276950 [Multi-domain]  Cd Length: 633  Bit Score: 806.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  352 NTVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTAS-PPHIFAMADLGYQSMITYNSDQCIVIS 430
Cdd:cd00124     1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSADlPPHVFAVADAAYRAMLRDGQNQSILIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  431 GESGAGKTENAHLLVQQLTVLGKANNR-------TLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVG 503
Cdd:cd00124    81 GESGAGKTETTKLVLKYLAALSGSGSSkssssasSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  504 AQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGLAEKKKlAHYKLPENKPPRYLQNDHLRTVQDIMNNSFYKSQYELIEQC 583
Cdd:cd00124   161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAR-EELKLELLLSYYYLNDYLNSSGCDRIDGVDDAEEFQELLDA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  584 FKVIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQiDKSHISNHTALENCASLLCIRADELQEALTSHCVVTRGETII 663
Cdd:cd00124   240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDED-SSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETIT 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  664 RPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGNgdeLSIGILDIFGFENFKKNSFEQLCINIANEQIQY 743
Cdd:cd00124   319 KPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEST---SFIGILDIFGFENFEVNSFEQLCINYANEKLQQ 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  744 YYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNLKSQ--YFWRPK 821
Cdd:cd00124   396 FFNQHVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHprFFSKKR 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  822 RMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSdnsvirqlvnhpltktgnlphsktknvinyqmrtsekli 901
Cdd:cd00124   476 KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSG--------------------------------------- 516
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  902 nlakgdtgeatrharettnmktqtvaSYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETA 981
Cdd:cd00124   517 --------------------------SQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAV 570
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767960106  982 RIRRLGFSHRILFANFIKRYYLLCYKSSEEPRMSPDTCATIL---EKAGLDNWALGKTKVFLK 1041
Cdd:cd00124   571 RIRRAGYPVRLPFDEFLKRYRILAPGATEKASDSKKAAVLALlllLKLDSSGYQLGKTKVFLR 633
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
337-1053 0e+00

Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.


Pssm-ID: 214580 [Multi-domain]  Cd Length: 677  Bit Score: 765.55  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    337 LKDVDDLATLEILDENTVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQ 416
Cdd:smart00242    5 FEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIADNAYR 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    417 SMITYNSDQCIVISGESGAGKTENAHLLVQQLTVLGKAN--NRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMK 494
Cdd:smart00242   85 NMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNteVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKFIEIH 164
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    495 FTSSGAVVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGL--AEKKKLaHYKLPENKppRYLQNDHLRTVqDIMNNsf 572
Cdd:smart00242  165 FDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGAseELKKEL-GLKSPEDY--RYLNQGGCLTV-DGIDD-- 238
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    573 yKSQYELIEQCFKVIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQIdkSHISNHTALENCASLLCIRADELQEALTS 652
Cdd:smart00242  239 -AEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAA--STVKDKEELSNAAELLGVDPEELEKALTK 315
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    653 HCVVTRGETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDsspsgNGDELSIGILDIFGFENFKKNSFEQL 732
Cdd:smart00242  316 RKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFK-----DGSTYFIGVLDIYGFEIFEVNSFEQL 390
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    733 CINIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNL 812
Cdd:smart00242  391 CINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQHH 470
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    813 K--SQYFWRPKRMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNHPLTKTGnlphSKTKNvi 890
Cdd:smart00242  471 KkhPHFSKPKKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAG----SKKRF-- 544
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    891 nyqmrtseklinlakgdtgeatrharettnmktQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLL 970
Cdd:smart00242  545 ---------------------------------QTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLH 591
                           650       660       670       680       690       700       710       720
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    971 QLRYTGILETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRMSP-DTCATILEKAGLDN--WALGKTKVFLKYYHVEQ 1047
Cdd:smart00242  592 QLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAkKACEALLQSLGLDEdeYQLGKTKVFLRPGQLAE 671

                    ....*.
gi 767960106   1048 LNLMRK 1053
Cdd:smart00242  672 LEELRE 677
Myosin_head pfam00063
Myosin head (motor domain);
340-1041 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 650.50  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   340 VDDLATLEILDENTVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMI 419
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   420 TYNSDQCIVISGESGAGKTENAHLLVQQLTVLGKANNR----TLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKF 495
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAgnvgRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   496 TSSGAVVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGLA--EKKKLahyKLPENKPPRYLQNDHLRTVqDIMNNSfy 573
Cdd:pfam00063  161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASaqLKKEL---RLTNPKDYHYLSQSGCYTI-DGIDDS-- 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   574 kSQYELIEQCFKVIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQidkSHISNHTALENCASLLCIRADELQEALTSH 653
Cdd:pfam00063  235 -EEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQ---AVPDDTENLQKAASLLGIDSTELEKALCKR 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   654 CVVTRGETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGNgdelSIGILDIFGFENFKKNSFEQLC 733
Cdd:pfam00063  311 RIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKAS----FIGVLDIYGFEIFEKNSFEQLC 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   734 INIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNL- 812
Cdd:pfam00063  387 INYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTFLDKLYSTFs 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   813 KSQYFWRPK-RMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNHPLTKtgnlphsktknvin 891
Cdd:pfam00063  467 KHPHFQKPRlQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETA-------------- 532
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   892 yqmrtSEKLINLAKGDTGEATRHARETtnmktqTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQ 971
Cdd:pfam00063  533 -----ESAAANESGKSTPKRTKKKRFI------TVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQ 601
                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767960106   972 LRYTGILETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRMSPDT-CATILEKAGLDN--WALGKTKVFLK 1041
Cdd:pfam00063  602 LRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKGDAKKgCEAILQSLNLDKeeYQFGKTKIFFR 674
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
2-287 0e+00

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 649.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    2 FPLIGKTIIFDNFPDPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVRF 81
Cdd:cd06638     1 FPLSGKTIIFDSFPDPSDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   82 YGIYFKKDKVNGDKLWLVLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTE 161
Cdd:cd06638    81 YGMYYKKDVKNGDQLWLVLELCNGGSVTDLVKGFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  162 GGVKLVDFGVSAQLTSTRHRRNTSVGTPFWMAPEVIACEQQLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFK 241
Cdd:cd06638   161 GGVKLVDFGVSAQLTSTRLRRNTSVGTPFWMAPEVIACEQQLDSTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFK 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767960106  242 IPRNPPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06638   241 IPRNPPPTLHQPELWSNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
352-1041 0e+00

class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276862 [Multi-domain]  Cd Length: 635  Bit Score: 645.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  352 NTVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIG-SKRTASPPHIFAMADLGYQSMITYNSDQCIVIS 430
Cdd:cd14897     1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNlSVRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  431 GESGAGKTENAHLLVQQLTVLGKANNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYL 510
Cdd:cd14897    81 GESGAGKTESTKYMIKHLMKLSPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  511 LEKSRVIHQAIGEKNFHIFYYIYAGLAEKKKLaHYKLPENKPPRYLQNDHL-RTVQDIMNN-SFYKSQYELIEQCFKVIG 588
Cdd:cd14897   161 LEKSRVVHRGNGEKNFHIFYALFAGMSRDRLL-YYFLEDPDCHRILRDDNRnRPVFNDSEElEYYRQMFHDLTNIMKLIG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  589 FTMEQLGSIYSILAAILNVGNIEFssvATEHQIDKSHISNHTALENCASLLCIRADELQEALTSHCVVTRGETIIRPNTV 668
Cdd:cd14897   240 FSEEDISVIFTILAAILHLTNIVF---IPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  669 EKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGNGDELSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQH 748
Cdd:cd14897   317 RQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDY 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  749 VFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNLK-SQYFWRPKRMELSF 827
Cdd:cd14897   397 VFPRERSEYEIEGIEWRDIEYHDNDDVLELFFKKPLGILPLLDEESTFPQSTDSSLVQKLNKYCGeSPRYVASPGNRVAF 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  828 GIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLvnhpltktgnlphsktknvinyqmrtseklinlakgd 907
Cdd:cd14897   477 GIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDL------------------------------------- 519
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  908 tgeatrharettnmktqtVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLG 987
Cdd:cd14897   520 ------------------FTSYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDG 581
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767960106  988 FSHRILFANFIKRYYLLCYKSSEEPRMSPDTCATILEKAGLDNWALGKTKVFLK 1041
Cdd:cd14897   582 YPIRIKYEDFVKRYKEICDFSNKVRSDDLGKCQKILKTAGIKGYQFGKTKVFLK 635
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
362-1041 0e+00

class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276832  Cd Length: 648  Bit Score: 638.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  362 YSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGKTENA 441
Cdd:cd01381    11 YREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGESGAGKTEST 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  442 HLLVQQL-TVLGKanNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLLEKSRVIHQA 520
Cdd:cd01381    91 KLILQYLaAISGQ--HSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYLLEKSRIVSQA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  521 IGEKNFHIFYYIYAGL--AEKKKLahyKLPENKPPRYLQNDHLRTVqDIMNNSfykSQYELIEQCFKVIGFTMEQLGSIY 598
Cdd:cd01381   169 PDERNYHIFYCMLAGLsaEEKKKL---ELGDASDYYYLTQGNCLTC-EGRDDA---AEFADIRSAMKVLMFTDEEIWDIF 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  599 SILAAILNVGNIEFSSvATEHQIDKSHISNHTALENCASLLCIRADELQEALTSHCVVTRGETIIRPNTVEKATDVRDAM 678
Cdd:cd01381   242 KLLAAILHLGNIKFEA-TVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRDAF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  679 AKTLYGRLFSWIVNCINSLLKHDSSPSGngDELSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVFAWEQNEYL 758
Cdd:cd01381   321 VKGIYGRLFIWIVNKINSAIYKPRGTDS--SRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEYD 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  759 NEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNLKS-QYFWRPK-RMELSFGIHHYAGKV 836
Cdd:cd01381   399 KEGINWQHIEFVDNQDVLDLIALKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNnKNYLKPKsDLNTSFGINHFAGVV 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  837 LYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNHpltktgnlphsktknviNYQMRTSeklinlakgdtgeatrhar 916
Cdd:cd01381   479 FYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNE-----------------DISMGSE------------------- 522
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  917 etTNMKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGFSHRILFAN 996
Cdd:cd01381   523 --TRKKSPTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEE 600
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|
gi 767960106  997 FIKRYYLL-----CYKSSEEPRMSPDTCATILekAGLDNWALGKTKVFLK 1041
Cdd:cd01381   601 FVERYRVLvpgipPAHKTDCRAATRKICCAVL--GGDADYQLGKTKIFLK 648
COG5022 COG5022
Myosin heavy chain [General function prediction only];
315-1345 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 619.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  315 EKARRERIHTKKGNFNRPLISNLK--DVDDLATLEILDENTVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHS 392
Cdd:COG5022    41 KKEDGESVSVKKKVLGNDRIKLPKfdGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDII 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  393 KLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGKTENAHLLVQQLTVLGKANN---RTLQEKILQVNNL 469
Cdd:COG5022   121 QSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTveiSSIEKQILATNPI 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  470 VEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGL-AEKKKLAHYKLP 548
Cdd:COG5022   201 LEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDpEELKKLLLLQNP 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  549 ENKppRYLQNDHLRTVQDIMNnsfyKSQYELIEQCFKVIGFTMEQLGSIYSILAAILNVGNIEFSsvatEHQIDKSHISN 628
Cdd:COG5022   281 KDY--IYLSQGGCDKIDGIDD----AKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFK----EDRNGAAIFSD 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  629 HTALENCASLLCIRADELQEALTSHCVVTRGETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGng 708
Cdd:COG5022   351 NSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASN-- 428
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  709 delSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQK-PMGLL 787
Cdd:COG5022   429 ---FIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKKnPLGIL 505
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  788 SLLDEESRFPKATDQTLVEKFEGNL---KSQYFWRPKRMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDN 864
Cdd:COG5022   506 SLLDEECVMPHATDESFTSKLAQRLnknSNPKFKKSRFRDNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTN 585
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  865 SVIRQLVnhpltktgnlPHSKTKNvinyqmrtseklinlakgdtgeatrharetTNMKTQTVASYFRYSLMDLLSKMVVG 944
Cdd:COG5022   586 EFVSTLF----------DDEENIE------------------------------SKGRFPTLGSRFKESLNSLMSTLNST 625
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  945 QPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGFSHRILFANFIKRYYLLCYKSSEE-----PRMSPDTC 1019
Cdd:COG5022   626 QPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTgeytwKEDTKNAV 705
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106 1020 ATILEKAGLD--NWALGKTKVFLKYYHVEQLNLMRKEAIDKL-ILIQACVRAFLCSRRYQKIQEKRKEsaiiIQSAARGH 1096
Cdd:COG5022   706 KSILEELVIDssKYQIGNTKVFFKAGVLAALEDMRDAKLDNIaTRIQRAIRGRYLRRRYLQALKRIKK----IQVIQHGF 781
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106 1097 LVRKQRKEivDMKNTAVTTIQTS-------DQEFDYKKNFENTRESFVKKQAENAISANERFISAPNNKGSV--SVVKTS 1167
Cdd:COG5022   782 RLRRLVDY--ELKWRLFIKLQPLlsllgsrKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFgrSLKAKK 859
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106 1168 TFKPEEETTNAVESNNRVYQTPKKMnNVYEEEVKQEFYLvgpevspKQKSVKDLEENSNLRKVEKEEAMIQSY------- 1240
Cdd:COG5022   860 RFSLLKKETIYLQSAQRVELAERQL-QELKIDVKSISSL-------KLVNLELESEIIELKKSLSSDLIENLEfktelia 931
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106 1241 -YQRYTEERNCEESKAAYLERKAISERpsypvpwLAENETSFKKTLEptlsqrsIYQNANSMEKEKKTSVVTQRAPI--- 1316
Cdd:COG5022   932 rLKKLLNNIDLEEGPSIEYVKLPELNK-------LHEVESKLKETSE-------EYEDLLKKSTILVREGNKANSELknf 997
                        1050      1060      1070
                  ....*....|....*....|....*....|....*
gi 767960106 1317 ----CSQEEGRGRLRHET--VKERQVEPVTQAQEE 1345
Cdd:COG5022   998 kkelAELSKQYGALQESTkqLKELPVEVAELQSAS 1032
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
352-1041 0e+00

class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276854  Cd Length: 659  Bit Score: 618.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  352 NTVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITY----NSDQCI 427
Cdd:cd14889     1 KVLLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLGRlargPKNQCI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  428 VISGESGAGKTENAHLLVQQLTVLGKANNRtLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFtSSGAVVGAQIS 507
Cdd:cd14889    81 VISGESGAGKTESTKLLLRQIMELCRGNSQ-LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  508 EYLLEKSRVIHQAIGEKNFHIFYYIYAGL-AEKKKLahYKLPENKPPRYLQN--DHLRTVQdimnnsFYKSQYELIEQCF 584
Cdd:cd14889   159 EYLLEKSRVVHQDGGEENFHIFYYMFAGIsAEDREN--YGLLDPGKYRYLNNgaGCKREVQ------YWKKKYDEVCNAM 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  585 KVIGFTMEQLGSIYSILAAILNVGNIEFSSvaTEHQIDKSHISNHTALENCASLLCIRADELQEALTSHCVVTRGETIIR 664
Cdd:cd14889   231 DMVGFTEQEEVDMFTILAGILSLGNITFEM--DDDEALKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQR 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  665 PNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLL--KHDSSPSGNgdelSIGILDIFGFENFKKNSFEQLCINIANEQIQ 742
Cdd:cd14889   309 HHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLapKDDSSVELR----EIGILDIFGFENFAVNRFEQACINLANEQLQ 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  743 YYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNLKSQ-YFWRPK 821
Cdd:cd14889   385 YFFNHHIFLMEQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNsYYGKSR 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  822 RMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNHPLTKTGNLPHSKTKNVINyqmrtsekli 901
Cdd:cd14889   465 SKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAG---------- 534
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  902 nlakGDTGEATRharettnmkTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETA 981
Cdd:cd14889   535 ----SDNFNSTR---------KQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETI 601
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767960106  982 RIRRLGFSHRILFANFIKRY-YLLCyksseEPRMSPD--TCATILEKAGLDNWALGKTKVFLK 1041
Cdd:cd14889   602 RIRREGFSWRPSFAEFAERYkILLC-----EPALPGTkqSCLRILKATKLVGWKCGKTRLFFK 659
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
353-1041 0e+00

class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276836 [Multi-domain]  Cd Length: 690  Bit Score: 598.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  353 TVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGE 432
Cdd:cd01385     2 TLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  433 SGAGKTENAHLLVQQLTVLG-KANNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLL 511
Cdd:cd01385    82 SGSGKTESTNFLLHHLTALSqKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYLL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  512 EKSRVIHQAIGEKNFHIFYYIYAGL-AEKKKLAHYKLPENKppRYL-QNDHLrtvqdIMNNSFYKSQYELIEQCFKVIGF 589
Cdd:cd01385   162 EKSRIVSQEKNERNYHVFYYLLAGAsEEERKELHLKQPEDY--HYLnQSDCY-----TLEGEDEKYEFERLKQAMEMVGF 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  590 TMEQLGSIYSILAAILNVGNIEFSSVATEHQiDKSHISNHTALENCASLLCIRADELQEALTSHCVVTRGETIIRPNTVE 669
Cdd:cd01385   235 LPETQRQIFSVLSAVLHLGNIEYKKKAYHRD-ESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLP 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  670 KATDVRDAMAKTLYGRLFSWIVNCIN-SLLKHDSSPSGNGdeLSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQH 748
Cdd:cd01385   314 EAIATRDAMAKCLYSALFDWIVLRINhALLNKKDLEEAKG--LSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQH 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  749 VFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNLK-SQYFWRPKRMELSF 827
Cdd:cd01385   392 IFKLEQEEYKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKdNKYYEKPQVMEPAF 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  828 GIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVN-HPLTKtgnlphsKTKNVINYQMRTSEKLI----- 901
Cdd:cd01385   472 IIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGiDPVAV-------FRWAVLRAFFRAMAAFReagrr 544
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  902 NLAKGDTGEATRHARETTNM-------KTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRY 974
Cdd:cd01385   545 RAQRTAGHSLTLHDRTTKSLlhlhkkkKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRY 624
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767960106  975 TGILETARIRRLGFSHRILFANFIKRYYLLCYKSSEEprmSPDTCATILEKAGLD--NWALGKTKVFLK 1041
Cdd:cd01385   625 TGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLIS---SKEDIKDFLEKLNLDrdNYQIGKTKVFLK 690
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
362-1041 0e+00

class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276849 [Multi-domain]  Cd Length: 661  Bit Score: 585.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  362 YSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGKTENA 441
Cdd:cd14883    11 YKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGESGAGKTETT 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  442 HLLVQQLTVLGkaNNRT-LQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLLEKSRVIHQA 520
Cdd:cd14883    91 KLILQYLCAVT--NNHSwVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYLLEQSRITFQA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  521 IGEKNFHIFYYIYAGLAEKKKLAH-YKLPENKPPRYLQNDHLRTVQDIMNnsfyKSQYELIEQCFKVIGFTMEQLGSIYS 599
Cdd:cd14883   169 PGERNYHVFYQLLAGAKHSKELKEkLKLGEPEDYHYLNQSGCIRIDNIND----KKDFDHLRLAMNVLGIPEEMQEGIFS 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  600 ILAAILNVGNIEFSSVATEhQIDKSHiSNHTALENCASLLCIRADELQEALTSHCVVTRGETIIRPNTVEKATDVRDAMA 679
Cdd:cd14883   245 VLSAILHLGNLTFEDIDGE-TGALTV-EDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNRDAMA 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  680 KTLYGRLFSWIVNCINSLLkHDSSPSGNgdelSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVFAWEQNEYLN 759
Cdd:cd14883   323 KALYSRTFAWLVNHINSCT-NPGQKNSR----FIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEEYEK 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  760 EDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNL-KSQYFWRP--KRMELSFGIHHYAGKV 836
Cdd:cd14883   398 EGINWSHIVFTDNQECLDLIEKPPLGILKLLDEECRFPKGTDLTYLEKLHAAHeKHPYYEKPdrRRWKTEFGVKHYAGEV 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  837 LYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVnhpltktgnlphsktknviNYQMRTSEKLINLAKGDTGEATRhar 916
Cdd:cd14883   478 TYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELF-------------------TYPDLLALTGLSISLGGDTTSRG--- 535
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  917 etTNMKTQTVASYFRY---SLMDLLSKMvvgQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGFSHRIL 993
Cdd:cd14883   536 --TSKGKPTVGDTFKHqlqSLVDVLSAT---QPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLT 610
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767960106  994 FANFIKRYYLLCYKSSEEPRMSPDTCATILEKAGL---DNWALGKTKVFLK 1041
Cdd:cd14883   611 FKEFVDRYLCLDPRARSADHKETCGAVRALMGLGGlpeDEWQVGKTKVFLR 661
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
356-1041 0e+00

class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276829  Cd Length: 652  Bit Score: 578.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  356 EQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGA 435
Cdd:cd01378     5 ENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGESGA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  436 GKTENAHLLVQQLTVLGKANNRTLQ---EKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLLE 512
Cdd:cd01378    85 GKTEASKRIMQYIAAVSGGSESEVErvkDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYLLE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  513 KSRVIHQAIGEKNFHIFYYIYAGlAEKKKLAHYKLpENKPPRYLQNDHLRTVQDIMNNsfyKSQYELIEQCFKVIGFTME 592
Cdd:cd01378   165 KSRVVGQIKGERNFHIFYQLLKG-ASQEYLQELGL-QRPEQYYYYSKSGCFDVDGIDD---AADFKEVLNAMKVIGFTEE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  593 QLGSIYSILAAILNVGNIEFssvaTEHQIDKSHISNHTALENCASLLCIRADELQEALTSHCVVTRGE---TIIRPNTVE 669
Cdd:cd01378   240 EQDSIFRILAAILHLGNIQF----AEDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGgrsVYEVPLNVE 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  670 KATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGNgdelSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHV 749
Cdd:cd01378   316 QAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKK----VIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELT 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  750 FAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFP-KATDQTLVEKFEGNLKS--QYFWRPKRMEL- 825
Cdd:cd01378   392 LKAEQEEYVREGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNhpHFECPSGHFELr 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  826 --SFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNHPltktgnlphsktknvinyqmrtseklinl 903
Cdd:cd01378   472 rgEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEG----------------------------- 522
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  904 akgdtgeatrhaRETTNMKT-QTVASYFRYS---LMDLLSKMvvgQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILE 979
Cdd:cd01378   523 ------------VDLDSKKRpPTAGTKFKNSanaLVETLMKK---QPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLE 587
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  980 TARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRMSP-DTCATILEKAGLDN--WALGKTKVFLK 1041
Cdd:cd01378   588 NVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWqGGVESILKDLNIPPeeYQMGKTKIFIR 652
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
362-1041 0e+00

class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276838 [Multi-domain]  Cd Length: 657  Bit Score: 567.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  362 YSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGKTENA 441
Cdd:cd01387    11 YERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGESGSGKTEAT 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  442 HLLVQQLTVLGKANNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFtSSGAVVGAQISEYLLEKSRVIHQAI 521
Cdd:cd01387    91 KLIMQYLAAVNQRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAITSQYLLEKSRIVTQAK 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  522 GEKNFHIFYYIYAGLAEKKKLAhYKLPENKPPRYLQ---NDHLRTVQDIMNnsfyksqYELIEQCFKVIGFTMEQLGSIY 598
Cdd:cd01387   170 NERNYHVFYELLAGLPAQLRQK-YGLQEAEKYFYLNqggNCEIAGKSDADD-------FRRLLAAMQVLGFSSEEQDSIF 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  599 SILAAILNVGNIEFSSVATEHQIDKSHISNHTALENCASLLCIRADELQEALTSHCVVTRGETIIRPNTVEKATDVRDAM 678
Cdd:cd01387   242 RILASVLHLGNVYFHKRQLRHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDARDAI 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  679 AKTLYGRLFSWIVNCINSLLKhdsspSGNGDELSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVFAWEQNEYL 758
Cdd:cd01387   322 AKALYALLFSWLVTRVNAIVY-----SGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYI 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  759 NEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGN-LKSQYFWRPKRMELSFGIHHYAGKVL 837
Cdd:cd01387   397 REQIDWTEIAFADNQPVINLISKKPVGILHILDDECNFPQATDHSFLEKCHYHhALNELYSKPRMPLPEFTIKHYAGQVW 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  838 YNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLvnhpltktgnlphskTKNVINyqmRTSEKLINLAKGdtgeatRHAre 917
Cdd:cd01387   477 YQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHL---------------FSSHRA---QTDKAPPRLGKG------RFV-- 530
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  918 TTNMKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGFSHRILFANF 997
Cdd:cd01387   531 TMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVF 610
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|
gi 767960106  998 IKRY-YLLcykSSEEPRMSP-DTCATILEK----AGLDNWALGKTKVFLK 1041
Cdd:cd01387   611 IDRYrCLV---ALKLPRPAPgDMCVSLLSRlctvTPKDMYRLGATKVFLR 657
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
358-1041 0e+00

class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276951 [Multi-domain]  Cd Length: 662  Bit Score: 564.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  358 LEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGK 437
Cdd:cd01377     7 LRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITGESGAGK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  438 TENAHLLVQQLTVLGKANNR---------TLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISE 508
Cdd:cd01377    87 TENTKKVIQYLASVAASSKKkkesgkkkgTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIAGADIET 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  509 YLLEKSRVIHQAIGEKNFHIFYYIYAGLAEKKKLAHYKLPENKPPRYLQNDHL--RTVQDimnnsfyKSQYELIEQCFKV 586
Cdd:cd01377   167 YLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELtiDGVDD-------AEEFKLTDEAFDI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  587 IGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQidkSHISNHTALENCASLLCIRADELQEALTSHCVVTRGETIIRPN 666
Cdd:cd01377   240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQ---AELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQ 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  667 TVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSpsgngDELSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYN 746
Cdd:cd01377   317 NKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSK-----RQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFN 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  747 QHVFAWEQNEYLNEDVDarvieyednWPLLD--MFLQ--------KPMGLLSLLDEESRFPKATDQTLVEK----FEGNL 812
Cdd:cd01377   392 HHMFVLEQEEYKKEGIE---------WTFIDfgLDLQptidliekPNMGILSILDEECVFPKATDKTFVEKlysnHLGKS 462
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  813 KSQYFWRPKRMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNHPLTKTGNLPHSKTKNVINy 892
Cdd:cd01377   463 KNFKKPKPKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGGGKKKKKGGSF- 541
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  893 qmrtseklinlakgdtgeatrharettnmktQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQL 972
Cdd:cd01377   542 -------------------------------RTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQL 590
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767960106  973 RYTGILETARIRRLGFSHRILFANFIKRYYLLCyksseePRMSPDT-------CATILEKAGLDN--WALGKTKVFLK 1041
Cdd:cd01377   591 RCNGVLEGIRICRKGFPNRIIFAEFKQRYSILA------PNAIPKGfddgkaaCEKILKALQLDPelYRIGNTKVFFK 662
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
14-287 0e+00

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 543.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   14 FPDPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVRFYGIYFKKDK-VN 92
Cdd:cd06608     1 LPDPAGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEEIKLEINILRKFSNHPNIATFYGAFIKKDPpGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   93 GDKLWLVLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS 172
Cdd:cd06608    81 DDQLWLVMEYCGGGSVTDLVKGLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLTSTRHRRNTSVGTPFWMAPEVIACEQQLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQ 252
Cdd:cd06608   161 AQLDSTLGRRNTFIGTPYWMAPEVIACDQQPDASYDARCDVWSLGITAIELADGKPPLCDMHPMRALFKIPRNPPPTLKS 240
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767960106  253 PELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06608   241 PEKWSKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
362-1041 4.42e-179

class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.


Pssm-ID: 276835  Cd Length: 647  Bit Score: 551.51  E-value: 4.42e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  362 YSRDQIYVYVGDILIALNPFQSLG-LYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGKTEN 440
Cdd:cd01384    11 YELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVSGESGAGKTET 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  441 AHLLVQQLTVLGKANN---RTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLLEKSRVI 517
Cdd:cd01384    91 TKMLMQYLAYMGGRAVtegRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRTYLLERSRVV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  518 HQAIGEKNFHIFYYIYAGlAEKKKLAHYKLPENKPPRYLQNDHLRTVQDIMNNSFYKSQYELIEqcfkVIGFTMEQLGSI 597
Cdd:cd01384   171 QVSDPERNYHCFYQLCAG-APPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMD----VVGISEEEQDAI 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  598 YSILAAILNVGNIEFSSVAtehQIDKSHISNHTA---LENCASLLCIRADELQEALTSHCVVTRGETIIRPNTVEKATDV 674
Cdd:cd01384   246 FRVVAAILHLGNIEFSKGE---EDDSSVPKDEKSefhLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAATLS 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  675 RDAMAKTLYGRLFSWIVNCINSLLKHD-SSPSgngdelSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVFAWE 753
Cdd:cd01384   323 RDALAKTIYSRLFDWLVDKINRSIGQDpNSKR------LIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKME 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  754 QNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNLK-SQYFWRPKRMELSFGIHHY 832
Cdd:cd01384   397 QEEYTKEEIDWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPRSTHETFAQKLYQTLKdHKRFSKPKLSRTDFTIDHY 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  833 AGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVnhPLtktgnLPHSKTKNvinyqmrtseklinlakgdtgeat 912
Cdd:cd01384   477 AGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLF--PP-----LPREGTSS------------------------ 525
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  913 rharettNMKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGFSHRI 992
Cdd:cd01384   526 -------SSKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRK 598
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*....
gi 767960106  993 LFANFIKRYYLLCYKSSEEPRMSPDTCATILEKAGLDNWALGKTKVFLK 1041
Cdd:cd01384   599 PFEEFLDRFGLLAPEVLKGSDDEKAACKKILEKAGLKGYQIGKTKVFLR 647
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
358-1041 5.30e-179

class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276834  Cd Length: 647  Bit Score: 551.54  E-value: 5.30e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  358 LEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYigSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGK 437
Cdd:cd01383     7 LEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY--RQKLLDSPHVYAVADTAYREMMRDEINQSIIISGESGAGK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  438 TENAHLLVQQLTVLGKANNRtLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLLEKSRVI 517
Cdd:cd01383    85 TETAKIAMQYLAALGGGSSG-IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTYLLEKSRVV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  518 HQAIGEKNFHIFYYIYAGL--AEKKKLahyKLPENKPPRYLQNDHLRTVQDIMNnsfyKSQYELIEQCFKVIGFTMEQLG 595
Cdd:cd01383   164 QLANGERSYHIFYQLCAGAspALREKL---NLKSASEYKYLNQSNCLTIDGVDD----AKKFHELKEALDTVGISKEDQE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  596 SIYSILAAILNVGNIEFSSVATEHQIDkshISNHTALENCASLLCIRADELQEALTSHCVVTRGETIIRPNTVEKATDVR 675
Cdd:cd01383   237 HIFQMLAAVLWLGNISFQVIDNENHVE---VVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDAR 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  676 DAMAKTLYGRLFSWIVNCINSLLKHDSSPSGNgdelSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVFAWEQN 755
Cdd:cd01383   314 DALAKAIYASLFDWLVEQINKSLEVGKRRTGR----SISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQE 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  756 EYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNLKSQYFWRpKRMELSFGIHHYAGK 835
Cdd:cd01383   390 EYELDGIDWTKVDFEDNQECLDLIEKKPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFK-GERGGAFTIRHYAGE 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  836 VLYNASGFLAKNRDTLPTDIVLLLRSSDNSvirqlvnhpltktgnLPHSKTknvinyqmrtseklINLAKGDTGEATRHA 915
Cdd:cd01383   469 VTYDTSGFLEKNRDLLHSDLIQLLSSCSCQ---------------LPQLFA--------------SKMLDASRKALPLTK 519
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  916 RETTNMKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGFSHRILFA 995
Cdd:cd01383   520 ASGSDSQKQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQ 599
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*...
gi 767960106  996 NFIKRYYLLCYKSSEEPRMSPDTCATILEKAGL--DNWALGKTKVFLK 1041
Cdd:cd01383   600 EFARRYGFLLPEDVSASQDPLSTSVAILQQFNIlpEMYQVGYTKLFFR 647
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
364-1041 1.64e-176

class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276831 [Multi-domain]  Cd Length: 629  Bit Score: 544.06  E-value: 1.64e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  364 RDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGKTENAHL 443
Cdd:cd01380    14 RNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSGESGAGKTVSAKY 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  444 LVQQLTVLGKANNRTLQ--EKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLLEKSRVIHQAI 521
Cdd:cd01380    94 AMRYFATVGGSSSGETQveEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRTYLLEKSRVVFQAE 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  522 GEKNFHIFYYIYAG--LAEKKKLAHYKlpenkpprylQNDHLRTVQ---DIMNNSFYKSQYELIEQCFKVIGFTMEQLGS 596
Cdd:cd01380   174 EERNYHIFYQLCAAasLPELKELHLGS----------AEDFFYTNQggsPVIDGVDDAAEFEETRKALTLLGISEEEQME 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  597 IYSILAAILNVGNIEFSSVATEHQIDKshiSNHTALENCASLLCIRADELQEALTSHCVVTRGETIIRPNTVEKATDVRD 676
Cdd:cd01380   244 IFRILAAILHLGNVEIKATRNDSASIS---PDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  677 AMAKTLYGRLFSWIVNCINSLLKHDSSPSgngDELSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVFAWEQNE 756
Cdd:cd01380   321 ALAKHIYAQLFDWIVDRINKALASPVKEK---QHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEE 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  757 YLNEDVDARVIEYEDNWPLLDMFlQKPMGLLSLLDEESRFPKATDQTLVEKFEGNL---KSQYFWRPKRMELSFGIHHYA 833
Cdd:cd01380   398 YVKEEIEWSFIDFYDNQPCIDLI-EGKLGILDLLDEECRLPKGSDENWAQKLYNQHlkkPNKHFKKPRFSNTAFIVKHFA 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  834 GKVLYNASGFLAKNRDTLPTDIVLLLRSSDNsvirqlvnhpltktgnlphsktknvinyqmrtseklinlakgdtgeatr 913
Cdd:cd01380   477 DDVEYQVEGFLEKNRDTVSEEHLNVLKASKN------------------------------------------------- 507
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  914 harettnmKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGFSHRIL 993
Cdd:cd01380   508 --------RKKTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWT 579
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|
gi 767960106  994 FANFIKRYYLLCYKSSEEPRMSPDTCATILEKAGLDN--WALGKTKVFLK 1041
Cdd:cd01380   580 YEEFFSRYRVLLPSKEWLRDDKKKTCENILENLILDPdkYQFGKTKIFFR 629
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
362-1041 2.35e-175

class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276840 [Multi-domain]  Cd Length: 651  Bit Score: 542.08  E-value: 2.35e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  362 YSRDQIYVYVGDILIALNPFQSL-GLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGKTEN 440
Cdd:cd14873    11 YKRNQIYTYIGSILASVNPYQPIaGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISGESGAGKTES 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  441 AHLLVQQLTVL--------GKANNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLLE 512
Cdd:cd14873    91 TKLILKFLSVIsqqslelsLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQGGRIVDYLLE 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  513 KSRVIHQAIGEKNFHIFYYIYAGLAEKKKLAHY-KLPENKppRYLQNDHLRTVQDIMNnsfyKSQYELIEQCFKVIGFTM 591
Cdd:cd14873   171 KNRVVRQNPGERNYHIFYALLAGLEHEEREEFYlSTPENY--HYLNQSGCVEDKTISD----QESFREVITAMEVMQFSK 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  592 EQLGSIYSILAAILNVGNIEFSSVAtehqidKSHISNHTALENCASLLCIRADELQEALTSHCVVTRGETIIRPNTVEKA 671
Cdd:cd14873   245 EEVREVSRLLAGILHLGNIEFITAG------GAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  672 TDVRDAMAKTLYGRLFSWIVNCINSLLKhdsspsGNGDELSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVFA 751
Cdd:cd14873   319 VDSRDSLAMALYARCFEWVIKKINSRIK------GKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFS 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  752 WEQNEYLNEDVDARVIEYEDNWPLLDMfLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNLKSQYFW-RPKRMELSFGIH 830
Cdd:cd14873   393 LEQLEYSREGLVWEDIDWIDNGECLDL-IEKKLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYvKPRVAVNNFGVK 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  831 HYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNHPLTKTGnlphsktknvinyqmrtseklinlakGDT-G 909
Cdd:cd14873   472 HYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNN--------------------------QDTlK 525
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  910 EATRHarettnmKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGFS 989
Cdd:cd14873   526 CGSKH-------RRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYA 598
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767960106  990 HRILFANFIKRYYLLCyKSSEEPRMSPDTCATILEK--AGLDNWALGKTKVFLK 1041
Cdd:cd14873   599 VRRPFQDFYKRYKVLM-RNLALPEDVRGKCTSLLQLydASNSEWQLGKTKVFLR 651
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
1-287 9.74e-174

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 523.40  E-value: 9.74e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    1 MFPLIGKTIIFDNFPDPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVR 80
Cdd:cd06639     4 LFPYNSSMLGLESLADPSDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEEIEAEYNILRSLPNHPNVVK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   81 FYGIYFKKDKVNGDKLWLVLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTT 160
Cdd:cd06639    84 FYGMFYKADQYVGGQLWLVLELCNGGSVTELVKGLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  161 EGGVKLVDFGVSAQLTSTRHRRNTSVGTPFWMAPEVIACEQQLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALF 240
Cdd:cd06639   164 EGGVKLVDFGVSAQLTSARLRRNTSVGTPFWMAPEVIACEQQYDYSYDARCDVWSLGITAIELADGDPPLFDMHPVKALF 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767960106  241 KIPRNPPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06639   244 KIPRNPPPTLLNPEKWCRGFSHFISQCLIKDFEKRPSVTHLLEHPFI 290
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
356-1041 9.86e-165

class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276855 [Multi-domain]  Cd Length: 662  Bit Score: 513.94  E-value: 9.86e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  356 EQLEKCYSRDQIYVYVGDILIALNPFQSL-GLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMI----TYNSDQCIVIS 430
Cdd:cd14890     5 HTLRLRYERDEIYTYVGPILISINPYKSIpDLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIqsgvLDPSNQSIIIS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  431 GESGAGKTENAHLLVQQLT---------------VLGKANNRT---LQEKILQVNNLVEAFGNACTIINDNSSRFGKYLE 492
Cdd:cd14890    85 GESGAGKTEATKIIMQYLAritsgfaqgasgegeAASEAIEQTlgsLEDRVLSSNPLLESFGNAKTLRNDNSSRFGKFIE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  493 MKFTSSGAVVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGlAEKKKLAHYKLPENKPPRYLQND--HLRTVQDimnn 570
Cdd:cd14890   165 IQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAG-ADEALRERLKLQTPVEYFYLRGEcsSIPSCDD---- 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  571 sfyKSQYELIEQCFKVIGFTMEQLGSIYSILAAILNVGNIEFSSV-ATEHQIDkshISNHTALENCASLLCIRADELQEA 649
Cdd:cd14890   240 ---AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESEnDTTVLED---ATTLQSLKLAAELLGVNEDALEKA 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  650 LTSHCVVTRGETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGngdelSIGILDIFGFENFKKNSF 729
Cdd:cd14890   314 LLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWG-----FIGVLDIYGFEKFEWNTF 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  730 EQLCINIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKP---MGLLSLLDEESRFpKATDQTLve 806
Cdd:cd14890   389 EQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVngkPGIFITLDDCWRF-KGEEANK-- 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  807 KFEGNLKSQY------------------FWRPK-RMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVi 867
Cdd:cd14890   466 KFVSQLHASFgrksgsggtrrgssqhphFVHPKfDADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSI- 544
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  868 rqlvnhpltktgnlphsktknvinyqmrtseklinlakgdtgeatrhaRETtnmktqTVASYFRYSLMDLLSKMVVGQPH 947
Cdd:cd14890   545 ------------------------------------------------REV------SVGAQFRTQLQELMAKISLTNPR 570
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  948 FVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGFSHRILFANFIKRYYLLcYKSSEEPRMSPDTCATILeKAG 1027
Cdd:cd14890   571 YVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVL-LPTAENIEQLVAVLSKML-GLG 648
                         730
                  ....*....|....
gi 767960106 1028 LDNWALGKTKVFLK 1041
Cdd:cd14890   649 KADWQIGSSKIFLK 662
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
358-1038 2.30e-157

class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276839  Cd Length: 644  Bit Score: 493.91  E-value: 2.30e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  358 LEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYI--GSKRTasPPHIFAMADLGYQSMITYNSDQCIVISGESGA 435
Cdd:cd14872     7 LRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMhkGPKEM--PPHTYNIADDAYRAMIVDAMNQSILISGESGA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  436 GKTENAHllvQQLT----VLGKANNrtLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLL 511
Cdd:cd14872    85 GKTEATK---QCLSffaeVAGSTNG--VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENYLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  512 EKSRVIHQAIGEKNFHIFYYIYAGLAEKKKlahYKLPENKPPRYL---QNDHLRTVQDimnnsfyKSQYELIEQCFKVIG 588
Cdd:cd14872   160 EKSRVVYQIKGERNFHIFYQLLASPDPASR---GGWGSSAAYGYLslsGCIEVEGVDD-------VADFEEVVLAMEQLG 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  589 FTMEQLGSIYSILAAILNVGNIEFSSVATEHQIDKSHISNHTALENCASLLCIRADELQEALTSHCVVTRG--ETIIrPN 666
Cdd:cd14872   230 FDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIKGcdPTRI-PL 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  667 TVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKhdssPSGNGDELSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYN 746
Cdd:cd14872   309 TPAQATDACDALAKAAYSRLFDWLVKKINESMR----PQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFN 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  747 QHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNLKSQYFWRP---KRM 823
Cdd:cd14872   385 QYTFKLEEALYQSEGVKFEHIDFIDNQPVLDLIEKKQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYaevRTS 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  824 ELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIrqLVNHPLTktgnLPHSKTKNVinyqmrtseklinl 903
Cdd:cd14872   465 RTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLI--AVLFPPS----EGDQKTSKV-------------- 524
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  904 akgdtgeatrharettnmktqTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARI 983
Cdd:cd14872   525 ---------------------TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKI 583
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767960106  984 RRLGFSHRILFANFIKRY-YLLCYKSSEEPRMSPDTCATILEKAGLDNWAL--GKTKV 1038
Cdd:cd14872   584 RKTGYPFRYSHERFLKRYrFLVKTIAKRVGPDDRQRCDLLLKSLKQDFSKVqvGKTRV 641
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
362-1041 3.18e-150

class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276853 [Multi-domain]  Cd Length: 667  Bit Score: 475.34  E-value: 3.18e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  362 YSRDQIYVYVGDILIALNPFQSL-GLYSTK---HSKLYIGSKrtasPPHIFAMADLGYQSMITYNSDQCIVISGESGAGK 437
Cdd:cd14888    11 FDIDEIYTFTGPILIAVNPFKTIpGLYSDEmllKFIQPSISK----SPHVFSTASSAYQGMCNNKKSQTILISGESGAGK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  438 TENAHLLVQQLTVLGKAN--NRTLQE-KILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFT---------SSGAVVGAQ 505
Cdd:cd14888    87 TESTKYVMKFLACAGSEDikKRSLVEaQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSklkskrmsgDRGRLCGAK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  506 ISEYLLEKSRVIHQAIGEKNFHIFYYIYAGlAEKKKLAHYKLPENKPPRYLQNDHLRTVQDI-----MNNSFYKSQYELI 580
Cdd:cd14888   167 IQTYLLEKVRVCDQQEGERNYHIFYQLCAA-AREAKNTGLSYEENDEKLAKGADAKPISIDMssfepHLKFRYLTKSSCH 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  581 E-------QCFK-------VIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQIDKSHISNHTALENCASLLCIRADEL 646
Cdd:cd14888   246 ElpdvddlEEFEstlyamqTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDDLEKVASLLGVDAEDL 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  647 QEALTSHCVVTRGETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSgngdELSIGILDIFGFENFKK 726
Cdd:cd14888   326 LNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNS----LLFCGVLDIFGFECFQL 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  727 NSFEQLCINIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTL-- 804
Cdd:cd14888   402 NSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKPLGIFCMLDEECFVPGGKDQGLcn 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  805 --VEKFEGNLKsqyFWRPKRMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVnhpltktgnlp 882
Cdd:cd14888   482 klCQKHKGHKR---FDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLF----------- 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  883 hsktknvinyqmrtsEKLINlakgdtgeatRHARETTNMKT-QTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQAR 961
Cdd:cd14888   548 ---------------SAYLR----------RGTDGNTKKKKfVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPD 602
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  962 KYDKEKVLLQLRYTGILETARIRRLGFSHRILFANFIKRYYLLCYKSseeprmspdtcatilEKAGLDNWALGKTKVFLK 1041
Cdd:cd14888   603 LFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLNGE---------------GKKQLSIWAVGKTLCFFK 667
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
362-1041 6.18e-149

class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276857 [Multi-domain]  Cd Length: 656  Bit Score: 471.55  E-value: 6.18e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  362 YSRDQIYVYVGDILIALNPFQSLGLystkhskLY----------IGSKRTASPPHIFAMADLGYQSM----ITYNSDQCI 427
Cdd:cd14892    11 YERDAIYTFTADILISINPYKSIPL-------LYdvpgfdsqrkEEATASSPPPHVFSIAERAYRAMkgvgKGQGTPQSI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  428 VISGESGAGKTENAHLLVQQLTVLGKANNRTLQEK------------ILQVNNLVEAFGNACTIINDNSSRFGKYLEMKF 495
Cdd:cd14892    84 VVSGESGAGKTEASKYIMKYLATASKLAKGASTSKgaanahesieecVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHY 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  496 TSSGAVVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGLAEKKKLAHyKLPENKPPRYLQNDHLRTVQDIMNnsfyKS 575
Cdd:cd14892   164 NSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAAL-ELTPAESFLFLNQGNCVEVDGVDD----AT 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  576 QYELIEQCFKVIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQIDkSHISNHTALENCASLLCIRADELQEALTSHCV 655
Cdd:cd14892   239 EFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVF-AQSADGVNVAKAAGLLGVDAAELMFKLVTQTT 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  656 VT-RGETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLK-HDSSPSGNGDELS----IGILDIFGFENFKKNSF 729
Cdd:cd14892   318 STaRGSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKqQTSGVTGGAASPTfspfIGILDIFGFEIMPTNSF 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  730 EQLCINIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFP-KATDQTLVEKF 808
Cdd:cd14892   398 EQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKPLGLLPLLEEQMLLKrKTTDKQLLTIY 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  809 EGN-LKSQYFWRPKRME-LSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSdnsvirqlvnhpltktgnlphskt 886
Cdd:cd14892   478 HQThLDKHPHYAKPRFEcDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSS------------------------ 533
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  887 knvinyqmrtseklinlakgdtgeatrharettnmktqtvaSYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKE 966
Cdd:cd14892   534 -----------------------------------------SKFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCE 572
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  967 KVLLQLRYTGILETARIRRLGFSHRILFANFIKRYYLLC---YKSSEEPRMSPDT-----CATILEKA-GLDNWALGKTK 1037
Cdd:cd14892   573 LVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLArnkAGVAASPDACDATtarkkCEEIVARAlERENFQLGRTK 652

                  ....
gi 767960106 1038 VFLK 1041
Cdd:cd14892   653 VFLR 656
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
362-1041 6.47e-149

class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276833  Cd Length: 649  Bit Score: 471.35  E-value: 6.47e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  362 YSRDQIYVYVGDILIALNP-FQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGKTEN 440
Cdd:cd01382    11 YSKDKIYTYVANILIAVNPyFDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGESGAGKTES 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  441 AHLLVQQLTVLGKANNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLLEKSRVIHQA 520
Cdd:cd01382    91 TKYILRYLTESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQS 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  521 IGEKNFHIFYYIYAGLAE--KKKLahyklpenkppryLQNDHLRTVQDimnnsfyksqYELIEQCFKVIGFTMEQLGSIY 598
Cdd:cd01382   171 KEERNYHIFYRLCAGAPEdlREKL-------------LKDPLLDDVGD----------FIRMDKAMKKIGLSDEEKLDIF 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  599 SILAAILNVGNIEF----SSVATEHQIDKshiSNHTALENCASLLCIRADELQEALTSHCVVTRGE----TIIR-PNTVE 669
Cdd:cd01382   228 RVVAAVLHLGNIEFeengSDSGGGCNVKP---KSEQSLEYAAELLGLDQDELRVSLTTRVMQTTRGgakgTVIKvPLKVE 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  670 KATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSgngdelSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHV 749
Cdd:cd01382   305 EANNARDALAKAIYSKLFDHIVNRINQCIPFETSSY------FIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERI 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  750 FAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNLKSQYFW---RPKRM--- 823
Cdd:cd01382   379 LKEEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLVGILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLsipRKSKLkih 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  824 -ELS----FGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLvnhpltktgnLPHSKTKNVINYQmrTSE 898
Cdd:cd01382   459 rNLRddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSL----------FESSTNNNKDSKQ--KAG 526
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  899 KLINLakgdtgeatrharettnmktqTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGIL 978
Cdd:cd01382   527 KLSFI---------------------SVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMV 585
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767960106  979 ETARIRRLGFSHRILFANFIKRY--YLlcykSSEEPRMSPDT-CATILEKAGLDN--WALGKTKVFLK 1041
Cdd:cd01382   586 SVLDLMQGGFPSRTSFHDLYNMYkkYL----PPKLARLDPRLfCKALFKALGLNEndFKFGLTKVFFR 649
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
362-1015 1.98e-148

class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276867 [Multi-domain]  Cd Length: 716  Bit Score: 472.45  E-value: 1.98e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  362 YSRDQIYVYVGDILIALNPFQSL-GLYSTKHSKLY--------IGSKRTASPPHIFAMADLGYQSMI-TYNSDQCIVISG 431
Cdd:cd14902    11 FEHDQIYTSIGDILVALNPLKPLpDLYSESQLNAYkasmtstsPVSQLSELPPHVFAIGGKAFGGLLkPERRNQSILVSG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  432 ESGAGKTENAHLLVQQLTVLGKANNRTLQE---------KILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVV 502
Cdd:cd14902    91 ESGSGKTESTKFLMQFLTSVGRDQSSTEQEgsdaveigkRILQTNPILESFGNAQTIRNDNSSRFGKFIKIQFGANNEIV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  503 GAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGlAEKKKLAHYKLpeNKPPRYL----QNDHLRTVQDIMNNsfYKSQYE 578
Cdd:cd14902   171 GAQIVSYLLEKVRLLHQSPEERSFHIFYELLEG-ADKTLLDLLGL--QKGGKYEllnsYGPSFARKRAVADK--YAQLYV 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  579 LIEQCFKVIGFTMEQLGSIYSILAAILNVGNIEFSsvATEHQIDKSHISNHTA--LENCASLLCIRADELQEALTSHCVV 656
Cdd:cd14902   246 ETVRAFEDTGVGELERLDIFKILAALLHLGNVNFT--AENGQEDATAVTAASRfhLAKCAELMGVDVDKLETLLSSREIK 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  657 TRGETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGNGDE----LSIGILDIFGFENFKKNSFEQL 732
Cdd:cd14902   324 AGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSISDEdeelATIGILDIFGFESLNRNGFEQL 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  733 CINIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFegnl 812
Cdd:cd14902   404 CINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSNGLFSLLDQECLMPKGSNQALSTKF---- 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  813 kSQYFWRpkrmELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNHPltktgnlphsktkNVINY 892
Cdd:cd14902   480 -YRYHGG----LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADE-------------NRDSP 541
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  893 QmrtseklinlakGDTGEATRhaRETTNMKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQL 972
Cdd:cd14902   542 G------------ADNGAAGR--RRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQM 607
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 767960106  973 RYTGILETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRMS 1015
Cdd:cd14902   608 RSVGVLEAVRIARHGYSVRLAHASFIELFSGFKCFLSTRDRAA 650
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
358-1040 2.01e-146

class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276866 [Multi-domain]  Cd Length: 655  Bit Score: 464.65  E-value: 2.01e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  358 LEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYI--GSKRTAS----PPHIFAMADLGYQSMITYNS----DQCI 427
Cdd:cd14901     7 LRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYYehGERRAAGerklPPHVYAVADKAFRAMLFASRgqkcDQSI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  428 VISGESGAGKTENAHLLVQQLTVLGKANNR--------TLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSG 499
Cdd:cd14901    87 LVSGESGAGKTETTKIIMNYLASVSSATTHgqnatereNVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRLGFASSG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  500 AVVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGlAEKKKLAHYKLPENKPPRYLQN----DHLRTVQDimnnsfyKS 575
Cdd:cd14901   167 SLLGASISTYLLERVRLVSQAKGERNYHIFYELLRG-ASSDELHALGLTHVEEYKYLNSsqcyDRRDGVDD-------SV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  576 QYELIEQCFKVIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHqiDKSHISNHTALENCASLLCIRADELQEALTSHCV 655
Cdd:cd14901   239 QYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEG--GTFSMSSLANVRAACDLLGLDMDVLEKTLCTREI 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  656 VTRGETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSpsgNGDELSIGILDIFGFENFKKNSFEQLCIN 735
Cdd:cd14901   317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSES---TGASRFIGIVDIFGFEIFATNSLEQLCIN 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  736 IANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNL-KS 814
Cdd:cd14901   394 FANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLaKH 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  815 QYFWRPK--RMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIrqlvnhpltktgnlphsktknviny 892
Cdd:cd14901   474 ASFSVSKlqQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFL------------------------- 528
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  893 qmrtseklinlakgdtgeatrharettnmkTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQL 972
Cdd:cd14901   529 ------------------------------SSTVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQL 578
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767960106  973 RYTGILETARIRRLGFSHRILFANFIKRYylLCYKSS----------EEPRMSPDTCATILEKAGLDNWALGKTKVFL 1040
Cdd:cd14901   579 RCSGVLEAVKISRSGYPVRFPHDAFVHTY--SCLAPDgasdtwkvneLAERLMSQLQHSELNIEHLPPFQVGKTKVFL 654
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
358-1041 3.24e-145

class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276868 [Multi-domain]  Cd Length: 658  Bit Score: 461.55  E-value: 3.24e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  358 LEKCYSRDQIYVYVGDILIALNPFQSL-GLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAG 436
Cdd:cd14903     7 VKKRFLRKLPYTYTGDICIAVNPYQWLpELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVSGESGAG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  437 KTENAHLLVQQL-TVLGKANNRTLqEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLLEKSR 515
Cdd:cd14903    87 KTETTKILMNHLaTIAGGLNDSTI-KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRTYLLEKTR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  516 VIHQAIGEKNFHIFYYIYAGLAEKKKLAHYKLPENKPPRYLQNDHLRTVQDimnnsfyKSQYELIEQCFKVIGFTMEQLG 595
Cdd:cd14903   166 VISHERPERNYHIFYQLLASPDVEERLFLDSANECAYTGANKTIKIEGMSD-------RKHFARTKEALSLIGVSEEKQE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  596 SIYSILAAILNVGNIEFSSVATEHQIDKSHISNHTALeNCASLLCIRADELQEALTSHCVVTRGETIIRPNTVEKATDVR 675
Cdd:cd14903   239 VLFEVLAGILHLGQLQIQSKPNDDEKSAIAPGDQGAV-YATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDCR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  676 DAMAKTLYGRLFSWIVNCINSLLKHDSSpSGNgdelSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVFAWEQN 755
Cdd:cd14903   318 DALAKAIYSNVFDWLVATINASLGNDAK-MAN----HIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQI 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  756 EYLNEDVDARVIEYEDNWPLLDMfLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNLKSQY----FWRPKRMElsFGIHH 831
Cdd:cd14903   393 EYEEEGIRWAHIDFADNQDVLAV-IEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQdvieFPRTSRTQ--FTIKH 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  832 YAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVnhpltKTGNLPHSktknvinyqmrtseklinlAKGDTGEA 911
Cdd:cd14903   470 YAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLF-----KEKVESPA-------------------AASTSLAR 525
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  912 TRHARETTNMKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGFSHR 991
Cdd:cd14903   526 GARRRRGGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNR 605
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767960106  992 ILFANFIKRYYLLCYKSSEEPRMSPDTCATILEKAGLD---NWALGKTKVFLK 1041
Cdd:cd14903   606 LLHEEFLDKFWLFLPEGRNTDVPVAERCEALMKKLKLEspeQYQMGLTRIYFQ 658
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
358-1041 1.11e-140

class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276861 [Multi-domain]  Cd Length: 644  Bit Score: 448.85  E-value: 1.11e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  358 LEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGK 437
Cdd:cd14896     7 LKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSGHSGSGK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  438 TENAHLLVQQLTVLG--KANNRTLQ-EKILQVnnlVEAFGNACTIINDNSSRFGKYLEMkFTSSGAVVGAQISEYLLEKS 514
Cdd:cd14896    87 TEAAKKIVQFLSSLYqdQTEDRLRQpEDVLPI---LESFGHAKTILNANASRFGQVLRL-HLQHGVIVGASVSHYLLETS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  515 RVIHQAIGEKNFHIFYYIYAGLAEKKKLAHYkLPENKPPRYL---QNDHLRTVQDimnnsfyKSQYELIEQCFKVIGFTM 591
Cdd:cd14896   163 RVVFQAQAERSFHVFYELLAGLDPEEREQLS-LQGPETYYYLnqgGACRLQGKED-------AQDFEGLLKALQGLGLCA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  592 EQLGSIYSILAAILNVGNIEFSSVATEHQiDKSHISNHTALENCASLLCIRADELQEALTSHCVVTRGETIIRPNTVEKA 671
Cdd:cd14896   235 EELTAIWAVLAAILQLGNICFSSSERESQ-EVAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGA 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  672 TDVRDAMAKTLYGRLFSWIVNCINSLLkhdsSPSGNGDELS-IGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVF 750
Cdd:cd14896   314 IDARDALAKTLYSRLFTWLLKRINAWL----APPGEAESDAtIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLL 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  751 AWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEK---FEGNlkSQYFWRPKRMELSF 827
Cdd:cd14896   390 AQEEEECQRELLPWVPIPQPPRESCLDLLVDQPHSLLSILDDQTWLSQATDHTFLQKchyHHGD--HPSYAKPQLPLPVF 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  828 GIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNHPLTKTGNLPHSKtknvinyqmrtseklinlakgd 907
Cdd:cd14896   468 TVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP---------------------- 525
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  908 tgeatrharettnmktqTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLG 987
Cdd:cd14896   526 -----------------TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEG 588
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767960106  988 FSHRILFANFIKRYYLLCyKSSEEPRMSPDTCATILEK---AGLDNWALGKTKVFLK 1041
Cdd:cd14896   589 FPVRVPFQAFLARFGALG-SERQEALSDRERCGAILSQvlgAESPLYHLGATKVLLK 644
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
358-1041 3.95e-138

class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276872 [Multi-domain]  Cd Length: 669  Bit Score: 442.93  E-value: 3.95e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  358 LEKCYSRDQIYVYVGDILIALNPFQSL-GLYSTKHSKLY---IGSKRTA-----SPPHIFAMADLGYQSMITYNSDQCIV 428
Cdd:cd14907     7 LKKRYQQDKIFTYVGPTLIVMNPYKQIdNLFSEEVMQMYkeqIIQNGEYfdikkEPPHIYAIAALAFKQLFENNKKQAIV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  429 ISGESGAGKTENAHLLVQQLTVLG-KANNR------------------TLQEKILQVNNLVEAFGNACTIINDNSSRFGK 489
Cdd:cd14907    87 ISGESGAGKTENAKYAMKFLTQLSqQEQNSeevltltssiratskstkSIEQKILSCNPILEAFGNAKTVRNDNSSRFGK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  490 Y----LEMKftsSGAVVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGlAEKKKLAHYKLPENKP---PRYLQNDHLR 562
Cdd:cd14907   167 YvsilVDKK---KRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYG-ADQQLLQQLGLKNQLSgdrYDYLKKSNCY 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  563 TVQDIMNNSFYKsqyELIEQcFKVIGFTMEQLGSIYSILAAILNVGNIEFSSVaTEHQIDKSHISNHTALENCASLLCIR 642
Cdd:cd14907   243 EVDTINDEKLFK---EVQQS-FQTLGFTEEEQDSIWRILAAILLLGNLQFDDS-TLDDNSPCCVKNKETLQIIAKLLGID 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  643 ADELQEALTSHCVVTRGETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSP---SGNGDELSIGILDIF 719
Cdd:cd14907   318 EEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMPKDEKdqqLFQNKYLSIGLLDIF 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  720 GFENFKKNSFEQLCINIANEQIQYYYNQHVFAWEQNEYLNEDVDARV--IEYEDNWPLLDMFLQKPMGLLSLLDEESRFP 797
Cdd:cd14907   398 GFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSYTDNQDVIDLLDKPPIGIFNLLDDSCKLA 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  798 KATDQTLVEKF--EGNLKSQYFWRPKRMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVnhpL 875
Cdd:cd14907   478 TGTDEKLLNKIkkQHKNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF---S 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  876 TKTGNLPHSKTKNVINYQmrtseklinlakgdtgeatrharettnmKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPN 955
Cdd:cd14907   555 GEDGSQQQNQSKQKKSQK----------------------------KDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPN 606
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  956 SERQARKYDKEKVLLQLRYTGILETARIRRLGFSHRILFANFIKRYYLLcyksseeprmspdtcatilekagLDNWALGK 1035
Cdd:cd14907   607 EEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLL-----------------------KKNVLFGK 663

                  ....*.
gi 767960106 1036 TKVFLK 1041
Cdd:cd14907   664 TKIFMK 669
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
357-1041 6.72e-138

class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276844 [Multi-domain]  Cd Length: 656  Bit Score: 441.56  E-value: 6.72e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  357 QLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGS--KRTAS-PPHIFAMADLGYQSMITYNSDQCIVISGES 433
Cdd:cd14878     6 EIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLSSsgQLCSSlPPHLFSCAERAFHQLFQERRPQCFILSGER 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  434 GAGKTENAHLLVQQLTVLGKANNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTS-SGAVVGAQISEYLLE 512
Cdd:cd14878    86 GSGKTEASKQIMKHLTCRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCErKKHLTGARIYTYMLE 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  513 KSRVIHQAIGEKNFHIFYYIYAGLAEKKKLAHYkLPENKPPRYLqNDHLRTVQDIMNNSFYKSQYELIEQCFKVIGFTME 592
Cdd:cd14878   166 KSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLH-LNNLCAHRYL-NQTMREDVSTAERSLNREKLAVLKQALNVVGFSSL 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  593 QLGSIYSILAAILNVGNIEFSSVATEhqiDKSHISNHTALENCASLLCIRADELQEALTSHCVVTRGETIIRPNTVEKAT 672
Cdd:cd14878   244 EVENLFVILSAILHLGDIRFTALTEA---DSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  673 DVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGNgDELSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVFAW 752
Cdd:cd14878   321 FYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSM-QTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQ 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  753 EQNEYLNEDVDARVIEYEDNWP-LLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNLKSQ-----YF--------W 818
Cdd:cd14878   400 EQTECVQEGVTMETAYSPGNQTgVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLESSntnavYSpmkdgngnV 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  819 RPKRMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNHPLTktgnlphsktknvinyqmrtse 898
Cdd:cd14878   480 ALKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLV---------------------- 537
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  899 klinlakgdtgeatrharettnmktqTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGIL 978
Cdd:cd14878   538 --------------------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVL 591
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  979 ETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRMSP--DTCATILEKAGLDNWALGKTKVFLK 1041
Cdd:cd14878   592 EMVKIFRYGYPVRLSFSDFLSRYKPLADTLLGEKKKQSaeERCRLVLQQCKLQGWQMGVRKVFLK 656
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
353-1019 3.69e-136

class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276865  Cd Length: 627  Bit Score: 435.89  E-value: 3.69e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  353 TVSEQLEKCYSRDQIYVYVGDILIALNPFQSL-GLYSTKHSKLYIGS-----------KRTASPPHIFAMADLGYQSMI- 419
Cdd:cd14900     2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLpGLYSSDTMAKYLLSfearssstrnkGSDPMPPHIYQVAGEAYKAMMl 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  420 ---TYNSDQCIVISGESGAGKTENAHLLVQQLTVLGKANNR----------TLQEKILQVNNLVEAFGNACTIINDNSSR 486
Cdd:cd14900    82 glnGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAasvsmgkstsGIAAKVLQTNILLESFGNARTLRNDNSSR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  487 FGKYLEMKFTSSGAVVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGLAEKKklahyklpenkppryLQNDHLRTVQD 566
Cdd:cd14900   162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAA---------------RKRDMYRRVMD 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  567 IMNnsfyksqyelieqcfkVIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQI--DKSHI--SNHTALENCASLLCIR 642
Cdd:cd14900   227 AMD----------------IIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLgqLKSDLapSSIWSRDAAATLLSVD 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  643 ADELQEALTSHCVVTRGETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGNGDELSIGILDIFGFE 722
Cdd:cd14900   291 ATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKSHGGLHFIGILDIFGFE 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  723 NFKKNSFEQLCINIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQ 802
Cdd:cd14900   371 VFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRPTGILSLIDEECVMPKGSDT 450
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  803 TLVEKFEGNLKSQYFWRPKRMELS---FGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSsdnsvirqlvnhpltktg 879
Cdd:cd14900   451 TLASKLYRACGSHPRFSASRIQRArglFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVY------------------ 512
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  880 nlphsktknvinyqmrtseklinlakgdtgeatrharettnmktqtvASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQ 959
Cdd:cd14900   513 -----------------------------------------------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCK 545
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767960106  960 ARKYDKEKVLLQLRYTGILETARIRRLGFSHRILFANFIKRYYLLcyKSSEEPRMS-------PDTC 1019
Cdd:cd14900   546 AGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSL--ARAKNRLLAkkqgtslPDTD 610
MYSc_Myo21 cd14882
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...
353-1041 2.61e-135

class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276848  Cd Length: 642  Bit Score: 434.17  E-value: 2.61e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  353 TVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGE 432
Cdd:cd14882     2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  433 SGAGKTENAHLLVQQLTVLGKANNRTlQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLLE 512
Cdd:cd14882    82 SYSGKTTNARLLIKHLCYLGDGNRGA-TGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  513 KSRVIHQAIGEKNFHIFYYIYAGLAEKKKLAHYKLPENKPPRYLQND------HLRTVQDIMNNSFYKsqYELIEQCFKV 586
Cdd:cd14882   161 KLRVSTTDGNQSNFHIFYYFYDFIEAQNRLKEYNLKAGRNYRYLRIPpevppsKLKYRRDDPEGNVER--YKEFEEILKD 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  587 IGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQIDKSHISNhtaleNCASLLCIRADELQEALTSHCVVTRGETIIRPN 666
Cdd:cd14882   239 LDFNEEQLETVRKVLAAILNLGEIRFRQNGGYAELENTEIAS-----RVAELLRLDEKKFMWALTNYCLIKGGSAERRKH 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  667 TVEKATDVRDAMAKTLYGRLFSWIVNCINslLKHDSSPSGNGDELSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYN 746
Cdd:cd14882   314 TTEEARDARDVLASTLYSRLVDWIINRIN--MKMSFPRAVFGDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYN 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  747 QHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRfpKATDQTLVEKFEGNLKSQYFWRPKRMEls 826
Cdd:cd14882   392 QRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDASR--SCQDQNYIMDRIKEKHSQFVKKHSAHE-- 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  827 FGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNhpltktgnlphsktknviNYQMRtseklinlakg 906
Cdd:cd14882   468 FSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFT------------------NSQVR----------- 518
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  907 dtgeatrharettnmKTQTVASYFRYSLMDLLSKMVVGQ----PHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETAR 982
Cdd:cd14882   519 ---------------NMRTLAATFRATSLELLKMLSIGAnsggTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAK 583
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767960106  983 IRRLGFSHRILFANFIKRYYLLCYKSSEEPRMSPDTCATILEKAGLDNWALGKTKVFLK 1041
Cdd:cd14882   584 ARQKGFSYRIPFQEFLRRYQFLAFDFDETVEMTKDNCRLLLIRLKMEGWAIGKTKVFLK 642
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
358-1041 2.46e-133

class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276860 [Multi-domain]  Cd Length: 704  Bit Score: 430.91  E-value: 2.46e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  358 LEKCYSRDQIYVYVGDILIALNPFQSL-GLYSTK--HSKLYigsKRTASPPHIFAMADLGYQSMITYN-------SDQCI 427
Cdd:cd14895     7 LAQRYGVDQVYCRSGAVLIAVNPFKHIpGLYDLHkyREEMP---GWTALPPHVFSIAEGAYRSLRRRLhepgaskKNQTI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  428 VISGESGAGKTENAHLLVQQLTVLGKANNRTLQEK---------ILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFT-- 496
Cdd:cd14895    84 LVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKrrraisgseLLSANPILESFGNARTLRNDNSSRFGKFVRMFFEgh 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  497 ---SSGAVVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGLAEKKKL-AHYKLPENKPPRYLQNDHLRTVQDIMNNsf 572
Cdd:cd14895   164 eldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLeLQLELLSAQEFQYISGGQCYQRNDGVRD-- 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  573 yKSQYELIEQCFKVIGFTMEQLGSIYSILAAILNVGNIEFSSVATehqiDKSHISNHTALENC----------------- 635
Cdd:cd14895   242 -DKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSE----DEGEEDNGAASAPCrlasaspssltvqqhld 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  636 --ASLLCIRADELQEALTSHCVVTRGETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSL---LKHDSSPSGNGDE 710
Cdd:cd14895   317 ivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSAspqRQFALNPNKAANK 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  711 LS---IGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLL 787
Cdd:cd14895   397 DTtpcIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRPSGIF 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  788 SLLDEESRFPKATDQTLVEKFEGNLKSQYFW---RPKRMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDN 864
Cdd:cd14895   477 SLLDEECVVPKGSDAGFARKLYQRLQEHSNFsasRTDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGKTSD 556
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  865 SVIRQL---VNHPLTKTGNLPHSKTKnvinyqmrtseklinlakgdtgeatrhaRETTNMKTQTVASYFRYSLMDLLSKM 941
Cdd:cd14895   557 AHLRELfefFKASESAELSLGQPKLR----------------------------RRSSVLSSVGIGSQFKQQLASLLDVV 608
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  942 VVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGFSHRILFANFIKRYYLLcyksSEEPRMSPDTCAT 1021
Cdd:cd14895   609 QQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLL----VAAKNASDATASA 684
                         730       740
                  ....*....|....*....|
gi 767960106 1022 ILEKAGLDNWALGKTKVFLK 1041
Cdd:cd14895   685 LIETLKVDHAELGKTRVFLR 704
MYSc_Myh15_mammals cd14929
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...
353-1041 2.48e-132

class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276892 [Multi-domain]  Cd Length: 662  Bit Score: 426.70  E-value: 2.48e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  353 TVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGE 432
Cdd:cd14929     2 SVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  433 SGAGKTENAHLLVQQLTVLG-----KANNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQIS 507
Cdd:cd14929    82 SGAGKTVNTKHIIQYFATIAamiesKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADID 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  508 EYLLEKSRVIHQAIGEKNFHIFYYIYAGlaeKKKLAHYKLPENKPPRYlqndHLRTVQDIMNNSFYKSQyELI--EQCFK 585
Cdd:cd14929   162 IYLLEKSRVIFQQPGERNYHIFYQILSG---KKELRDLLLVSANPSDF----HFCSCGAVAVESLDDAE-ELLatEQAMD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  586 VIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQIDKSHISNhtaLENCASLLCIRADELQEALTSHCVVTRGETIIRP 665
Cdd:cd14929   234 ILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTEN---ADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRS 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  666 NTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLkhDSSPSgngDELSIGILDIFGFENFKKNSFEQLCINIANEQIQYYY 745
Cdd:cd14929   311 QNIEQVTYAVGALSKSIYERMFKWLVARINRVL--DAKLS---RQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFF 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  746 NQHVFAWEQNEYLNEDVDARVIEYE-DNWPLLDmFLQKPMGLLSLLDEESRFPKATDQTLVEK-FEGNL-KSQYFWRPKR 822
Cdd:cd14929   386 NQHMFVLEQEEYRKEGIDWVSIDFGlDLQACID-LIEKPMGIFSILEEECMFPKATDLTFKTKlFDNHFgKSVHFQKPKP 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  823 MELSFGIH----HYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNHPLTKTGNLPHsktknvinyqmrtse 898
Cdd:cd14929   465 DKKKFEAHfelvHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSAIQF--------------- 529
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  899 klinlakgdtGEATRhaRETTNMktQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGIL 978
Cdd:cd14929   530 ----------GEKKR--KKGASF--QTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVL 595
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767960106  979 ETARIRRLGFSHRILFANFIKRYYLLcyksseEPRMSPDT--------CATILEKAGLDN--WALGKTKVFLK 1041
Cdd:cd14929   596 EGIRICREGFPNRLLYADFKQRYCIL------NPRTFPKSkfvssrkaAEELLGSLEIDHtqYRFGITKVFFK 662
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
359-1041 3.26e-130

class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276856  Cd Length: 645  Bit Score: 420.22  E-value: 3.26e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  359 EKCYSRDQ-IYVYVGDILIALNPFQSLglySTKHSKLYIGSKRTASPPHIFAMADLGYQSMItYNS----DQCIVISGES 433
Cdd:cd14891     9 ERSKLDNQrPYTFMANVLIAVNPLRRL---PEPDKSDYINTPLDPCPPHPYAIAEMAYQQMC-LGSgrmqNQSIVISGES 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  434 GAGKTENAHLLVQQLT---VLGKANNR---------------TLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKF 495
Cdd:cd14891    85 GAGKTETSKIILRFLTtraVGGKKASGqdieqsskkrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSRFGKFMKLQF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  496 TSSG-AVVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGlAEKKKLAHYKLPENKPPRYLQNDHLRTVQDIMNnsfyK 574
Cdd:cd14891   165 TKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAG-ASAELLKELLLLSPEDFIYLNQSGCVSDDNIDD----A 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  575 SQYELIEQCFKVIGFTMEQLGSIYSILAAILNVGNIEFSSVAT-EHQIDKSHISNHTALENCASLLCIRADELQEALTSH 653
Cdd:cd14891   240 ANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTsEGEAEIASESDKEALATAAELLGVDEEALEKVITQR 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  654 CVVTRGETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSspsgngDELS-IGILDIFGFENFK-KNSFEQ 731
Cdd:cd14891   320 EIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDP------DPLPyIGVLDIFGFESFEtKNDFEQ 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  732 LCINIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATD----QTLVEK 807
Cdd:cd14891   394 LLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPNGILPLLDNEARNPNPSDaklnETLHKT 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  808 FEGNlksQYFWRP--KRMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSdnsvirqlvnhpltktgnlphsk 885
Cdd:cd14891   474 HKRH---PCFPRPhpKDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS----------------------- 527
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  886 tkNVINYQMRTsekLInlakgDTGEATRharettnmktqtvasyfryslmdllskmvvgqPHFVRCIKPNSERQARKYDK 965
Cdd:cd14891   528 --AKFSDQMQE---LV-----DTLEATR--------------------------------CNFIRCIKPNAAMKVGVFDN 565
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  966 EKVLLQLRYTGILETARIRRLGFSHRILFANfIKRYYLLCYKSSEEPRM-SPDTCAT--ILekagldnWA---------L 1033
Cdd:cd14891   566 RYVVDQLRCSGILQTCEVLKVGLPTRVTYAE-LVDVYKPVLPPSVTRLFaENDRTLTqaIL-------WAfrvpsdayrL 637

                  ....*...
gi 767960106 1034 GKTKVFLK 1041
Cdd:cd14891   638 GRTRVFFR 645
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
358-1041 1.62e-128

class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276869  Cd Length: 653  Bit Score: 415.88  E-value: 1.62e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  358 LEKCYSRDQIYVYVGDILIALNPFQSL-GLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAG 436
Cdd:cd14904     7 LKKRFAASKPYTYTNDIVIALNPYKWIdNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVSGESGAG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  437 KTENAHLLVQQLT-VLGKANNRTLqEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLLEKSR 515
Cdd:cd14904    87 KTETTKIVMNHLAsVAGGRKDKTI-AKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETYLLEKSR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  516 VIHQAIGEKNFHIFYYIYAGLAeKKKLAHYKLPENKPPRYLQNDHLRTVQDIMNNS--FYKSQYELieqcfKVIGFTMEQ 593
Cdd:cd14904   166 VVSIAEGERNYHIFYQLLAGLS-SEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAklFASTQKSL-----SLIGLDNDA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  594 LGSIYSILAAILNVGNIEFSsvatEHQIDKSHISNHTALENCASLLCIRADELQEALTSHCVVTRGETIIRPNTVEKATD 673
Cdd:cd14904   240 QRTLFKILSGVLHLGEVMFD----KSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEE 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  674 VRDAMAKTLYGRLFSWIVNCINSLLKHDSSP-SGNgdelsIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVFAW 752
Cdd:cd14904   316 NRDALAKAIYSKLFDWMVVKINAAISTDDDRiKGQ-----IGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKT 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  753 EQNEYLNEDVDARVIEYEDNWPLLDMFLQKpMGLLSLLDEESRFPKATDQTLVEKFEGNLKSQ----YFWRPKRMELSFG 828
Cdd:cd14904   391 VEEEYIREGLQWDHIEYQDNQGIVEVIDGK-MGIIALMNDHLRQPRGTEEALVNKIRTNHQTKkdneSIDFPKVKRTQFI 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  829 IHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVnhpltktgnlphsktknvinyqmrtseklinlakgDT 908
Cdd:cd14904   470 INHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELF-----------------------------------GS 514
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  909 GEATRHARETTNMKT----QTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIR 984
Cdd:cd14904   515 SEAPSETKEGKSGKGtkapKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRIT 594
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  985 RLGFSHRILFANFIKRYYLLcYKSSEEPRMSPDTCATILEKAGLDN---WALGKTKVFLK 1041
Cdd:cd14904   595 RSGYPSRLTPKELATRYAIM-FPPSMHSKDVRRTCSVFMTAIGRKSpleYQIGKSLIYFK 653
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
353-1041 1.76e-128

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276876 [Multi-domain]  Cd Length: 674  Bit Score: 416.69  E-value: 1.76e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  353 TVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGE 432
Cdd:cd14911     2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  433 SGAGKTENAHLLVQQLTVLGKANNRT-----------------LQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKF 495
Cdd:cd14911    82 SGAGKTENTKKVIQFLAYVAASKPKGsgavphpavnpavligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  496 TSSGAVVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGLAEKKKlAHYKLPENKPPRYLQNDHLRT--VQDimnnsfy 573
Cdd:cd14911   162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQR-EKFILDDVKSYAFLSNGSLPVpgVDD------- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  574 KSQYELIEQCFKVIGFTMEQLGSIYSILAAILNVGNIEFSSvatEHQIDKSHISNHTALENCASLLCIRADELQEA-LTS 652
Cdd:cd14911   234 YAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQ---ERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAfLTP 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  653 HCVVTRgETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGNgdelSIGILDIFGFENFKKNSFEQL 732
Cdd:cd14911   311 RIKVGR-DFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGAS----FIGILDMAGFEIFELNSFEQL 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  733 CINIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYE-DNWPLLDMfLQKPMGLLSLLDEESRFPKATDQTLVEKfegn 811
Cdd:cd14911   386 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDL-IDKPGGIMALLDEECWFPKATDKTFVDK---- 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  812 LKSQYFWRPKRME------LSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIrqlvnhpltktgnlphsk 885
Cdd:cd14911   461 LVSAHSMHPKFMKtdfrgvADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFV------------------ 522
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  886 tknvinYQMRTSEKLINLAKGDTGEATRHARETTNMkTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDK 965
Cdd:cd14911   523 ------VNIWKDAEIVGMAQQALTDTQFGARTRKGM-FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDA 595
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767960106  966 EKVLLQLRYTGILETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRMS-PDTCATILEKAGLDN--WALGKTKVFLK 1041
Cdd:cd14911   596 PLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDgKKACEKMIQALELDSnlYRVGQSKIFFR 674
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
353-1041 2.20e-128

class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276952 [Multi-domain]  Cd Length: 673  Bit Score: 416.33  E-value: 2.20e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  353 TVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGE 432
Cdd:cd14920     2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  433 SGAGKTENAHLLVQQLT-VLGKANNRT-------LQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGA 504
Cdd:cd14920    82 SGAGKTENTKKVIQYLAhVASSHKGRKdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  505 QISEYLLEKSRVIHQAIGEKNFHIFYYIYAGLAEKKKlAHYKLPENKPPRYLQNDHLRTVQDIMNNSFYKSQyelieQCF 584
Cdd:cd14920   162 NIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLK-SDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETM-----EAM 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  585 KVIGFTMEQLGSIYSILAAILNVGNIEFSSvatEHQIDKSHISNHTALENCASLLCIRADELQEA-LTSHCVVTRgETII 663
Cdd:cd14920   236 HIMGFSHEEILSMLKVVSSVLQFGNISFKK---ERNTDQASMPENTVAQKLCHLLGMNVMEFTRAiLTPRIKVGR-DYVQ 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  664 RPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGNgdelSIGILDIFGFENFKKNSFEQLCINIANEQIQY 743
Cdd:cd14920   312 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS----FIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  744 YYNQHVFAWEQNEYLNEDVDARVIEYE-DNWPLLDMFLQ--KPMGLLSLLDEESRFPKATDQTLVEKFEGNLKSQ-YFWR 819
Cdd:cd14920   388 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHsKFQK 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  820 PK--RMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLvnhpltktgnlphskTKNVINYQMRTS 897
Cdd:cd14920   468 PRqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAEL---------------WKDVDRIVGLDQ 532
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  898 EKLINLAKGDTGEATRHARettnmkTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGI 977
Cdd:cd14920   533 VTGMTETAFGSAYKTKKGM------FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGV 606
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767960106  978 LETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRMS-PDTCATILEKAGLDN--WALGKTKVFLK 1041
Cdd:cd14920   607 LEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDgKQACERMIRALELDPnlYRIGQSKIFFR 673
MYSc_Myh1_insects_crustaceans cd14909
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
353-1041 3.14e-127

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276874  Cd Length: 666  Bit Score: 412.70  E-value: 3.14e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  353 TVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGE 432
Cdd:cd14909     2 SVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  433 SGAGKTENAHLLVQQLTVLGKANNR--------TLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGA 504
Cdd:cd14909    82 SGAGKTENTKKVIAYFATVGASKKTdeaakskgSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAGA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  505 QISEYLLEKSRVIHQAIGEKNFHIFYYIYAGlaekkklahyKLPENKPPRYLQNDhlrtVQDIMNNSFYK---------S 575
Cdd:cd14909   162 DIETYLLEKARVISQQSLERSYHIFYQIMSG----------SVPGVKEMCLLSDN----IYDYYIVSQGKvtvpnvddgE 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  576 QYELIEQCFKVIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQIDKSHISNHtalENCASLLCIRADELQEALTSHCV 655
Cdd:cd14909   228 EFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEG---GRVSKLFGCDTAELYKNLLKPRI 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  656 VTRGETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKhdsspSGNGDELSIGILDIFGFENFKKNSFEQLCIN 735
Cdd:cd14909   305 KVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-----TQQKRQHFIGVLDIAGFEIFEYNGFEQLCIN 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  736 IANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNL--K 813
Cdd:cd14909   380 FTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHlgK 459
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  814 SQYFWRPK-----RMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQL-VNHPltktgnlphsktk 887
Cdd:cd14909   460 SAPFQKPKppkpgQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIfADHA------------- 526
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  888 nvinyqmrtseklinlAKGDTGEATRHARETTNMKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEK 967
Cdd:cd14909   527 ----------------GQSGGGEQAKGGRGKKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHL 590
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767960106  968 VLLQLRYTGILETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRMSPDTCATILEKAGLD--NWALGKTKVFLK 1041
Cdd:cd14909   591 VMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEEDPKKAAEIILESIALDpdQYRLGHTKVFFR 666
PTZ00014 PTZ00014
myosin-A; Provisional
362-1103 1.40e-126

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 416.35  E-value: 1.40e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  362 YSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYigsKRTAS----PPHIFAMADLGYQSMITYNSDQCIVISGESGAGK 437
Cdd:PTZ00014  120 YLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRY---RDAKDsdklPPHVFTTARRALENLHGVKKSQTIIVSGESGAGK 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  438 TENAHLLVQQ-LTVLGKANNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLLEKSRV 516
Cdd:PTZ00014  197 TEATKQIMRYfASSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRV 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  517 IHQAIGEKNFHIFYYIYAGLAEKKKlAHYKLPENKPPRYLqNDHLRTVQDIMNnsfyKSQYELIEQCFKVIGFTMEQLGS 596
Cdd:PTZ00014  277 VTQEDDERSYHIFYQLLKGANDEMK-EKYKLKSLEEYKYI-NPKCLDVPGIDD----VKDFEEVMESFDSMGLSESQIED 350
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  597 IYSILAAILNVGNIEFSSVATEHQIDKSHIS--NHTALENCASLLCIRADELQEALTSHCVVTRGETIIRPNTVEKATDV 674
Cdd:PTZ00014  351 IFSILSGVLLLGNVEIEGKEEGGLTDAAAISdeSLEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEML 430
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  675 RDAMAKTLYGRLFSWIVNCINSLLKhdssPSGnGDELSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVFAWEQ 754
Cdd:PTZ00014  431 KDSLSKAVYEKLFLWIIRNLNATIE----PPG-GFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERES 505
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  755 NEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNLKSQYFWRPKR--MELSFGIHHY 832
Cdd:PTZ00014  506 KLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKvdSNKNFVIKHT 585
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  833 AGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVnhpltktgnlphsktknvinyqmrtseklinlaKGDTGEAT 912
Cdd:PTZ00014  586 IGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLF---------------------------------EGVEVEKG 632
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  913 RHArettnmKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGFSHRI 992
Cdd:PTZ00014  633 KLA------KGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRR 706
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  993 LFANFIKRYYLLCYKSSEEPRMSP-DTCATILEKAGL--DNWALGKTKVFLKyyhveqlnlmrKEAIDKLILIQ-ACVRA 1068
Cdd:PTZ00014  707 TFAEFLSQFKYLDLAVSNDSSLDPkEKAEKLLERSGLpkDSYAIGKTMVFLK-----------KDAAKELTQIQrEKLAA 775
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....*
gi 767960106 1069 F--LCS--------RRYQKIQEKRKESAIIIQSAARGHLVRKQRK 1103
Cdd:PTZ00014  776 WepLVSvlealilkIKKKRKVRKNIKSLVRIQAHLRRHLVIAEIK 820
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
353-1041 1.68e-122

class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276953 [Multi-domain]  Cd Length: 676  Bit Score: 400.10  E-value: 1.68e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  353 TVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGE 432
Cdd:cd14927     2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  433 SGAGKTENAHLLVQQLTV--------------LGKANNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSS 498
Cdd:cd14927    82 SGAGKTVNTKRVIQYFAIvaalgdgpgkkaqfLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  499 GAVVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGlaEKKKLAHYKLPENKPPRYLQNDHLRTVQDIMNNSfykSQYE 578
Cdd:cd14927   162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSG--KKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDG---EELM 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  579 LIEQCFKVIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQidkSHISNHTALENCASLLCIRADELQEALTSHCVVTR 658
Cdd:cd14927   237 ATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQ---AEADGTESADKAAYLMGVSSADLLKGLLHPRVKVG 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  659 GETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLkHDSSPSgngdELSIGILDIFGFENFKKNSFEQLCINIAN 738
Cdd:cd14927   314 NEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTL-DTKLPR----QFFIGVLDIAGFEIFEFNSFEQLCINFTN 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  739 EQIQYYYNQHVFAWEQNEYLNEDVDARVIEYE-DNWPLLDMfLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNL--KSQ 815
Cdd:cd14927   389 EKLQQFFNHHMFILEQEEYKREGIEWVFIDFGlDLQACIDL-IEKPLGILSILEEECMFPKASDASFKAKLYDNHlgKSP 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  816 YFWRPK-----RMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLvnhpltktgnlphsktknvi 890
Cdd:cd14927   468 NFQKPRpdkkrKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATL-------------------- 527
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  891 nYQMRTSEKLINLAKGDTGEATRHArettnMKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLL 970
Cdd:cd14927   528 -YENYVGSDSTEDPKSGVKEKRKKA-----ASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLH 601
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  971 QLRYTGILETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRMSPDTCAT--ILEKAGLDN--WALGKTKVFLK 1041
Cdd:cd14927   602 QLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIPDDKFVDSRKATekLLGSLDIDHtqYQFGHTKVFFK 676
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
362-1041 3.13e-122

class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276843  Cd Length: 649  Bit Score: 398.59  E-value: 3.13e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  362 YSRDQIYVYVGDILIALNPFQSLGlystKHSKLYIGSKRTAS-----PPHIFAMADLGYQSMITYNSDQCIVISGESGAG 436
Cdd:cd14876    11 YLKNQIYTTADPLLVAINPFKDLG----NATDEWIRKYRDAPdltklPPHVFYTARRALENLHGVNKSQTIIVSGESGAG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  437 KTENAHLLVQQLTVLGKAN-NRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLLEKSR 515
Cdd:cd14876    87 KTEATKQIMRYFASAKSGNmDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVAFLLEKSR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  516 VIHQAIGEKNFHIFYYIYAGLAEKKKlAHYKLPENKPPRYLqNDHLRTVQDIMNnsfyKSQYELIEQCFKVIGFTMEQLG 595
Cdd:cd14876   167 IVTQDDNERSYHIFYQLLKGADSEMK-SKYHLLGLKEYKFL-NPKCLDVPGIDD----VADFEEVLESLKSMGLTEEQID 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  596 SIYSILAAILNVGNIEFSSVATEHQIDKSHISNHT--ALENCASLLCIRADELQEALTSHCVVTRGETIIRPNTVEKATD 673
Cdd:cd14876   241 TVFSIVSGVLLLGNVKITGKTEQGVDDAAAISNESleVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDDAEM 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  674 VRDAMAKTLYGRLFSWIVNCINSLLKhdssPSGNGDELsIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVFAWE 753
Cdd:cd14876   321 LKLSLAKAMYDKLFLWIIRNLNSTIE----PPGGFKNF-MGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERE 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  754 QNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNLKSQYFWRPKRM--ELSFGIHH 831
Cdd:cd14876   396 SKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVdsNINFIVVH 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  832 YAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNhpltktgNLPHSKTKnvinyqmrtseklinLAKGdtgea 911
Cdd:cd14876   476 TIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFE-------GVVVEKGK---------------IAKG----- 528
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  912 trharettnmktQTVASYFRY---SLMDLLSKMvvgQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGF 988
Cdd:cd14876   529 ------------SLIGSQFLKqleSLMGLINST---EPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGY 593
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767960106  989 SHRILFANFIKRYYLLCYKSSEEPRMSPDT-CATILEKAGL--DNWALGKTKVFLK 1041
Cdd:cd14876   594 SYRRPFEEFLYQFKFLDLGIANDKSLDPKVaALKLLESSGLseDEYAIGKTMVFLK 649
MYSc_Myh3 cd14913
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...
358-1041 2.11e-121

class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276878 [Multi-domain]  Cd Length: 668  Bit Score: 396.73  E-value: 2.11e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  358 LEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGK 437
Cdd:cd14913     7 LKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  438 TENAHLLVQQLTVLGKANNR----------TLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQIS 507
Cdd:cd14913    87 TVNTKRVIQYFATIAATGDLakkkdskmkgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIE 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  508 EYLLEKSRVIHQAIGEKNFHIFYYIYAGlaEKKKLAHYKLPENKPprylqNDHLRTVQDIMNNSFYKSQYELI--EQCFK 585
Cdd:cd14913   167 TYLLEKSRVTFQLKAERSYHIFYQILSN--KKPELIELLLITTNP-----YDYPFISQGEILVASIDDAEELLatDSAID 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  586 VIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQI--DKSHISNHTALencasLLCIRADELQEALTSHCVVTRGETII 663
Cdd:cd14913   240 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAepDGTEVADKTAY-----LMGLNSSDLLKALCFPRVKVGNEYVT 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  664 RPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLkhDSS-PSgngdELSIGILDIFGFENFKKNSFEQLCINIANEQIQ 742
Cdd:cd14913   315 KGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQL--DTKlPR----QHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQ 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  743 YYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEK-FEGNL-KSQYFWRP 820
Cdd:cd14913   389 QFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKlYDQHLgKSNNFQKP 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  821 K----RMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLvnhpltktgnlphsktknvinyqmrt 896
Cdd:cd14913   469 KvvkgRAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHL-------------------------- 522
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  897 sekLINLAKGDTGEATRHARETTNMKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTG 976
Cdd:cd14913   523 ---YATFATADADSGKKKVAKKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNG 599
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767960106  977 ILETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRM--SPDTCATILEKAGLDN--WALGKTKVFLK 1041
Cdd:cd14913   600 VLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFidSKKACEKLLASIDIDHtqYKFGHTKVFFK 668
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
353-1041 3.90e-121

class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276895 [Multi-domain]  Cd Length: 676  Bit Score: 396.32  E-value: 3.90e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  353 TVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGE 432
Cdd:cd14932     2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  433 SGAGKTENAHLLVQQLTVLGKA------------NNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGA 500
Cdd:cd14932    82 SGAGKTENTKKVIQYLAYVASSfktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  501 VVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGLAEKKKlAHYKLPENKPPRYLQNDHLrTVQDIMNNSFYKSQYEli 580
Cdd:cd14932   162 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLR-SELCLEDYSKYRFLSNGNV-TIPGQQDKELFAETME-- 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  581 eqCFKVIGFTMEQLGSIYSILAAILNVGNIEFSSvatEHQIDKSHISNHTALENCASLLCIRADELQEALTSHCVVTRGE 660
Cdd:cd14932   238 --AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKK---ERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRD 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  661 TIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGNgdelSIGILDIFGFENFKKNSFEQLCINIANEQ 740
Cdd:cd14932   313 YVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGAS----FIGILDIAGFEIFELNSFEQLCINYTNEK 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  741 IQYYYNQHVFAWEQNEYLNEDVDARVIEYE-DNWPLLDMFLQK--PMGLLSLLDEESRFPKATDQTLVEKFEGNLKSQ-Y 816
Cdd:cd14932   389 LQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQEQGNNpK 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  817 FWRPKRM--ELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLvnhpltktgnlphsktknvinyqM 894
Cdd:cd14932   469 FQKPKKLkdDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSEL-----------------------W 525
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  895 RTSEKLINLAK-GDTGEATRHARETTNMKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLR 973
Cdd:cd14932   526 KDVDRIVGLDKvAGMGESLHGAFKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLR 605
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767960106  974 YTGILETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRMS-PDTCATILEKAGLDN--WALGKTKVFLK 1041
Cdd:cd14932   606 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDgKQACVLMVKALELDPnlYRIGQSKVFFR 676
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
358-1030 2.96e-119

class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276871 [Multi-domain]  Cd Length: 715  Bit Score: 392.42  E-value: 2.96e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  358 LEKCYSRDQIYVYVGDILIALNPFQSLG-LYSTKHSKLYIGSKRTASP-PHIFAMADLGYQSMITYNSDQCIVISGESGA 435
Cdd:cd14906     7 LGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQNKSPiPHIYAVALRAYQSMVSEKKNQSIIISGESGS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  436 GKTENAHLLVQQLTVLGKA----------NNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKF-TSSGAVVGA 504
Cdd:cd14906    87 GKTEASKTILQYLINTSSSnqqqnnnnnnNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFrSSDGKIDGA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  505 QISEYLLEKSRVIHQA-IGEKNFHIFYYIYAGlAEKKKLAHYKLpENKPPRYLQNDHLRTVQDIMNNSFYKSQ------- 576
Cdd:cd14906   167 SIETYLLEKSRISHRPdNINLSYHIFYYLVYG-ASKDERSKWGL-NNDPSKYRYLDARDDVISSFKSQSSNKNsnhnnkt 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  577 -----YELIEQCFKVIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQIDKSHISNHTALENCASLLCIRADELQEALT 651
Cdd:cd14906   245 esiesFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLESVSKLLGYIESVFKQALL 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  652 SHCVVT--RGETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGNG------DELSIGILDIFGFEN 723
Cdd:cd14906   325 NRNLKAggRGSVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSNDLAggsnkkNNLFIGVLDIFGFEN 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  724 FKKNSFEQLCINIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQT 803
Cdd:cd14906   405 LSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKSDGILSLLDDECIMPKGSEQS 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  804 LVEKFEGNLKS--QYFWRpKRMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNHPLTKTGNl 881
Cdd:cd14906   485 LLEKYNKQYHNtnQYYQR-TLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQITSTTN- 562
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  882 phsktknvinyqmrtseklinlakgdtgeatrhareTTNMKTQ--TVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQ 959
Cdd:cd14906   563 ------------------------------------TTKKQTQsnTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMD 606
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767960106  960 ARKYDKEKVLLQLRYTGILETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRMSPdTCATILEKAGLDN 1030
Cdd:cd14906   607 CNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNP-KLASQLILQNIQS 676
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
362-1041 3.70e-117

class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276873 [Multi-domain]  Cd Length: 682  Bit Score: 385.42  E-value: 3.70e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  362 YSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLY-----IGSKRTASP----PHIFAMADLGYQSMIT-YNSDQCIVISG 431
Cdd:cd14908    11 FFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYrqeglLRSQGIESPqalgPHVFAIADRSYRQMMSeIRASQSILISG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  432 ESGAGKTENAHLLVQQLTVLGKANNR-----------TLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGA 500
Cdd:cd14908    91 ESGAGKTESTKIVMLYLTTLGNGEEGapnegeelgklSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKFIELGFNRAGN 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  501 VVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGLAEKKKlAHYKLPENKP-----PRYL----QND--HLRTVQDimn 569
Cdd:cd14908   171 LLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEH-EKYEFHDGITgglqlPNEFhytgQGGapDLREFTD--- 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  570 nsfyKSQYELIEQCFKVIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQIDKSHISNHTALENCASLLCIRADELQEA 649
Cdd:cd14908   247 ----EDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARVAKLLGVDVDKLLRA 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  650 LTSHCVVTRGETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDsspsgNGDEL--SIGILDIFGFENFKKN 727
Cdd:cd14908   323 LTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWE-----NDKDIrsSVGVLDIFGFECFAHN 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  728 SFEQLCINIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFP-KATDQTLVE 806
Cdd:cd14908   398 SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAKKKGILTMLDDECRLGiRGSDANYAS 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  807 KFEGNL---KSQYFWRPKRME--------LSFGIHHYAGKVLYNA-SGFLAKNRDTLPtdivlllrssdnsvirqlvnhp 874
Cdd:cd14908   478 RLYETYlpeKNQTHSENTRFEatsiqktkLIFAVRHFAGQVQYTVeTTFCEKNKDEIP---------------------- 535
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  875 ltktgnlphsktknvinyqmRTSEKLInlakgdtgeatrhaRETTNMKTQTvasyfrYSLMDLLSKMvvgQPHFVRCIKP 954
Cdd:cd14908   536 --------------------LTADSLF--------------ESGQQFKAQL------HSLIEMIEDT---DPHYIRCIKP 572
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  955 NSERQARKYDKEKVLLQLRYTGILETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPR-MSPD------TCATILEKAG 1027
Cdd:cd14908   573 NDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPLIPEVVLsWSMErldpqkLCVKKMCKDL 652
                         730       740       750
                  ....*....|....*....|....*....|
gi 767960106 1028 L----------------DNWALGKTKVFLK 1041
Cdd:cd14908   653 VkgvlspamvsmknipeDTMQLGKSKVFMR 682
MYSc_Myh16 cd14934
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...
353-1041 3.15e-116

class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.


Pssm-ID: 276896 [Multi-domain]  Cd Length: 659  Bit Score: 382.07  E-value: 3.15e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  353 TVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGE 432
Cdd:cd14934     2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  433 SGAGKTENAHLLVQQLTVLGKANNR------TLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQI 506
Cdd:cd14934    82 SGAGKTENTKKVIQYFANIGGTGKQssdgkgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGADI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  507 SEYLLEKSRVIHQAIGEKNFHIFYYIYAGlaEKKKLAHYKLPENKPPRYLQNDHLRTVQDIMNNSfykSQYELIEQCFKV 586
Cdd:cd14934   162 ESYLLEKSRVISQQAAERGYHIFYQILSN--KKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDG---EELQITDVAFDV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  587 IGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQIDkshISNHTALENCASLLCIRADELQEALTSHCVVTRGETIIRPN 666
Cdd:cd14934   237 LGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAE---VDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQ 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  667 TVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSpsgngDELSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYN 746
Cdd:cd14934   314 NMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQ-----RQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFN 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  747 QHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNL--KSQYFWRP---- 820
Cdd:cd14934   389 HHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHlgKSSNFLKPkggk 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  821 -KRMELSFGIHHYAGKVLYNASGFLAKNRDtlptdivlllrssdnsvirqlvnhPLTKTgnlphsktknVINYQMRTSEK 899
Cdd:cd14934   469 gKGPEAHFELVHYAGTVGYNITGWLEKNKD------------------------PLNET----------VVGLFQKSSLG 514
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  900 LINLAKGDTGEATRHARETTNMKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILE 979
Cdd:cd14934   515 LLALLFKEEEAPAGSKKQKRGSSFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLE 594
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767960106  980 TARIRRLGFSHRILFANFIKRYYLLcyksseEPRMSPD-------TCATILEKAGLD--NWALGKTKVFLK 1041
Cdd:cd14934   595 GIRICRKGFPNRLQYPEFKQRYQVL------NPNVIPQgfvdnkkASELLLGSIDLDvnEYKIGHTKVFFR 659
MYSc_Myh9 cd14919
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...
353-1041 5.05e-116

class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276883 [Multi-domain]  Cd Length: 670  Bit Score: 382.13  E-value: 5.05e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  353 TVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGE 432
Cdd:cd14919     2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  433 SGAGKTENAHLLVQQLTVLG-----KANNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQIS 507
Cdd:cd14919    82 SGAGKTENTKKVIQYLAHVAsshksKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  508 EYLLEKSRVIHQAIGEKNFHIFYYIYAGLAEKKKLAHYKLPENKpPRYLQNDHLrTVQDIMNNSFYKSQYELIeqcfKVI 587
Cdd:cd14919   162 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNK-YRFLSNGHV-TIPGQQDKDMFQETMEAM----RIM 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  588 GFTMEQLGSIYSILAAILNVGNIEFSSvatEHQIDKSHISNHTALENCASLLCIRADELQEALTSHCVVTRGETIIRPNT 667
Cdd:cd14919   236 GIPEEEQMGLLRVISGVLQLGNIVFKK---ERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  668 VEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGNgdelSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQ 747
Cdd:cd14919   313 KEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAS----FIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNH 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  748 HVFAWEQNEYLNEDVDARVIEYE-DNWPLLDMFLQK--PMGLLSLLDEESRFPKATDQTLVEK-FEGNLKSQYFWRPKRM 823
Cdd:cd14919   389 TMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKvVQEQGTHPKFQKPKQL 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  824 --ELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLvnhpltktgnlphsktknvinyqMRTSEKLI 901
Cdd:cd14919   469 kdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSEL-----------------------WKDVDRII 525
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  902 NLAK--GDTGEATRHARETTNMKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILE 979
Cdd:cd14919   526 GLDQvaGMSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLE 605
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  980 TARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRMS-PDTCATILEKAGLDN--WALGKTKVFLK 1041
Cdd:cd14919   606 GIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDgKQACVLMIKALELDSnlYRIGQSKVFFR 670
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
353-1041 1.72e-114

class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276885 [Multi-domain]  Cd Length: 673  Bit Score: 377.82  E-value: 1.72e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  353 TVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGE 432
Cdd:cd14921     2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  433 SGAGKTENAHLLVQQLTVL-----GKANNRT---LQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGA 504
Cdd:cd14921    82 SGAGKTENTKKVIQYLAVVasshkGKKDTSItgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  505 QISEYLLEKSRVIHQAIGEKNFHIFYYIYAGLAEKKKlAHYKLPENKPPRYLQNDHLrTVQDIMNNSFYKSQYELIeqcf 584
Cdd:cd14921   162 NIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMR-SDLLLEGFNNYTFLSNGFV-PIPAAQDDEMFQETLEAM---- 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  585 KVIGFTMEQLGSIYSILAAILNVGNIEFSSvatEHQIDKSHISNHTALENCASLLCIRADELQEALTSHCVVTRGETIIR 664
Cdd:cd14921   236 SIMGFSEEEQLSILKVVSSVLQLGNIVFKK---ERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  665 PNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGNgdelSIGILDIFGFENFKKNSFEQLCINIANEQIQYY 744
Cdd:cd14921   313 AQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGAS----FLGILDIAGFEIFEVNSFEQLCINYTNEKLQQL 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  745 YNQHVFAWEQNEYLNEDVDARVIEYE-DNWPLLDMFLQ--KPMGLLSLLDEESRFPKATDQTLVEKF---EGNlkSQYFW 818
Cdd:cd14921   389 FNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLcteQGN--HPKFQ 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  819 RPKRM--ELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNHPLTKTGnlphsktknvinyqmrt 896
Cdd:cd14921   467 KPKQLkdKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVG----------------- 529
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  897 sekLINLAKGdTGEATRHARETTNMKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTG 976
Cdd:cd14921   530 ---LDQMAKM-TESSLPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNG 605
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767960106  977 ILETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRMS-PDTCATILEKAGLDN--WALGKTKVFLK 1041
Cdd:cd14921   606 VLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDgKQACILMIKALELDPnlYRIGQSKIFFR 673
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
354-1041 1.79e-113

class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276842 [Multi-domain]  Cd Length: 664  Bit Score: 374.53  E-value: 1.79e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  354 VSEQLEKCYsrdQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTAS-PPHIFAMADLGYQSMITYN-SDQCIVISG 431
Cdd:cd14875     7 IKERFEKLH---QQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFNAIFVQGlGNQSVVISG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  432 ESGAGKTENAHLLVQQLTVL-----GKANNRTLQEKILQ----VNNLVEAFGNACTIINDNSSRFGKYLEMKF-TSSGAV 501
Cdd:cd14875    84 ESGSGKTENAKMLIAYLGQLsymhsSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFdPTSGVM 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  502 VGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGLA--EKKKLAHYKLPENKPPRYLQNDHLRTVQD--IMNNSfykSQY 577
Cdd:cd14875   164 VGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSpeEKKELGGLKTAQDYKCLNGGNTFVRRGVDgkTLDDA---HEF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  578 ELIEQCFKVIGFTMEQLGSIYSILAAILNVGNIEFssvaTEHQIDKSHISNHTALENCASLLCIRADELQEaltshCVVT 657
Cdd:cd14875   241 QNVRHALSMIGVELETQNSIFRVLASILHLMEVEF----ESDQNDKAQIADETPFLTACRLLQLDPAKLRE-----CFLV 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  658 RGET---IIRPNTVEkATDVRDAMAKTLYGRLFSWIVNCINSLLkhdsSPSGNGDELS-IGILDIFGFENFKKNSFEQLC 733
Cdd:cd14875   312 KSKTslvTILANKTE-AEGFRNAFCKAIYVGLFDRLVEFVNASI----TPQGDCSGCKyIGLLDIFGFENFTRNSFEQLC 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  734 INIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATdqtlVEKFEGNL- 812
Cdd:cd14875   387 INYANESLQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKRTGIFSMLDEECNFKGGT----TERFTTNLw 462
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  813 -----KSQYFWRPKR-MELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVnhpltktgnlphskt 886
Cdd:cd14875   463 dqwanKSPYFVLPKStIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLL--------------- 527
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  887 knvinyqmrTSEKLINLAKgdtgeatrharettnmktQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKE 966
Cdd:cd14875   528 ---------STEKGLARRK------------------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNL 580
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  967 KVLLQLRYTGILETARIRRLGFSHRILFANFIKRYYLLCYKSS----EEPRMSpDTCATILE------KAGLDNWALGKT 1036
Cdd:cd14875   581 LVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTaslfKQEKYS-EAAKDFLAyyqrlyGWAKPNYAVGKT 659

                  ....*
gi 767960106 1037 KVFLK 1041
Cdd:cd14875   660 KVFLR 664
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
362-1042 5.75e-113

class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276845 [Multi-domain]  Cd Length: 647  Bit Score: 372.65  E-value: 5.75e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  362 YSRDQIYVYVGD-ILIALNPFQSLGLYSTKHSKLY-------IGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGES 433
Cdd:cd14879    14 FRSDLPYTRLGSsALVAVNPYKYLSSNSDASLGEYgseyydtTSGSKEPLPPHAYDLAARAYLRMRRRSEDQAVVFLGET 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  434 GAGKTENAHLLVQQLTVLGKANNRT--LQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLL 511
Cdd:cd14879    94 GSGKSESRRLLLRQLLRLSSHSKKGtkLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNERGRLIGAKVLDYRL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  512 EKSRVIHQAIGEKNFHIFYYIYAGL--AEKkklAHYKLpENKP-----PRYLQ---------NDHLRtvqdimnnsfyks 575
Cdd:cd14879   174 ERSRVASVPTGERNFHVFYYLLAGAspEER---QHLGL-DDPSdyallASYGChplplgpgsDDAEG------------- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  576 qYELIEQCFKVIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQiDKSHISNHTALENCASLLCIRADELQEALTSHCV 655
Cdd:cd14879   237 -FQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHEGGE-ESAVVKNTDVLDIVAAFLGVSPEDLETSLTYKTK 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  656 VTRGE--TIIRpnTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGNgdelSIGILDIFGFENF---KKNSFE 730
Cdd:cd14879   315 LVRKElcTVFL--DPEGAAAQRDELARTLYSLLFAWVVETINQKLCAPEDDFAT----FISLLDFPGFQNRsstGGNSLD 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  731 QLCINIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEE-SRFPKATDQTLVE--- 806
Cdd:cd14879   389 QFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGGLLGILDDQtRRMPKKTDEQMLEalr 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  807 -KFEGN---LKSQYFWRPKRMElSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSdnsvirqlvnhpltktgnlp 882
Cdd:cd14879   469 kRFGNHssfIAVGNFATRSGSA-SFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLLRGA-------------------- 527
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  883 hsktknvinyqmrtseklinlakgdtgeatrharettnmkTQtvasyFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARK 962
Cdd:cd14879   528 ----------------------------------------TQ-----LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNS 562
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  963 YDKEKVLLQLRYTGILETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRmspDTCATILEKAGLDNWALGKTKVFLKY 1042
Cdd:cd14879   563 FDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLRGSAAERI---RQCARANGWWEGRDYVLGNTKVFLSY 639
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
17-287 7.05e-113

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 357.35  E-value: 7.05e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   17 PSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILdPIHDIDEEIEAEYNILKAlSDHPNVVRFYGIYFKKDKvngdkL 96
Cdd:cd06612     1 PEEVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVV-PVEEDLQEIIKEISILKQ-CDSPYIVKYYGSYFKNTD-----L 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLVKgflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:cd06612    74 WIVMEYCGAGSVSDIMK---ITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRHRRNTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQPELW 256
Cdd:cd06612   151 DTMAKRNTVIGTPFWMAPEVI-----QEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPNKPPPTLSDPEKW 225
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767960106  257 SAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06612   226 SPEFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
353-1040 7.12e-113

class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276846 [Multi-domain]  Cd Length: 658  Bit Score: 372.65  E-value: 7.12e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  353 TVSEQLEKCYSRDQIYVYVGDILIALNPFQSLG-LYSTKHSKLYIGSKRTAS-PPHIFAMADLGY---QSMITyNSDQCI 427
Cdd:cd14880     2 TVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQKlKPHIFTVGEQTYrnvKSLIE-PVNQSI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  428 VISGESGAGKTENAHLLVQQLTVLGKA-----NNRT---LQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSG 499
Cdd:cd14880    81 VVSGESGAGKTWTSRCLMKFYAVVAASptsweSHKIaerIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  500 AVVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGLAEKKKLaHYKLPENKPPRYLQNdhlrtvqdimnnsfykSQYEL 579
Cdd:cd14880   161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERL-QWHLPEGAAFSWLPN----------------PERNL 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  580 IEQCFKVIGFTMEQLG-------SIYSILAAILNVGNIEFSSVATEHQ----IDKSHISNHTAlencASLLCIRADELQE 648
Cdd:cd14880   224 EEDCFEVTREAMLHLGidtptqnNIFKVLAGLLHLGNIQFADSEDEAQpcqpMDDTKESVRTS----ALLLKLPEDHLLE 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  649 ALTSHCVVT-RGETIIR-PNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGNgdelSIGILDIFGFENFKK 726
Cdd:cd14880   300 TLQIRTIRAgKQQQVFKkPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTT----FIGLLDVYGFESFPE 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  727 NSFEQLCINIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATD----Q 802
Cdd:cd14880   376 NSLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSPISICSLINEECRLNRPSSaaqlQ 455
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  803 TLVEKFEGNlkSQYFWRPK-RMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVnhPLTktgnl 881
Cdd:cd14880   456 TRIESALAG--NPCLGHNKlSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLF--PAN----- 526
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  882 PHSKTKNVINYQMRTSeklinlakgdtgeatrharettnmkTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQAR 961
Cdd:cd14880   527 PEEKTQEEPSGQSRAP-------------------------VLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQ 581
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767960106  962 KYDKEKVLLQLRYTGILETARIRRLGFSHRILFANFIKRYYLLcykSSEEPRMSPDTCATILEKAGLDNWALGKTKVFL 1040
Cdd:cd14880   582 TFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLL---RRLRPHTSSGPHSPYPAKGLSEPVHCGRTKVFM 657
MYSc_Myo25 cd14886
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...
354-1041 1.45e-112

class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276851  Cd Length: 650  Bit Score: 371.53  E-value: 1.45e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  354 VSEQLEKCYSRDQIYVYVGDILIALNPFQSL-GLYSTKHSKLYIGSKRTAS-----PPHIFAMADLGYQSMITYNSDQCI 427
Cdd:cd14886     3 VIDILRDRFAKDKIYTYAGKLLVALNPFKQIrNLYGTEVIGRYRQADTSRGfpsdlPPHSYAVAQSALNGLISDGISQSC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  428 VISGESGAGKTENAHLLVQQLTVLGKANNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQIS 507
Cdd:cd14886    83 IVSGESGAGKTETAKQLMNFFAYGHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGKIT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  508 EYLLEKSRVIHQAIGEKNFHIFYYIYAGLA--EKKKLAHYKLpenKPPRYLQNDHLRT---VQDIMNNSFYKSQYELIeq 582
Cdd:cd14886   163 SYMLELSRIEFQSTNERNYHIFYQCIKGLSpeEKKSLGFKSL---ESYNFLNASKCYDapgIDDQKEFAPVRSQLEKL-- 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  583 cfkvigFTMEQLGSIYSILAAILNVGNIEFSSVATEHQIDKSHISNHTALENCASLLCIRADELQEALTSHCVVTRGETI 662
Cdd:cd14886   238 ------FSKNEIDSFYKCISGILLAGNIEFSEEGDMGVINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETI 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  663 IRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGngdelSIGILDIFGFENFKKNSFEQLCINIANEQIQ 742
Cdd:cd14886   312 ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARP-----WIGILDIYGFEFFERNTYEQLLINYANERLQ 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  743 YYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNLKSQYFWRPKR 822
Cdd:cd14886   387 QYFINQVFKSEIQEYEIEGIDHSMITFTDNSNVLAVFDKPNLSIFSFLEEQCLIQTGSSEKFTSSCKSKIKNNSFIPGKG 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  823 MELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQlvnhpltktgnlphsktknvinyqmrTSEKLIN 902
Cdd:cd14886   467 SQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNK--------------------------AFSDIPN 520
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  903 lakgdtgeatrharETTNMKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETAR 982
Cdd:cd14886   521 --------------EDGNMKGKFLGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQ 586
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767960106  983 IRRLGFSHRILFANFIKRYYLLCYKSSEEPRMSPDTCAT---ILEKAGLD--NWALGKTKVFLK 1041
Cdd:cd14886   587 TIHRGFAYNDTFEEFFHRNKILISHNSSSQNAGEDLVEAvksILENLGIPcsDYRIGKTKVFLR 650
MYSc_Myh7 cd14917
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...
358-1041 2.94e-112

class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276881 [Multi-domain]  Cd Length: 668  Bit Score: 371.36  E-value: 2.94e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  358 LEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGK 437
Cdd:cd14917     7 LKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  438 TENAHLLVQQLTVLGKANNR----------TLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQIS 507
Cdd:cd14917    87 TVNTKRVIQYFAVIAAIGDRskkdqtpgkgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIE 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  508 EYLLEKSRVIHQAIGEKNFHIFYYIYAGlaEKKKLAHYKLPENKPPRYLQNDHLRTVQDIMNNSfykSQYELIEQCFKVI 587
Cdd:cd14917   167 TYLLEKSRVIFQLKAERDYHIFYQILSN--KKPELLDMLLITNNPYDYAFISQGETTVASIDDA---EELMATDNAFDVL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  588 GFTMEQLGSIYSILAAILNVGNIEFSSVATEHQIDKSHISNhtaLENCASLLCIRADELQEALTSHCVVTRGETIIRPNT 667
Cdd:cd14917   242 GFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEE---ADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  668 VEKATDVRDAMAKTLYGRLFSWIVNCINSLLKhdsspSGNGDELSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQ 747
Cdd:cd14917   319 VQQVIYATGALAKAVYEKMFNWMVTRINATLE-----TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNH 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  748 HVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEK-FEGNL-KSQYFWRPKRM-- 823
Cdd:cd14917   394 HMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKlFDNHLgKSNNFQKPRNIkg 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  824 --ELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLvnhpltktgnlphsktknvinyqmrtsekLI 901
Cdd:cd14917   474 kpEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNL-----------------------------FA 524
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  902 NLAKGDTGEATRHARETTNMKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETA 981
Cdd:cd14917   525 NYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGI 604
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767960106  982 RIRRLGFSHRILFANFIKRYYLLCYKSSEEPRM--SPDTCATILEKAGLDN--WALGKTKVFLK 1041
Cdd:cd14917   605 RICRKGFPNRILYGDFRQRYRILNPAAIPEGQFidSRKGAEKLLSSLDIDHnqYKFGHTKVFFK 668
MYSc_Myh2_mammals cd14912
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
358-1041 8.55e-112

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276877 [Multi-domain]  Cd Length: 673  Bit Score: 370.22  E-value: 8.55e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  358 LEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGK 437
Cdd:cd14912     7 LKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  438 TENAHLLVQQLTVLGKANNR------------TLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQ 505
Cdd:cd14912    87 TVNTKRVIQYFATIAVTGEKkkeeitsgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASAD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  506 ISEYLLEKSRVIHQAIGEKNFHIFYYIYAGlaEKKKLAHYKLPENKPprylqNDHLRTVQDIMNNSFYKSQYELI--EQC 583
Cdd:cd14912   167 IETYLLEKSRVTFQLKAERSYHIFYQITSN--KKPELIEMLLITTNP-----YDYPFVSQGEISVASIDDQEELMatDSA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  584 FKVIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQIDKSHISnhtALENCASLLCIRADELQEALTSHCVVTRGETII 663
Cdd:cd14912   240 IDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTE---VADKAAYLQSLNSADLLKALCYPRVKVGNEYVT 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  664 RPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKhdsspSGNGDELSIGILDIFGFENFKKNSFEQLCINIANEQIQY 743
Cdd:cd14912   317 KGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-----TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQ 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  744 YYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEK-FEGNL-KSQYFWRPK 821
Cdd:cd14912   392 FFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKlYEQHLgKSANFQKPK 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  822 ----RMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNHPLTKTGnlphsktknvinyqmrts 897
Cdd:cd14912   472 vvkgKAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEG------------------ 533
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  898 eklinlaKGDTGEATRHARETTNmKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGI 977
Cdd:cd14912   534 -------ASAGGGAKKGGKKKGS-SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGV 605
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767960106  978 LETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRM--SPDTCATILEKAGLDN--WALGKTKVFLK 1041
Cdd:cd14912   606 LEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFidSKKASEKLLASIDIDHtqYKFGHTKVFFK 673
MYSc_Myh14_mammals cd14930
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...
353-1041 2.60e-111

class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.


Pssm-ID: 276893 [Multi-domain]  Cd Length: 670  Bit Score: 369.04  E-value: 2.60e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  353 TVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGE 432
Cdd:cd14930     2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  433 SGAGKTENAHLLVQQLT-VLGKANNRT-------LQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGA 504
Cdd:cd14930    82 SGAGKTENTKKVIQYLAhVASSPKGRKepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  505 QISEYLLEKSRVIHQAIGEKNFHIFYYIYAGLAEKKK-------LAHYKLPENKPprylqndhlrtvqdimnNSFYKSQY 577
Cdd:cd14930   162 NIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKadlllepCSHYRFLTNGP-----------------SSSPGQER 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  578 ELIEQCF---KVIGFTMEQLGSIYSILAAILNVGNIefsSVATEHQIDKSHISNHTALENCASLLCIRADELQEALTSHC 654
Cdd:cd14930   225 ELFQETLeslRVLGFSHEEITSMLRMVSAVLQFGNI---VLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPR 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  655 VVTRGETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLkhDSSPSGNGDELsiGILDIFGFENFKKNSFEQLCI 734
Cdd:cd14930   302 IKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSPRQGASFL--GILDIAGFEIFQLNSFEQLCI 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  735 NIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYE-DNWPLLDMFLQ--KPMGLLSLLDEESRFPKATDQTLVEKFEGN 811
Cdd:cd14930   378 NYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQE 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  812 LKSQ-YFWRPK--RMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLvnhpltktgnlpHSKTKN 888
Cdd:cd14930   458 QGGHpKFQRPRhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEI------------WKDVEG 525
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  889 VINYqmrtsEKLINLAKGDTGEATRHARettnmkTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKV 968
Cdd:cd14930   526 IVGL-----EQVSSLGDGPPGGRPRRGM------FRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLV 594
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767960106  969 LLQLRYTGILETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRMS-PDTCATILEKAGLDN--WALGKTKVFLK 1041
Cdd:cd14930   595 LDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDgKQACEKMIQALELDPnlYRVGQSKIFFR 670
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
21-287 4.03e-111

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 352.76  E-value: 4.03e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKI--LDPIHDIdEEIEAEYNILKAlSDHPNVVRFYGIYFKkdkvnGDKLWL 98
Cdd:cd06613     2 YELIQRIGSGTYGDVYKARNIATGELAAVKVikLEPGDDF-EIIQQEISMLKE-CRHPNIVAYFGSYLR-----RDKLWI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   99 VLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST 178
Cdd:cd06613    75 VMEYCGGGSLQDI----YQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTAT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  179 RHRRNTSVGTPFWMAPEVIACEQQldTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPR--NPPPKLRQPELW 256
Cdd:cd06613   151 IAKRKSFIGTPYWMAPEVAAVERK--GGYDGKCDIWALGITAIELAELQPPMFDLHPMRALFLIPKsnFDPPKLKDKEKW 228
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767960106  257 SAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06613   229 SPDFHDFIKKCLTKNPKKRPTATKLLQHPFV 259
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
353-1041 6.00e-111

class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276899 [Multi-domain]  Cd Length: 675  Bit Score: 367.85  E-value: 6.00e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  353 TVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGE 432
Cdd:cd15896     2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  433 SGAGKTENAHLLVQQLTVLGKANNRT------------LQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGA 500
Cdd:cd15896    82 SGAGKTENTKKVIQYLAHVASSHKTKkdqnslalshgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  501 VVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGLAEKKKlAHYKLPENKPPRYLQNDHLrTVQDIMNNSFYKSQYEli 580
Cdd:cd15896   162 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLR-SELLLENYNNYRFLSNGNV-TIPGQQDKDLFTETME-- 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  581 eqCFKVIGFTMEQLGSIYSILAAILNVGNIEFSSvatEHQIDKSHISNHTALENCASLLCIRADELQEALTSHCVVTRGE 660
Cdd:cd15896   238 --AFRIMGIPEDEQIGMLKVVASVLQLGNMSFKK---ERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRD 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  661 TIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGNgdelSIGILDIFGFENFKKNSFEQLCINIANEQ 740
Cdd:cd15896   313 YVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGAS----FIGILDIAGFEIFELNSFEQLCINYTNEK 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  741 IQYYYNQHVFAWEQNEYLNEDVDARVIEYE-DNWPLLDMFLQ--KPMGLLSLLDEESRFPKATDQTLVEK-FEGNLKSQY 816
Cdd:cd15896   389 LQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIEKpaSPPGILALLDEECWFPKATDKSFVEKvLQEQGTHPK 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  817 FWRPKRM--ELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLvnhpltktgnlphsktknvinyqM 894
Cdd:cd15896   469 FFKPKKLkdEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSEL-----------------------W 525
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  895 RTSEKLINLAKGDTGEATRHARETTNMKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRY 974
Cdd:cd15896   526 KDVDRIVGLDKVSGMSEMPGAFKTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRC 605
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  975 TGILETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRMS-PDTCATILEKAGLDN--WALGKTKVFLK 1041
Cdd:cd15896   606 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDgKQACVLMIKSLELDPnlYRIGQSKVFFR 675
MYSc_Myh1_mammals cd14910
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
358-1041 5.73e-110

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276875 [Multi-domain]  Cd Length: 671  Bit Score: 365.21  E-value: 5.73e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  358 LEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGK 437
Cdd:cd14910     7 LKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  438 TENAHLLVQQLTVLGKANNR------------TLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQ 505
Cdd:cd14910    87 TVNTKRVIQYFATIAVTGEKkkeeatsgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASAD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  506 ISEYLLEKSRVIHQAIGEKNFHIFYYIYAGlaEKKKLAHYKLPENKPprylqNDHLRTVQDIMNNSFYKSQYELI--EQC 583
Cdd:cd14910   167 IETYLLEKSRVTFQLKAERSYHIFYQIMSN--KKPDLIEMLLITTNP-----YDYAFVSQGEITVPSIDDQEELMatDSA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  584 FKVIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQIDKSHISnhtALENCASLLCIRADELQEALTSHCVVTRGETII 663
Cdd:cd14910   240 IEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTE---VADKAAYLQNLNSADLLKALCYPRVKVGNEYVT 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  664 RPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKhdsspSGNGDELSIGILDIFGFENFKKNSFEQLCINIANEQIQY 743
Cdd:cd14910   317 KGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-----TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQ 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  744 YYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEK-FEGNL-KSQYFWRPK 821
Cdd:cd14910   392 FFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKlYEQHLgKSNNFQKPK 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  822 ----RMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSdnsvirqlvnhpltktgnlphsktknvinyQMRTS 897
Cdd:cd14910   472 pakgKVEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKS------------------------------SMKTL 521
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  898 EKLINLAKGDTGEA--TRHARETTNMKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYT 975
Cdd:cd14910   522 ALLFSGAAAAEAEEggGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCN 601
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  976 GILETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRM--SPDTCATILEKAGLDN--WALGKTKVFLK 1041
Cdd:cd14910   602 GVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFidSKKASEKLLGSIDIDHtqYKFGHTKVFFK 671
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
21-287 1.56e-108

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 345.34  E-value: 1.56e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDP-IHDIDEEIEAEYNILKALsDHPNVVRFYGIYFKKDKvngdkLWLV 99
Cdd:cd05122     2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLeSKEKKESILNEIAILKKC-KHPNIVKYYGSYLKKDE-----LWIV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  100 LELCSGGSVTDLVKgflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTR 179
Cdd:cd05122    76 MEFCSGGSLKDLLK---NTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  180 hRRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQPELWSAE 259
Cdd:cd05122   153 -TRNTFVGTPYWMAPEVIQGKP-----YGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGPPGLRNPKKWSKE 226
                         250       260
                  ....*....|....*....|....*...
gi 767960106  260 FNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd05122   227 FKDFLKKCLQKDPEKRPTAEQLLKHPFI 254
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
358-1041 1.86e-108

class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276880 [Multi-domain]  Cd Length: 670  Bit Score: 360.91  E-value: 1.86e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  358 LEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGK 437
Cdd:cd14916     7 LKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  438 TENAHLLVQQLTVLG-----------KANNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQI 506
Cdd:cd14916    87 TVNTKRVIQYFASIAaigdrskkenpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADI 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  507 SEYLLEKSRVIHQAIGEKNFHIFYYIYAGlaEKKKLAHYKLPENKPprylqNDHLRTVQDIMNNSFYKSQYELI--EQCF 584
Cdd:cd14916   167 ETYLLEKSRVIFQLKAERNYHIFYQILSN--KKPELLDMLLVTNNP-----YDYAFVSQGEVSVASIDDSEELLatDSAF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  585 KVIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQIDKSHISNhtaLENCASLLCIRADELQEALTSHCVVTRGETIIR 664
Cdd:cd14916   240 DVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTED---ADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTK 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  665 PNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKhdsspSGNGDELSIGILDIFGFENFKKNSFEQLCINIANEQIQYY 744
Cdd:cd14916   317 GQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-----TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  745 YNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEK-FEGNL-KSQYFWRPK- 821
Cdd:cd14916   392 FNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKlYDNHLgKSNNFQKPRn 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  822 ---RMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNhpltktgnlphsktknvinyqmrtse 898
Cdd:cd14916   472 vkgKQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFS-------------------------- 525
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  899 kliNLAKGDTGEATR-HARETTNMKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGI 977
Cdd:cd14916   526 ---TYASADTGDSGKgKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGV 602
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767960106  978 LETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRM--SPDTCATILEKAGLDN--WALGKTKVFLK 1041
Cdd:cd14916   603 LEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFidSRKGAEKLLGSLDIDHnqYKFGHTKVFFK 670
MYSc_Myh8 cd14918
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...
358-1041 7.05e-108

class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276882 [Multi-domain]  Cd Length: 668  Bit Score: 359.05  E-value: 7.05e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  358 LEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGK 437
Cdd:cd14918     7 LKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  438 TENAHLLVQQLTVLGKANNR----------TLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQIS 507
Cdd:cd14918    87 TVNTKRVIQYFATIAVTGEKkkeesgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIE 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  508 EYLLEKSRVIHQAIGEKNFHIFYYIYAGlaEKKKLAHYKLPENKPprylqNDHLRTVQDIMNNSFYKSQYELI--EQCFK 585
Cdd:cd14918   167 TYLLEKSRVTFQLKAERSYHIFYQITSN--KKPDLIEMLLITTNP-----YDYAFVSQGEITVPSIDDQEELMatDSAID 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  586 VIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQIDKSHISnhtALENCASLLCIRADELQEALTSHCVVTRGETIIRP 665
Cdd:cd14918   240 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTE---VADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  666 NTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKhdsspSGNGDELSIGILDIFGFENFKKNSFEQLCINIANEQIQYYY 745
Cdd:cd14918   317 QTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-----TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  746 NQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEK-FEGNL-KSQYFWRPK-- 821
Cdd:cd14918   392 NHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKlYDQHLgKSANFQKPKvv 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  822 --RMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSdnsvirqlvnhpltktgnlphsktknvinyQMRTSEK 899
Cdd:cd14918   472 kgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKS------------------------------AMKTLAS 521
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  900 LIN-LAKGDTGEATRHARETTNMKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGIL 978
Cdd:cd14918   522 LFStYASAEADSGAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVL 601
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767960106  979 ETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRM--SPDTCATILEKAGLDN--WALGKTKVFLK 1041
Cdd:cd14918   602 EGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFidSKKASEKLLASIDIDHtqYKFGHTKVFFK 668
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
16-287 4.94e-107

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 342.37  E-value: 4.94e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVRFYGIYFKKDKV-NGD 94
Cdd:cd06636    13 DPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKYSHHRNIATYYGAFIKKSPPgHDD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 KLWLVLELCSGGSVTDLVKGflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:cd06636    93 QLWLVMEFCGAGSVTDLVKN--TKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LTSTRHRRNTSVGTPFWMAPEVIACEQQLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQPE 254
Cdd:cd06636   171 LDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPKLKSKK 250
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767960106  255 lWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06636   251 -WSKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
MYSc_Myh4 cd14915
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...
358-1041 8.52e-107

class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276879 [Multi-domain]  Cd Length: 671  Bit Score: 356.35  E-value: 8.52e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  358 LEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGK 437
Cdd:cd14915     7 LKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  438 TENAHLLVQQLTVLGKANNR------------TLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQ 505
Cdd:cd14915    87 TVNTKRVIQYFATIAVTGEKkkeeaasgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASAD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  506 ISEYLLEKSRVIHQAIGEKNFHIFYYIYAGlaEKKKLAHYKLPENKPprylqNDHLRTVQDIMNNSFYKSQYELI--EQC 583
Cdd:cd14915   167 IETYLLEKSRVTFQLKAERSYHIFYQIMSN--KKPELIEMLLITTNP-----YDFAFVSQGEITVPSIDDQEELMatDSA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  584 FKVIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQIDKSHISnhtALENCASLLCIRADELQEALTSHCVVTRGETII 663
Cdd:cd14915   240 VDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTE---VADKAAYLTSLNSADLLKALCYPRVKVGNEYVT 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  664 RPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKhdsspSGNGDELSIGILDIFGFENFKKNSFEQLCINIANEQIQY 743
Cdd:cd14915   317 KGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-----TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQ 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  744 YYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEK-FEGNL-KSQYFWRPK 821
Cdd:cd14915   392 FFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKlYEQHLgKSNNFQKPK 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  822 ----RMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDnsvirqlvnhpltktgnlphSKTKNVINYQMRTS 897
Cdd:cd14915   472 pakgKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSG--------------------MKTLAFLFSGGQTA 531
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  898 EklinlAKGDTGEATRHARETTnmkTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGI 977
Cdd:cd14915   532 E-----AEGGGGKKGGKKKGSS---FQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGV 603
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767960106  978 LETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRM--SPDTCATILEKAGLDN--WALGKTKVFLK 1041
Cdd:cd14915   604 LEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFidSKKASEKLLGSIDIDHtqYKFGHTKVFFK 671
MYSc_Myh13 cd14923
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...
358-1041 1.80e-105

class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276887 [Multi-domain]  Cd Length: 671  Bit Score: 352.45  E-value: 1.80e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  358 LEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGK 437
Cdd:cd14923     7 LKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGESGAGK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  438 TENAHLLVQQLTVLGKANNR-----------TLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQI 506
Cdd:cd14923    87 TVNTKRVIQYFATIAVTGDKkkeqqpgkmqgTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADI 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  507 SEYLLEKSRVIHQAIGEKNFHIFYYIYAGlaEKKKLAHYKLPENKP---PRYLQNDhlRTVQDIMNNSfyksqyELI--E 581
Cdd:cd14923   167 ETYLLEKSRVTFQLSSERSYHIFYQIMSN--KKPELIDLLLISTNPfdfPFVSQGE--VTVASIDDSE------ELLatD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  582 QCFKVIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQIDKSHISnhtALENCASLLCIRADELQEALTSHCVVTRGET 661
Cdd:cd14923   237 NAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTE---VADKAGYLMGLNSAEMLKGLCCPRVKVGNEY 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  662 IIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKhdsspSGNGDELSIGILDIFGFENFKKNSFEQLCINIANEQI 741
Cdd:cd14923   314 VTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-----TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  742 QYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEK-FEGNL-KSQYFWR 819
Cdd:cd14923   389 QQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKlYDQHLgKSNNFQK 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  820 PK----RMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNhpltktgnlphsktknviNYQMR 895
Cdd:cd14923   469 PKpakgKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFS------------------NYAGA 530
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  896 TSeklinlakGDTGEATRHARETTNmKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYT 975
Cdd:cd14923   531 EA--------GDSGGSKKGGKKKGS-SFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCN 601
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  976 GILETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRM--SPDTCATILEKAGLDN--WALGKTKVFLK 1041
Cdd:cd14923   602 GVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQFidSKNASEKLLNSIDVDReqYRFGHTKVFFK 671
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
22-289 4.04e-105

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 336.52  E-value: 4.04e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDID--EEIEAEYNILKALsDHPNVVRFYGIYFKkdkvnGDKLWLV 99
Cdd:cd06609     4 TLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAEDeiEDIQQEIQFLSQC-DSPYITKYYGSFLK-----GSKLWII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  100 LELCSGGSVTDLvkgfLKRGeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTR 179
Cdd:cd06609    78 MEYCGGGSVLDL----LKPG-PLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTM 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  180 HRRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLrQPELWSAE 259
Cdd:cd06609   153 SKRNTFVGTPFWMAPEVIKQSG-----YDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNNPPSL-EGNKFSKP 226
                         250       260       270
                  ....*....|....*....|....*....|
gi 767960106  260 FNDFISKCLTKDYEKRPTVSELLQHKFITQ 289
Cdd:cd06609   227 FKDFVELCLNKDPKERPSAKELLKHKFIKK 256
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
16-303 1.65e-103

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 332.09  E-value: 1.65e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDpIHDiDEEIE---AEYNILkALSDHPNVVRFYGIYFkkdkvN 92
Cdd:cd06611     2 NPNDIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQ-IES-EEELEdfmVEIDIL-SECKHPNIVGLYEAYF-----Y 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   93 GDKLWLVLELCSGGSVTDLVkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS 172
Cdd:cd06611    74 ENKLWILIEFCDGGALDSIM---LELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLTSTRHRRNTSVGTPFWMAPEVIACEQQLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQ 252
Cdd:cd06611   151 AKNKSTLQKRDTFIGTPYWMAPEVVACETFKDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEPPTLDQ 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767960106  253 PELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQIeGKDVMLQKQLTE 303
Cdd:cd06611   231 PSKWSSSFNDFLKSCLVKDPDDRPTAAELLKHPFVSDQ-SDNKAIKDLLAE 280
MYSc_Myo38 cd14899
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...
362-1001 6.22e-100

class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276864 [Multi-domain]  Cd Length: 717  Bit Score: 338.22  E-value: 6.22e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  362 YSRDQIYVYVGDILIALNPFQSLGL---------YSTKHSKLYIGSKRTASP--PHIFAMADLGYQSMITYNSDQCIVIS 430
Cdd:cd14899    11 YERHAIYTHIGDILISINPFQDLPQlygdeilrgYAYDHNSQFGDRVTSTDPrePHLFAVARAAYIDIVQNGRSQSILIS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  431 GESGAGKTENAHLLVQQLTVLGKANN-----------------RTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEM 493
Cdd:cd14899    91 GESGAGKTEATKIIMTYFAVHCGTGNnnltnsesisppaspsrTTIEEQVLQSNPILEAFGNARTVRNDNSSRFGKFIEL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  494 KFTSSG-AVVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGLA------EKKKLAHYKLPENKppRYLQNDHLRTVQD 566
Cdd:cd14899   171 RFRDERrRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADNncvskeQKQVLALSGGPQSF--RLLNQSLCSKRRD 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  567 IMNNSFyksQYELIEQCFKVIGFTMEQLGSIYSILAAILNVGNIEFSSV---------ATEHQIDKSHISNHTALENCAS 637
Cdd:cd14899   249 GVKDGV---QFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIphkgddtvfADEARVMSSTTGAFDHFTKAAE 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  638 LLCIRADELQEALTSHCVVTRGETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGNGDELS----- 712
Cdd:cd14899   326 LLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASAPWGADESDvddee 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  713 -----IGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLL 787
Cdd:cd14899   406 datdfIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELFEHRPIGIF 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  788 SLLDEESRFPKATDQTLVEK----FEGNLKSQYFWRPKRMELS--FGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRS 861
Cdd:cd14899   486 SLTDQECVFPQGTDRALVAKyyleFEKKNSHPHFRSAPLIQRTtqFVVAHYAGCVTYTIDGFLAKNKDSFCESAAQLLAG 565
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  862 SDNSVIRQLVnhplTKTGNLPHSKTKNVINYQMRTSEKlinlAKGDTGEAtrharettnmktqTVASYFRYSLMDLLSKM 941
Cdd:cd14899   566 SSNPLIQALA----AGSNDEDANGDSELDGFGGRTRRR----AKSAIAAV-------------SVGTQFKIQLNELLSTV 624
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  942 VVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGFSHRILFANFIKRY 1001
Cdd:cd14899   625 RATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
352-1004 5.77e-99

class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276863  Cd Length: 578  Bit Score: 330.71  E-value: 5.77e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  352 NTVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKhsKLYIGSKRTASPpHIFAMADLGYQSMITYnSDQCIVISG 431
Cdd:cd14898     1 NATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAM--KAYLKNYSHVEP-HVYDVAEASVQDLLVH-GNQTIVISG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  432 ESGAGKTENAHLLVQQLtVLGKANNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFtsSGAVVGAQISEYLL 511
Cdd:cd14898    77 ESGSGKTENAKLVIKYL-VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGKITGAKFETYLL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  512 EKSRVIHQAIGEKNFHIFYYIYAglaeKKKLAhyklpenkppryLQNDHLRT---VQDIMNNSFYKSQYELIEQCFKVIG 588
Cdd:cd14898   154 EKSRVTHHEKGERNFHIFYQFCA----SKRLN------------IKNDFIDTsstAGNKESIVQLSEKYKMTCSAMKSLG 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  589 FTmeQLGSIYSILAAILNVGNIEFSSvateHQIDKShISNHTALENCaSLLCIRADELQEALTSHCVVTRGETIIRPNTV 668
Cdd:cd14898   218 IA--NFKSIEDCLLGILYLGSIQFVN----DGILKL-QRNESFTEFC-KLHNIQEEDFEESLVKFSIQVKGETIEVFNTL 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  669 EKATDVRDAMAKTLYGRLFSWIVNCINSLLkhdsspSGNGdELSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQH 748
Cdd:cd14898   290 KQARTIRNSMARLLYSNVFNYITASINNCL------EGSG-ERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKK 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  749 VFAWEQNEYLNEDVDARVIEYEDNWPLLDMFlQKPMGLLSLLDEESRFPKATDQTLVEKFEGNLKsqYFWRPKRMElSFG 828
Cdd:cd14898   363 MFRAKQGMYKEEGIEWPDVEFFDNNQCIRDF-EKPCGLMDLISEESFNAWGNVKNLLVKIKKYLN--GFINTKARD-KIK 438
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  829 IHHYAGKVLYNASGFLAKNRDtlptdivlllrssdnsvirqlvnhpltkTGNLphsktknvinyqmrtseklinLAKGDT 908
Cdd:cd14898   439 VSHYAGDVEYDLRDFLDKNRE----------------------------KGQL---------------------LIFKNL 469
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  909 GEATRHAREttnmktqTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGF 988
Cdd:cd14898   470 LINDEGSKE-------DLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCF 542
                         650
                  ....*....|....*.
gi 767960106  989 SHRILFANFIKRYYLL 1004
Cdd:cd14898   543 PQEIPKDRFEERYRIL 558
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
365-1040 1.07e-96

class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276847 [Multi-domain]  Cd Length: 633  Bit Score: 326.30  E-value: 1.07e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  365 DQIYVYVGDILIALNPFQSLG----LYSTKHSKLY---IGSKRTASPPHifamADLGYQsmitynsdQCIVISGESGAGK 437
Cdd:cd14881    14 KEFFTNVGPILLSVNPYRDVGnpltLTSTRSSPLApqlLKVVQEAVRQQ----SETGYP--------QAIILSGTSGSGK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  438 TENAHLLVQQLTVLGKANNRTLQEKilqvnNLVEAF------GNACTIINDNSSRFGKYLEMKFTSsGAVVGAQISEYLL 511
Cdd:cd14881    82 TYASMLLLRQLFDVAGGGPETDAFK-----HLAAAFtvlrslGSAKTATNSESSRIGHFIEVQVTD-GALYRTKIHCYFL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  512 EKSRVIHQAIGEKNFHIFYYIYAGLA--EKKK--LAHYKlPENKppRYLQNDHLRtvQDIMNNsfyKSQYELIEQCFKVI 587
Cdd:cd14881   156 DQTRVIRPLPGEKNYHIFYQMLAGLSqeERVKlhLDGYS-PANL--RYLSHGDTR--QNEAED---AARFQAWKACLGIL 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  588 G--FTmeqlgSIYSILAAILNVGNIEFSSvATEHQIDkshISNHTALENCASLLCIRADELQEALTSHCVVTRGETIIRP 665
Cdd:cd14881   228 GipFL-----DVVRVLAAVLLLGNVQFID-GGGLEVD---VKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKSV 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  666 NTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGNGDELSIGILDIFGFENFKKNSFEQLCINIANEQIQYYY 745
Cdd:cd14881   299 CDANMSNMTRDALAKALYCRTVATIVRRANSLKRLGSTLGTHATDGFIGILDMFGFEDPKPSQLEHLCINLCAETMQHFY 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  746 NQHVFAWEQNEYLNEDVDARV-IEYEDNWPLLDMFLQKPMGLLSLLDEESRfPKATDQTLVEKFEGNLK-SQYFWRPKRM 823
Cdd:cd14881   379 NTHIFKSSIESCRDEGIQCEVeVDYVDNVPCIDLISSLRTGLLSMLDVECS-PRGTAESYVAKIKVQHRqNPRLFEAKPQ 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  824 ELS-FGIHHYAGKVLYNASGFLAKNRDTLPTDIVlllrssdnSVIRqlvnhpltktgnlphsktKNVINYqmrtseklin 902
Cdd:cd14881   458 DDRmFGIRHFAGRVVYDASDFLDTNRDVVPDDLV--------AVFY------------------KQNCNF---------- 501
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  903 lakgdtGEATrHarettnmkTQTvasyFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETAR 982
Cdd:cd14881   502 ------GFAT-H--------TQD----FHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVN 562
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767960106  983 IRRLGFSHRILFANFIKRYYLLCY----KSSEEPRMspDTCATILEKAGLD----------NWALGKTKVFL 1040
Cdd:cd14881   563 LMAGGYPHRMRFKAFNARYRLLAPfrllRRVEEKAL--EDCALILQFLEAQppsklssvstSWALGKRHIFL 632
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
16-287 1.34e-96

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 313.58  E-value: 1.34e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVRFYGIYFKKDKVN-GD 94
Cdd:cd06637     3 DPAGIFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKNPPGmDD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 KLWLVLELCSGGSVTDLVKGflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:cd06637    83 QLWLVMEFCGAGSVTDLIKN--TKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LTSTRHRRNTSVGTPFWMAPEVIACEQQLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQPE 254
Cdd:cd06637   161 LDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPAPRLKSKK 240
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767960106  255 lWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06637   241 -WSKKFQSFIESCLVKNHSQRPSTEQLMKHPFI 272
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
25-288 3.77e-92

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 299.13  E-value: 3.77e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSdHPNVVRFYGIYfkkdKVNGDkLWLVLELCS 104
Cdd:cd06614     6 EKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKELIINEILIMKECK-HPNIVDYYDSY----LVGDE-LWVVMEYMD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  105 GGSVTDLVKGFLKRgerMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRRNT 184
Cdd:cd06614    80 GGSLTDIITQNPVR---MNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKRNS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  185 SVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQPELWSAEFNDFI 264
Cdd:cd06614   157 VVGTPYWMAPEVI-----KRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKGIPPLKNPEKWSPEFKDFL 231
                         250       260
                  ....*....|....*....|....
gi 767960106  265 SKCLTKDYEKRPTVSELLQHKFIT 288
Cdd:cd06614   232 NKCLVKDPEKRPSAEELLQHPFLK 255
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
21-287 6.83e-87

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 284.04  E-value: 6.83e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106     21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDID--EEIEAEYNILKALsDHPNVVRFYGIYFKKDKvngdkLWL 98
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKdrERILREIKILKKL-KHPNIVRLYDVFEDEDK-----LYL 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106     99 VLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST 178
Cdd:smart00220   75 VMEYCEGGDLFDL----LKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPG 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    179 rHRRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQPE-LWS 257
Cdd:smart00220  151 -EKLTTFVGTPEYMAPEVLLGKG-----YGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEwDIS 224
                           250       260       270
                    ....*....|....*....|....*....|
gi 767960106    258 AEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:smart00220  225 PEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
16-288 1.07e-84

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 278.83  E-value: 1.07e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPihDIDEEIE---AEYNILkALSDHPNVVRFYGIYFKKDKvn 92
Cdd:cd06643     2 NPEDFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDT--KSEEELEdymVEIDIL-ASCDHPNIVKLLDAFYYENN-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   93 gdkLWLVLELCSGGSVtDLVKGFLKRGerMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS 172
Cdd:cd06643    77 ---LWILIEFCAGGAV-DAVMLELERP--LTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLTSTRHRRNTSVGTPFWMAPEVIACEQQLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQ 252
Cdd:cd06643   151 AKNTRTLQRRDSFIGTPYWMAPEVVMCETSKDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLAQ 230
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767960106  253 PELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFIT 288
Cdd:cd06643   231 PSRWSPEFKDFLRKCLEKNVDARWTTSQLLQHPFVS 266
MYSc_Myo18 cd01386
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...
367-1041 5.48e-84

class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276837 [Multi-domain]  Cd Length: 689  Bit Score: 291.14  E-value: 5.48e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  367 IYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGKTENAHLLVQ 446
Cdd:cd01386    16 IHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRSGSGKTTNCRHILE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  447 QL-TVLGKANNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLLEKSRVIHQAIGEKN 525
Cdd:cd01386    96 YLvTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLLERSRVARRPEGESN 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  526 FHIFYYIYAGL--AEKKKLAHYKLPENK----PPRYLQNDHLRTVQdimnnsfyksQYELIEQCFKVIGFTMEQLGSIYS 599
Cdd:cd01386   176 FNVFYYLLAGAdaALRTELHLNQLAESNsfgiVPLQKPEDKQKAAA----------AFSKLQAAMKTLGISEEEQRAIWS 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  600 ILAAILNVGNIEfssVATEHQIDKSHISNHTALENCASLLCIRADELQEALTSHCV----------VTRGETIIRPNTVE 669
Cdd:cd01386   246 ILAAIYHLGAAG---ATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHHLsggpqqsttsSGQESPARSSSGGP 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  670 KATDVR--DAMAKTLYGRLFSWIVNCIN-SLLKHDSSPSgngdelSIGILDIFGFENFKKN------SFEQLCINIANEQ 740
Cdd:cd01386   323 KLTGVEalEGFAAGLYSELFAAVVSLINrSLSSSHHSTS------SITIVDTPGFQNPAHSgsqrgaTFEDLCHNYAQER 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  741 IQYYYNQHVFAWEQNEYLNEDVDARVIEYEDN-WPLLDMFLQKPM--------------GLLSLLDEESRFPKATDQTLV 805
Cdd:cd01386   397 LQLLFHERTFVAPLERYKQENVEVDFDLPELSpGALVALIDQAPQqalvrsdlrdedrrGLLWLLDEEALYPGSSDDTFL 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  806 EKF------EGNLKSQYFWRPKRMELSFGIHHYAGK--VLYNASGFLAKNRDtlptdivlllrssdnsvirqlvnHPLTK 877
Cdd:cd01386   477 ERLfshygdKEGGKGHSLLRRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKE-----------------------NPSAQ 533
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  878 TGN--LPHSKtknvinyqmrtseklinlakgdtgeatrhaRETTNMKTQTVASYFRYS---LMDLLSKMvvgQPHFVRCI 952
Cdd:cd01386   534 NATqlLQESQ------------------------------KETAAVKRKSPCLQIKFQvdaLIDTLRRT---GLHFVHCL 580
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  953 KPNSE------RQARKYDKEKVL------LQLRYTGILETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRMSPDTCA 1020
Cdd:cd01386   581 LPQHNagkderSTSSPAAGDELLdvpllrSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGLNSEVAD 660
                         730       740
                  ....*....|....*....|....*....
gi 767960106 1021 ------TILEKAGLD--NWALGKTKVFLK 1041
Cdd:cd01386   661 erkaveELLEELDLEksSYRIGLSQVFFR 689
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
354-1041 1.54e-83

class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276841 [Multi-domain]  Cd Length: 628  Bit Score: 287.92  E-value: 1.54e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  354 VSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYigskrtasppHIFAMADLGYQSMITYNSD-QCIVISGE 432
Cdd:cd14874     3 IAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGGE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  433 SGAGKTENAHLLVQQLTVLGKANNRTLQEKILQvnNLVEAFGNACTIINDNSSRFGKYLEMKFTSSgAVVGAQISEYL-L 511
Cdd:cd14874    73 SGSGKSYNAFQVFKYLTSQPKSKVTTKHSSAIE--SVFKSFGCAKTLKNDEATRFGCSIDLLYKRN-VLTGLNLKYTVpL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  512 EKSRVIHQAIGEKNFHIFYYIYAGLAEKKKlAHYKLPENKPPRYL-QNDHLRTVQDIMNNsfyksqYELIEQCFKVIGFT 590
Cdd:cd14874   150 EVPRVISQKPGERNFNVFYEVYHGLNDEMK-AKFGIKGLQKFFYInQGNSTENIQSDVNH------FKHLEDALHVLGFS 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  591 MEQLGSIYSILAAILNVGNIEFSSVA---TEHQIdkSHISNHTALENCASLLCIRADELQEALTshCVVTRGETIirpnT 667
Cdd:cd14874   223 DDHCISIYKIISTILHIGNIYFRTKRnpnVEQDV--VEIGNMSEVKWVAFLLEVDFDQLVNFLL--PKSEDGTTI----D 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  668 VEKATDVRDAMAKTLYGRLFSWIVNCINSLLKhdsSPSGNGdelSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQ 747
Cdd:cd14874   295 LNAALDNRDSFAMLIYEELFKWVLNRIGLHLK---CPLHTG---VISILDHYGFEKYNNNGVEEFLINSVNERIENLFVK 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  748 HVFAWEQNEYLNE--DVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNL--KSQYFWRPKRM 823
Cdd:cd14874   369 HSFHDQLVDYAKDgiSVDYKVPNSIENGKTVELLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHtdRSSYGKARNKE 448
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  824 ELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNhpltktgnlphsktknviNYQMRTSEKLInl 903
Cdd:cd14874   449 RLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE------------------SYSSNTSDMIV-- 508
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  904 akgdtgeatrharettnmktqTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARI 983
Cdd:cd14874   509 ---------------------SQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSF 567
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767960106  984 RRLGFSHRILFANFIKRYYLLCYKSSEEPRMSPDTCATILEKAGL---DNWALGKTKVFLK 1041
Cdd:cd14874   568 RIKGYPVKISKTTFARQYRCLLPGDIAMCQNEKEIIQDILQGQGVkyeNDFKIGTEYVFLR 628
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
16-290 3.87e-83

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 274.99  E-value: 3.87e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDidEEIE---AEYNILkALSDHPNVVRFYGIYFKKDKvn 92
Cdd:cd06644     9 DPNEVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSE--EELEdymVEIEIL-ATCNHPYIVKLLGAFYWDGK-- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   93 gdkLWLVLELCSGGSVtDLVKGFLKRGerMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS 172
Cdd:cd06644    84 ---LWIMIEFCPGGAV-DAIMLELDRG--LTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLTSTRHRRNTSVGTPFWMAPEVIACEQQLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQ 252
Cdd:cd06644   158 AKNVKTLQRRDSFIGTPYWMAPEVVMCETMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLSQ 237
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767960106  253 PELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQI 290
Cdd:cd06644   238 PSKWSMEFRDFLKTALDKHPETRPSAAQLLEHPFVSSV 275
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
352-997 1.95e-82

class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276870  Cd Length: 673  Bit Score: 286.22  E-value: 1.95e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  352 NTVSEQLEKCYSRDQIYVYVGDILIALNPFQSLG-LYSTKHSKLYigSKRTASPPHIFAMADLGYQSMITYNSDQCIVIS 430
Cdd:cd14905     1 DTLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  431 GESGAGKTENAHLLVQQLTVLGKANNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYL 510
Cdd:cd14905    79 GESGSGKSENTKIIIQYLLTTDLSRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  511 LEKSRVIHQAIGEKNFHIFYYIYAGLAEKKKLAhYKLPENKPPRYLQNDHLRTVQDIMNNSFyksqYELIEQCFKVIGFT 590
Cdd:cd14905   159 LDENRVTYQNKGERNFHIFYQFLKGITDEEKAA-YQLGDINSYHYLNQGGSISVESIDDNRV----FDRLKMSFVFFDFP 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  591 MEQLGSIYSILAAILNVGNIEFSsvateHQIDKSHISNHTALENCASLLCIRADELQEALTSHcvvtrgetiiRPNTVEK 670
Cdd:cd14905   234 SEKIDLIFKTLSFIIILGNVTFF-----QKNGKTEVKDRTLIESLSHNITFDSTKLENILISD----------RSMPVNE 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  671 ATDVRDAMAKTLYGRLFSWIVNCINSLLKhdssPSGNGDELsiGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVF 750
Cdd:cd14905   299 AVENRDSLARSLYSALFHWIIDFLNSKLK----PTQYSHTL--GILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVL 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  751 AWEQNEYLNEDVDARV-IEYEDNWPLLDMFLQkpmgLLSLLDEESRFPKATDQTLVEKFEGNLKSQYFWRPKRMElsFGI 829
Cdd:cd14905   373 KQEQREYQTERIPWMTpISFKDNEESVEMMEK----IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFGKKPNK--FGI 446
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  830 HHYAGKVLYNASGFLAKNRDTLPTDIVLLLRssdNSVIRQLVNHPLTKTGNLPHSKTKNVINYQMRTSEKLINLAKGDTG 909
Cdd:cd14905   447 EHYFGQFYYDVRGFIIKNRDEILQRTNVLHK---NSITKYLFSRDGVFNINATVAELNQMFDAKNTAKKSPLSIVKVLLS 523
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  910 EATRHARETTNMKTQT----------------VASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLR 973
Cdd:cd14905   524 CGSNNPNNVNNPNNNSgggggggnsgggsgsgGSTYTTYSSTNKAINNSNCDFHFIRCIKPNSKKTHLTFDVKSVNEQIK 603
                         650       660
                  ....*....|....*....|....*...
gi 767960106  974 YTGILETARIRRLGFS----HRILFANF 997
Cdd:cd14905   604 SLCLLETTRIQRFGYTihynNKIFFDRF 631
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
364-1041 1.37e-81

class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276852  Cd Length: 725  Bit Score: 285.39  E-value: 1.37e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  364 RDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGKTENAHL 443
Cdd:cd14887    21 RNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRRSQSILISGESGAGKTETSKH 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  444 LVQQLTVLGK----ANNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLLEKSRVIHQ 519
Cdd:cd14887   101 VLTYLAAVSDrrhgADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRI 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  520 AIGEKNFHIFYYIyaglaekkklahyklpenkppryLQNDHLRTVQDIMNNSFYKSQYEL--IEQCFKVIGFTMEQLGSI 597
Cdd:cd14887   181 PSDEFSFHIFYAL-----------------------CNAAVAAATQKSSAGEGDPESTDLrrITAAMKTVGIGGGEQADI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  598 YSILAAILNVGNIEFSSVAT-----------------EHQIDKSHIS--------------NHTALENCASLLCIRA--- 643
Cdd:cd14887   238 FKLLAAILHLGNVEFTTDQEpetskkrkltsvsvgceETAADRSHSSevkclssglkvteaSRKHLKTVARLLGLPPgve 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  644 --DELQEALTSHCVVTRGETIirpnTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPS-GNGDE--------LS 712
Cdd:cd14887   318 geEMLRLALVSRSVRETRSFF----DLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKPSeSDSDEdtpsttgtQT 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  713 IGILDIFGFENFK---KNSFEQLCINIANEQI------QYYYNQHVFAWEQNEYLNEDVDArvieYEDNWPLLDMFLQKP 783
Cdd:cd14887   394 IGILDLFGFEDLRnhsKNRLEQLCINYANERLhcflleQLILNEHMLYTQEGVFQNQDCSA----FPFSFPLASTLTSSP 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  784 MGLLSLL---DEESRFPKATDQTLVEKF--------------EGNLKSQYFWRP------------------KRMELSFG 828
Cdd:cd14887   470 SSTSPFSptpSFRSSSAFATSPSLPSSLsslssslsssppvwEGRDNSDLFYEKlnkniinsakyknitpalSRENLEFT 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  829 IHHYAGKVLYNASGFLAKNRDTLPTDIVLLLrSSDNSVIRqlvnhpltktgnlphsktknvinyqmrtseklINLAKGDT 908
Cdd:cd14887   550 VSHFACDVTYDARDFCRANREATSDELERLF-LACSTYTR--------------------------------LVGSKKNS 596
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  909 GeatrhaRETTNMKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGF 988
Cdd:cd14887   597 G------VRAISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGF 670
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  989 SHRILFANFIKRYYLLCYKSSEEPRMSPDTCATILEKAGLD--NWALGKTKVFLK 1041
Cdd:cd14887   671 PCRLPYVELWRRYETKLPMALREALTPKMFCKIVLMFLEINsnSYTFGKTKIFFR 725
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
25-287 1.44e-81

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 268.71  E-value: 1.44e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQKAAVKILdPIHDIDEE----IEAEYNILKALsDHPNVVRFYGiYFKkdkvNGDKLWLVL 100
Cdd:cd06627     6 DLIGRGAFGSVYKGLNLNTGEFVAIKQI-SLEKIPKSdlksVMGEIDLLKKL-NHPNIVKYIG-SVK----TKDSLYIIL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCSGGSVTDLVKGFlkrgERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRH 180
Cdd:cd06627    79 EYVENGSLASIIKKF----GKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVEK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  181 RRNTSVGTPFWMAPEVIacEQQLDTTydaRCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLrqPELWSAEF 260
Cdd:cd06627   155 DENSVVGTPYWMAPEVI--EMSGVTT---ASDIWSVGCTVIELLTGNPPYYDLQPMAALFRIVQDDHPPL--PENISPEL 227
                         250       260
                  ....*....|....*....|....*..
gi 767960106  261 NDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06627   228 RDFLLQCFQKDPTLRPSAKELLKHPWL 254
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
362-1041 1.60e-80

class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276897  Cd Length: 637  Bit Score: 279.59  E-value: 1.60e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  362 YSRDQIYVYVGDILIALNPFQSLGL----YSTKHSKLYigskrtasPPHIFAMADLGYQSMITYNSDQCIVISGESGAGK 437
Cdd:cd14937    11 YKKNYIYTIAEPMLISINPYQVIDVdineYKNKNTNEL--------PPHVYSYAKDAMTDFINTKTNQSIIISGESGSGK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  438 TEnAHLLVQQLTVLGKANNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLLEKSRVI 517
Cdd:cd14937    83 TE-ASKLVIKYYLSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLLENIRVV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  518 HQAIGEKNFHIFYYIYAGLAEKKKlAHYKLPENKPPRYLQN--------DHLRTVQDIMnNSFYKSQYELIEQcfkvigf 589
Cdd:cd14937   162 SQEEEERGYHIFYQIFNGMSQELK-NKYKIRSENEYKYIVNknvvipeiDDAKDFGNLM-ISFDKMNMHDMKD------- 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  590 tmeqlgSIYSILAAILNVGNIEFSSVATEHQIDKSHI-SNHTALENCAS-LLCIRADELQEALTSHCVVTRGETIIRPNT 667
Cdd:cd14937   233 ------DLFLTLSGLLLLGNVEYQEIEKGGKTNCSELdKNNLELVNEISnLLGINYENLKDCLVFTEKTIANQKIEIPLS 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  668 VEKATDVRDAMAKTLYGRLFSWIVNCINSLLKhdsspsgNGDELS--IGILDIFGFENFKKNSFEQLCINIANEQIQYYY 745
Cdd:cd14937   307 VEESVSICKSISKDLYNKIFSYITKRINNFLN-------NNKELNnyIGILDIFGFEIFSKNSLEQLLINIANEEIHSIY 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  746 NQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMfLQKPMGLLSLLDEESRFPKATDQTLV----EKFEGNLKsqYFWRPK 821
Cdd:cd14937   380 LYIVYEKETELYKAEDILIESVKYTTNESIIDL-LRGKTSIISILEDSCLGPVKNDESIVsvytNKFSKHEK--YASTKK 456
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  822 RMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQL-----VNHPLTKtgnlphsktKNVINYQMrt 896
Cdd:cd14937   457 DINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLyedveVSESLGR---------KNLITFKY-- 525
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  897 sekLINLakgdtgeatrharettnmktQTVASYFRYSLMdllskmvvgqpHFVRCIKPNSERQARKYDKEKVLLQLRYTG 976
Cdd:cd14937   526 ---LKNL--------------------NNIISYLKSTNI-----------YFIKCIKPNENKEKNNFNQKKVFPQLFSLS 571
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767960106  977 ILETARIRRLgFSHRILFANFIKRYYLLCYKSSEEPRMSPDTCATILEKAGLDN--WALGKTKVFLK 1041
Cdd:cd14937   572 IIETLNISFF-FQYKYTFDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQNTVDPdlYKVGKTMVFLK 637
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
19-287 4.78e-80

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 264.99  E-value: 4.78e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILD------PIHDIDEEIEAeynilKALSDHPNVVRFYGIYfkkdkVN 92
Cdd:cd06610     1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDlekcqtSMDELRKEIQA-----MSQCNHPNVVSYYTSF-----VV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   93 GDKLWLVLELCSGGSVTDLVKGFLKRGErMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS 172
Cdd:cd06610    71 GDELWLVMPLLSGGSLLDIMKSSYPRGG-LDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQL----TSTRHRRNTSVGTPFWMAPEVIacEQqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPP 248
Cdd:cd06610   150 ASLatggDRTRKVRKTFVGTPCWMAPEVM--EQ--VRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDPP 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767960106  249 KL---RQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06610   226 SLetgADYKKYSKSFRKMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
21-287 9.89e-80

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 263.61  E-value: 9.89e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEA---EYNILKALSdHPNVVRFYGIYFKKDKVNgdklw 97
Cdd:cd06606     2 WKKGELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEAlerEIRILSSLK-HPNIVRYLGTERTENTLN----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVTDLVKGFLKrgerMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL-- 175
Cdd:cd06606    76 IFLEYVPGGSLASLLKKFGK----LPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLae 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTRHRRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPLADLH-PMRALFKIPRNP-PPKLrqP 253
Cdd:cd06606   152 IATGEGTKSLRGTPYWMAPEVIRGEG-----YGRAADIWSLGCTVIEMATGKPPWSELGnPVAALFKIGSSGePPPI--P 224
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767960106  254 ELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06606   225 EHLSEEAKDFLRKCLQRDPKKRPTADELLQHPFL 258
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
16-297 2.09e-74

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 249.20  E-value: 2.09e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDpIHDIDEEIEAEYNILKALS--DHPNVVRFYGIYFKkdkvnG 93
Cdd:cd06642     1 DPEELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIID-LEEAEDEIEDIQQEITVLSqcDSPYITRYYGSYLK-----G 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   94 DKLWLVLELCSGGSVTDLvkgfLKRGErMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSA 173
Cdd:cd06642    75 TKLWIIMEYLGGGSALDL----LKPGP-LEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  174 QLTSTRHRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQP 253
Cdd:cd06642   150 QLTDTQIKRNTFVGTPFWMAPEVIK-----QSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSPPTLEGQ 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 767960106  254 elWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQIEGKDVML 297
Cdd:cd06642   225 --HSKPFKEFVEACLNKDPRFRPTAKELLKHKFITRYTKKTSFL 266
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
24-302 1.78e-73

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 246.62  E-value: 1.78e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   24 TETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDE--EIEAEYNILKAL--SDHPNVVRFYGIYFKkdkvnGDKLWLV 99
Cdd:cd06917     6 LELVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDDDvsDIQKEVALLSQLklGQPKNIIKYYGSYLK-----GPSLWII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  100 LELCSGGSVTDLVkgflkRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTR 179
Cdd:cd06917    81 MDYCEGGSIRTLM-----RAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  180 HRRNTSVGTPFWMAPEVIACEQqldtTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLrQPELWSAE 259
Cdd:cd06917   156 SKRSTFVGTPYWMAPEVITEGK----YYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSKPPRL-EGNGYSPL 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 767960106  260 FNDFISKCLTKDYEKRPTVSELLQHKFITQIEGKDVMLQKQLT 302
Cdd:cd06917   231 LKEFVAACLDEEPKDRLSADELLKSKWIKQHSKTPTSVLKELI 273
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
16-289 2.48e-73

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 246.11  E-value: 2.48e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKI--LDPIHDIDEeIEAEYNILKALSdHPNVVRFYGIYFKKDKvng 93
Cdd:cd06645     8 NPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVikLEPGEDFAV-VQQEIIMMKDCK-HSNIVAYFGSYLRRDK--- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   94 dkLWLVLELCSGGSVTDL--VKGFLkrgermSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGV 171
Cdd:cd06645    83 --LWICMEFCGGGSLQDIyhVTGPL------SESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  172 SAQLTSTRHRRNTSVGTPFWMAPEVIACEQQldTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRN--PPPK 249
Cdd:cd06645   155 SAQITATIAKRKSFIGTPYWMAPEVAAVERK--GGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMTKSnfQPPK 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 767960106  250 LRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQ 289
Cdd:cd06645   233 LKDKMKWSNSFHHFVKMALTKNPKKRPTAEKLLQHPFVTQ 272
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
16-304 3.07e-73

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 245.73  E-value: 3.07e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDpIHDIDEEIEAEYNILKALS--DHPNVVRFYGIYFKkdkvnG 93
Cdd:cd06640     1 DPEELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIID-LEEAEDEIEDIQQEITVLSqcDSPYVTKYYGSYLK-----G 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   94 DKLWLVLELCSGGSVTDLVkgflkRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSA 173
Cdd:cd06640    75 TKLWIIMEYLGGGSALDLL-----RAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  174 QLTSTRHRRNTSVGTPFWMAPEVIaceQQldTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQP 253
Cdd:cd06640   150 QLTDTQIKRNTFVGTPFWMAPEVI---QQ--SAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIPKNNPPTLVGD 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767960106  254 elWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQIEGKDVMLQKQLTEF 304
Cdd:cd06640   225 --FSKPFKEFIDACLNKDPSFRPTAKELLKHKFIVKNAKKTSYLTELIDRF 273
MYSc_Myo32 cd14893
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...
362-1040 4.15e-72

class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276858  Cd Length: 741  Bit Score: 257.59  E-value: 4.15e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  362 YSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTA----------SPPHIFAMADLGYQSMITYNSDQCIVISG 431
Cdd:cd14893    11 YRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQTplyekdtvndAPPHVFALAQNALRCMQDAGEDQAVILLG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  432 ESGAGKTENAHLLVQQLTVLGKANN------------RTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSG 499
Cdd:cd14893    91 GMGAGKSEAAKLIVQYLCEIGDETEprpdsegasgvlHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMISVEFSKHG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  500 AVVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGLAEKKKLAHyKLPENKPPRylQNDHLRTVQDIMNN-SFYKSQYE 578
Cdd:cd14893   171 HVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDPTLRD-SLEMNKCVN--EFVMLKQADPLATNfALDARDYR 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  579 LIEQCFKVIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQIDKShiSNHTALENCASllCIRADELQEALTSHC---- 654
Cdd:cd14893   248 DLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGG--ANSTTVSDAQS--CALKDPAQILLAAKLleve 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  655 -VV------TR-------GETI--IRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLK--HDSSPSGNG--DELSIG 714
Cdd:cd14893   324 pVVldnyfrTRqffskdgNKTVssLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILGgiFDRYEKSNIviNSQGVH 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  715 ILDIFGFENF--KKNSFEQLCINIANEQIQYYYNQHVFAweQNEYLNEDVDARV-----------IEYEDNwPLLDMFLQ 781
Cdd:cd14893   404 VLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYVQNTLA--INFSFLEDESQQVenrltvnsnvdITSEQE-KCLQLFED 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  782 KPMGLLSLLDEESRFPKATDQTLVEK-FEGN--------------LKSQYFWRPKRMELSFGIHHYAGKVLYNASGFLAK 846
Cdd:cd14893   481 KPFGIFDLLTENCKVRLPNDEDFVNKlFSGNeavgglsrpnmgadTTNEYLAPSKDWRLLFIVQHHCGKVTYNGKGLSSK 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  847 NRDTLPTDIVLLLRSSDNSVIrqlvnHPLTKTGNLPHSKTKNVINYQMRTSEklinlaKGDTGEATRHARETTNMKTQTV 926
Cdd:cd14893   561 NMLSISSTCAAIMQSSKNAVL-----HAVGAAQMAAASSEKAAKQTEERGST------SSKFRKSASSARESKNITDSAA 629
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  927 ASYfrYSLMD-LLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGFSHRILFANFIKRYYLLC 1005
Cdd:cd14893   630 TDV--YNQADaLLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKNVC 707
                         730       740       750
                  ....*....|....*....|....*....|....*.
gi 767960106 1006 -YKSSEEPRMSPDTCATILEKaglDNWALGKTKVFL 1040
Cdd:cd14893   708 gHRGTLESLLRSLSAIGVLEE---EKFVVGKTKVYL 740
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
16-287 4.48e-72

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 242.24  E-value: 4.48e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKI--LDPIHDIdEEIEAEYNILKALSdHPNVVRFYGIYFKKDKvng 93
Cdd:cd06646     6 NPQHDYELIQRVGSGTYGDVYKARNLHTGELAAVKIikLEPGDDF-SLIQQEIFMVKECK-HCNIVAYFGSYLSREK--- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   94 dkLWLVLELCSGGSVTDL--VKGFLkrgermSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGV 171
Cdd:cd06646    81 --LWICMEYCGGGSLQDIyhVTGPL------SELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  172 SAQLTSTRHRRNTSVGTPFWMAPEVIACEQqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRN--PPPK 249
Cdd:cd06646   153 AAKITATIAKRKSFIGTPYWMAPEVAAVEK--NGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMSKSnfQPPK 230
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767960106  250 LRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06646   231 LKDKTKWSSTFHNFVKISLTKNPKKRPTAERLLTHLFV 268
MYSc_Myo23 cd14884
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ...
353-993 1.15e-71

class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276850 [Multi-domain]  Cd Length: 685  Bit Score: 254.83  E-value: 1.15e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  353 TVSEQLEKCYSRDQIYVYVGDILIALNPFQSL-GLYSTKHSKLYIGSKRTAS-------PPHIFAMADLGYQSMITYNSD 424
Cdd:cd14884     2 NVLQNLKNRYLKNKIYTFHASLLLALNPYKPLkELYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLKR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  425 QCIVISGESGAGKTENAHLLVQQLT-VLGKANNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTS------ 497
Cdd:cd14884    82 QTIVVSGHSGSGKTENCKFLFKYFHyIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEventqk 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  498 ---SGAVVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGLAEK--------KKLAHYKLPENKPPRYLQ--NDHLRTV 564
Cdd:cd14884   162 nmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEdlarrnlvRNCGVYGLLNPDESHQKRsvKGTLRLG 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  565 QDimNNSFYKSQYELIEQCFKV-------IGFTMEQLGSIYSILAAILNVGNiefssvatehqidkshisnhTALENCAS 637
Cdd:cd14884   242 SD--SLDPSEEEKAKDEKNFVAllhglhyIKYDERQINEFFDIIAGILHLGN--------------------RAYKAAAE 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  638 LLCIRADELQEALTSHCVVTRGETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCIN-SLLKHDS--------SPSGNg 708
Cdd:cd14884   300 CLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINrNVLKCKEkdesdnedIYSIN- 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  709 dELSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLdMFLQKpmgLLS 788
Cdd:cd14884   379 -EAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTL-IFIAK---IFR 453
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  789 LLDEESRFP----KATDQTLVEKFEGNLKSQY--------FWRPKRMELS----------FGIHHYAGKVLYNASGFLAK 846
Cdd:cd14884   454 RLDDITKLKnqgqKKTDDHFFRYLLNNERQQQlegkvsygFVLNHDADGTakkqnikkniFFIRHYAGLVTYRINNWIDK 533
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  847 NRDTLPTDIVLLLRSSDNSVIRQlvnhpltktgNLPHSKTKNVINyqmrTSEKLINlakgdtgeatrharETTNMKTQtv 926
Cdd:cd14884   534 NSDKIETSIETLISCSSNRFLRE----------ANNGGNKGNFLS----VSKKYIK--------------ELDNLFTQ-- 583
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767960106  927 asyfryslmdlLSKMVVgqpHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGFSHRIL 993
Cdd:cd14884   584 -----------LQSTDM---YYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
16-304 1.56e-68

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 232.27  E-value: 1.56e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDpIHDIDEEIEAEYNILKALS--DHPNVVRFYGIYFKKDKvng 93
Cdd:cd06641     1 DPEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIID-LEEAEDEIEDIQQEITVLSqcDSPYVTKYYGSYLKDTK--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   94 dkLWLVLELCSGGSVTDLvkgfLKRGErMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSA 173
Cdd:cd06641    77 --LWIIMEYLGGGSALDL----LEPGP-LDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  174 QLTSTRHRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQP 253
Cdd:cd06641   150 QLTDTQIKRN*FVGTPFWMAPEVIK-----QSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGN 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767960106  254 elWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQIEGKDVMLQKQLTEF 304
Cdd:cd06641   225 --YSKPLKEFVEACLNKEPSFRPTAKELLKHKFILRNAKKTSYLTELIDRY 273
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
22-292 1.67e-67

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 228.63  E-value: 1.67e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDID--EEIEAEYNILKAlSDHPNVVRFYGIYFKKDKVNgdklwLV 99
Cdd:cd06623     4 ERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEfrKQLLRELKTLRS-CESPYVVKCYGAFYKEGEIS-----IV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  100 LELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNN-KTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST 178
Cdd:cd06623    78 LEYMDGGSLADL----LKKVGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGEVKIADFGISKVLENT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  179 RHRRNTSVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPLADLH---PMRALFKIPRNPPPKLrQPEL 255
Cdd:cd06623   154 LDQCNTFVGTVTYMSPERIQGE-----SYSYAADIWSLGLTLLECALGKFPFLPPGqpsFFELMQAICDGPPPSL-PAEE 227
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767960106  256 WSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQIEG 292
Cdd:cd06623   228 FSPEFRDFISACLQKDPKKRPSAAELLQHPFIKKADN 264
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
16-287 9.91e-66

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 223.65  E-value: 9.91e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVRFYGIYFKkdkvnGDK 95
Cdd:cd06647     4 DPKKKYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLV-----GDE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSGGSVTDLVKGflkrgERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL 175
Cdd:cd06647    79 LWVVMEYLAGGSLTDVVTE-----TCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTRHRRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQPEL 255
Cdd:cd06647   154 TPEQSKRSTMVGTPYWMAPEVVTRKA-----YGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEK 228
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767960106  256 WSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06647   229 LSAIFRDFLNRCLEMDVEKRGSAKELLQHPFL 260
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
27-287 2.10e-65

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 222.70  E-value: 2.10e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDPIHDidEEIEAEYNILKALSD--HPNVVRFYGIYFKkdkvnGDKLWLVLELCS 104
Cdd:cd06648    15 IGEGSTGIVCIATDKSTGRQVAVKKMDLRKQ--QRRELLFNEVVIMRDyqHPNIVEMYSSYLV-----GDELWVVMEFLE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  105 GGSVTDLVKGflkrgERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRRNT 184
Cdd:cd06648    88 GGALTDIVTH-----TRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKEVPRRKS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  185 SVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQPELWSAEFNDFI 264
Cdd:cd06648   163 LVGTPYWMAPEVISRL-----PYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEPPKLKNLHKVSPRLRSFL 237
                         250       260
                  ....*....|....*....|...
gi 767960106  265 SKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06648   238 DRMLVRDPAQRATAAELLNHPFL 260
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
20-287 1.39e-64

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 220.35  E-value: 1.39e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   20 TWEITETIGKGTYGKVFKVLNKKNGQKAAVK----ILDPIHDID--EEIEAEYNILKALSdHPNVVRFYGIyfkkdKVNG 93
Cdd:cd06632     1 RWQKGQLLGSGSFGSVYEGFNGDTGDFFAVKevslVDDDKKSREsvKQLEQEIALLSKLR-HPNIVQYYGT-----EREE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   94 DKLWLVLELCSGGSVTDLVKGFlkrgERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSA 173
Cdd:cd06632    75 DNLYIFLEYVPGGSIHKLLQRY----GAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  174 QLTSTRHRRnTSVGTPFWMAPEVIAceqQLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNP--PPKlr 251
Cdd:cd06632   151 HVEAFSFAK-SFKGSPYWMAPEVIM---QKNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGelPPI-- 224
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767960106  252 qPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06632   225 -PDHLSPDAKDFIRLCLQRDPEDRPTASQLLEHPFV 259
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
27-289 4.08e-64

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 218.86  E-value: 4.08e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILD----PIHDIDEEIEAEYNILKALSdHPNVVRFYGIYFKKDKVngdklWLVLEL 102
Cdd:cd06607     9 IGHGSFGAVYYARNKRTSEVVAIKKMSysgkQSTEKWQDIIKEVKFLRQLR-HPNTIEYKGCYLREHTA-----WLVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGgSVTDLVKgFLKRGERMSEplIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGvSAQLTSTrhrR 182
Cdd:cd06607    83 CLG-SASDIVE-VHKKPLQEVE--IAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFG-SASLVCP---A 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  183 NTSVGTPFWMAPEVIAC--EQQldttYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLrQPELWSAEF 260
Cdd:cd06607   155 NSFVGTPYWMAPEVILAmdEGQ----YDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNDSPTL-SSGEWSDDF 229
                         250       260
                  ....*....|....*....|....*....
gi 767960106  261 NDFISKCLTKDYEKRPTVSELLQHKFITQ 289
Cdd:cd06607   230 RNFVDSCLQKIPQDRPSAEDLLKHPFVTR 258
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
16-287 2.60e-61

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 212.28  E-value: 2.60e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVRFYGIYFKkdkvnGDK 95
Cdd:cd06654    17 DPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLV-----GDE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSGGSVTDLVKGFLkrgerMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL 175
Cdd:cd06654    92 LWVVMEYLAGGSLTDVVTETC-----MDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQI 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTRHRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQPEL 255
Cdd:cd06654   167 TPEQSKRSTMVGTPYWMAPEVVT-----RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEK 241
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767960106  256 WSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06654   242 LSAIFRDFLNRCLEMDVEKRGSAKELLQHQFL 273
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
22-287 3.77e-61

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 210.40  E-value: 3.77e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKILDpIHDIDE----EIEAEYNILKALsDHPNVVRFYGIYFKKDKVNgdklw 97
Cdd:cd08215     3 EKIRVIGKGSFGSAYLVRRKSDGKLYVLKEID-LSNMSEkereEALNEVKLLSKL-KHPNIVKYYESFEENGKLC----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 177
Cdd:cd08215    76 IVMEYADGGDLAQKIKKQKKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLES 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  178 TRHRRNTSVGTPFWMAPEViaCEQQldtTYDARCDTWSLGITAIELGDGDPPLaDLHPMRALF-KIPRNPPPKLrqPELW 256
Cdd:cd08215   156 TTDLAKTVVGTPYYLSPEL--CENK---PYNYKSDIWALGCVLYELCTLKHPF-EANNLPALVyKIVKGQYPPI--PSQY 227
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767960106  257 SAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd08215   228 SSELRDLVNSMLQKDPEKRPSANEILSSPFI 258
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
16-287 9.57e-61

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 210.73  E-value: 9.57e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVRFYGIYFKkdkvnGDK 95
Cdd:cd06656    16 DPKKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLV-----GDE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSGGSVTDLVKGFLkrgerMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL 175
Cdd:cd06656    91 LWVVMEYLAGGSLTDVVTETC-----MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTRHRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQPEL 255
Cdd:cd06656   166 TPEQSKRSTMVGTPYWMAPEVVT-----RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPER 240
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767960106  256 WSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06656   241 LSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 272
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
22-291 1.28e-59

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 206.04  E-value: 1.28e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKIldpIH-DIDEEIEAEynILKAL-----SDHPNVVRFYGIYFkkdkVNGDk 95
Cdd:cd06605     4 EYLGELGEGNGGVVSKVRHRPSGQIMAVKV---IRlEIDEALQKQ--ILRELdvlhkCNSPYIVGFYGAFY----SEGD- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNN-KTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:cd06605    74 ISICMEYMDGGSLDK----ILKEVGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQVKLCDFGVSGQ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LTSTRhrRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDG----DPPLADLHPM--RALFKIPRNPPP 248
Cdd:cd06605   150 LVDSL--AKTFVGTRSYMAPERISGGK-----YTVKSDIWSLGLSLVELATGrfpyPPPNAKPSMMifELLSYIVDEPPP 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 767960106  249 KLRQPElWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQIE 291
Cdd:cd06605   223 LLPSGK-FSPDFQDFVSQCLQKDPTERPSYKELMEHPFIKRYE 264
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
16-287 1.90e-59

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 206.88  E-value: 1.90e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEE-IEAEYNILKALSDhPNVVRFYGIYFKkdkvnGD 94
Cdd:cd06655    16 DPKKKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKElIINEILVMKELKN-PNIVNFLDSFLV-----GD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 KLWLVLELCSGGSVTDLVKGFLkrgerMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:cd06655    90 ELFVVMEYLAGGSLTDVVTETC-----MDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQ 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LTSTRHRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQPE 254
Cdd:cd06655   165 ITPEQSKRSTMVGTPYWMAPEVVT-----RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPE 239
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767960106  255 LWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06655   240 KLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFL 272
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
27-287 5.76e-57

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 198.55  E-value: 5.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKIL-------------------DPIHDIDEEIEaeynILKALsDHPNVVRFYGIYfk 87
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIFnksrlrkrregkndrgkikNALDDVRREIA----IMKKL-DHPNIVRLYEVI-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   88 kDKVNGDKLWLVLELCSGGSVTDLVKGflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLV 167
Cdd:cd14008    74 -DDPESDKLYLVLEYCEGGPVMELDSG--DRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKIS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  168 DFGVSAQLTSTRHRRNTSVGTPFWMAPEviACeQQLDTTYDAR-CDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNP 246
Cdd:cd14008   151 DFGVSEMFEDGNDTLQKTAGTPAFLAPE--LC-DGDSKTYSGKaADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQN 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767960106  247 PPKLRQPELwSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14008   228 DEFPIPPEL-SPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
21-283 1.53e-56

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 197.04  E-value: 1.53e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEI----EAEYNILKALSdHPNVVRFYGIYFkkdkvNGDKL 96
Cdd:cd14014     2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFrerfLREARALARLS-HPNIVRVYDVGE-----DDGRP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:cd14014    76 YIVMEYVEGGSLADL----LRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRHRR-NTSVGTPFWMAPeviacEQQLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQ--P 253
Cdd:cd14014   152 DSGLTQtGSVLGTPAYMAP-----EQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPlnP 226
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767960106  254 ELwSAEFNDFISKCLTKDYEKRP-TVSELLQ 283
Cdd:cd14014   227 DV-PPALDAIILRALAKDPEERPqSAAELLA 256
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
16-287 2.64e-56

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 198.34  E-value: 2.64e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILD----PIHDIDEEIEAEYNILKALSdHPNVVRFYGIYFKKDKV 91
Cdd:cd06633    18 DPEEIFVDLHEIGHGSFGAVYFATNSHTNEVVAIKKMSysgkQTNEKWQDIIKEVKFLQQLK-HPNTIEYKGCYLKDHTA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   92 ngdklWLVLELCSGgSVTDLVKGFLKRgerMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGv 171
Cdd:cd06633    97 -----WLVMEYCLG-SASDLLEVHKKP---LQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  172 SAQLTSTrhrRNTSVGTPFWMAPEVIACEQQldTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLR 251
Cdd:cd06633   167 SASIASP---ANSFVGTPYWMAPEVILAMDE--GQYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQNDSPTLQ 241
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767960106  252 QPElWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06633   242 SNE-WTDSFRGFVDYCLQKIPQERPSSAELLRHDFV 276
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
20-287 3.13e-56

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 196.50  E-value: 3.13e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   20 TWEITETIGKGTYGKVFKVLNKKnGQKAAVK--ILDPIHDID-----EEIEAEYNILKALsDHPNVVRFYGIYFKKDKVN 92
Cdd:cd06631     2 QWKKGNVLGKGAYGTVYCGLTST-GQLIAVKqvELDTSDKEKaekeyEKLQEEVDLLKTL-KHVNIVGYLGTCLEDNVVS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   93 gdklwLVLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFG-- 170
Cdd:cd06631    80 -----IFMEFVPGGSIASI----LARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGca 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  171 --VSAQLTSTRHRR--NTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKI--PR 244
Cdd:cd06631   151 krLCINLSSGSQSQllKSMRGTPYWMAPEVIN-----ETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIgsGR 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 767960106  245 NPPPKLrqPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06631   226 KPVPRL--PDKFSPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
22-299 1.75e-55

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 195.33  E-value: 1.75e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITE--TIGKGTYGKVFKVLNKKNGQKAAVKIL--DPIHDIDEEIEAEYNILKALSdHPNVVRFYGIYFKKDKVNgdkLW 97
Cdd:cd06621     2 KIVElsSLGEGAGGSVTKCRLRNTKTIFALKTIttDPNPDVQKQILRELEINKSCA-SPYIVKYYGAFLDEQDSS---IG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 177
Cdd:cd06621    78 IAMEYCEGGSLDSIYKKVKKKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSGELVN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  178 TrhRRNTSVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELG--------DGDPPLAdlhPMRALFKIPRNPPPK 249
Cdd:cd06621   158 S--LAGTFTGTSYYMAPERIQGG-----PYSITSDVWSLGLTLLEVAqnrfpfppEGEPPLG---PIELLSYIVNMPNPE 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767960106  250 LRQ-PEL---WSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQIEGKDVMLQK 299
Cdd:cd06621   228 LKDePENgikWSESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKAQEKKKVNMAK 281
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
21-283 2.14e-55

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 201.39  E-value: 2.14e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEA----EYNILKALsDHPNVVRFYGiYFkkdkVNGDKL 96
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARErfrrEARALARL-NHPNIVRVYD-VG----EEDGRP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:COG0515    83 YLVMEYVEGESLADL----LRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRH-RRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQ--P 253
Cdd:COG0515   159 GATLtQTGTVVGTPGYMAPEQARGEP-----VDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSElrP 233
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767960106  254 ELwSAEFNDFISKCLTKDYEKRP-TVSELLQ 283
Cdd:COG0515   234 DL-PPALDAIVLRALAKDPEERYqSAAELAA 263
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
21-286 3.43e-55

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 193.08  E-value: 3.43e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILD--PIHDIDEE-IEAEYNILKALsDHPNVVRFYGIYfkkdkVNGDKLW 97
Cdd:cd05117     2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDkkKLKSEDEEmLRREIEILKRL-DHPNIVKLYEVF-----EDDKNLY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGsvtDLVKGFLKRGeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG---VKLVDFGVSAQ 174
Cdd:cd05117    76 LVMELCTGG---ELFDRIVKKG-SFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPdspIKIIDFGLAKI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LTSTRHRRnTSVGTPFWMAPEVIACeqqldTTYDARCDTWSLG-ITAIELGdGDPPLADLHPMRALFKIpRNPPPKLRQP 253
Cdd:cd05117   152 FEEGEKLK-TVCGTPYYVAPEVLKG-----KGYGKKCDIWSLGvILYILLC-GYPPFYGETEQELFEKI-LKGKYSFDSP 223
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767960106  254 ELW--SAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd05117   224 EWKnvSEEAKDLIKRLLVVDPKKRLTAAEALNHPW 258
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
27-284 4.37e-55

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 191.33  E-value: 4.37e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDPI--HDIDEEIEAEYNILKALsDHPNVVRFYGIYFKkdkvnGDKLWLVLELCS 104
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPKEklKKLLEELLREIEILKKL-NHPNIVKLYDVFET-----ENFLYLVMEYCE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  105 GGSVTDLVKgflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRRNT 184
Cdd:cd00180    75 GGSLKDLLK---ENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  185 SVGTPFWMAPEViacEQQLDTTYDARCDTWSLGITAIELgdgdppladlhpmralfkiprnpppklrqpelwsAEFNDFI 264
Cdd:cd00180   152 TGGTTPPYYAPP---ELLGGRYYGPKVDIWSLGVILYEL----------------------------------EELKDLI 194
                         250       260
                  ....*....|....*....|
gi 767960106  265 SKCLTKDYEKRPTVSELLQH 284
Cdd:cd00180   195 RRMLQYDPKKRPSAKELLEH 214
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
21-287 6.86e-55

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 192.52  E-value: 6.86e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILdPIHDID----EEIEAEYNILKALsDHPNVVRFYGIyfkkdKVNGDKL 96
Cdd:cd06626     2 WQRGNKIGEGTFGKVYTAVNLDTGELMAMKEI-RFQDNDpktiKEIADEMKVLEGL-DHPNLVRYYGV-----EVHREEV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:cd06626    75 YIFMEYCQEGTLEEL----LRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 ST-----RHRRNTSVGTPFWMAPEVIAceQQLDTTYDARCDTWSLGITAIELGDGDPPLADL-HPMRALFKIPRNPPPKL 250
Cdd:cd06626   151 NNtttmaPGEVNSLVGTPAYMAPEVIT--GNKGEGHGRAADIWSLGCVVLEMATGKRPWSELdNEWAIMYHVGMGHKPPI 228
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767960106  251 RQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06626   229 PDSLQLSPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
19-295 9.71e-54

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 189.94  E-value: 9.71e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEE--IEAEYNILKALSDHPNVVRFYGIYFKKdkvnGDkL 96
Cdd:cd06617     1 DDLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRATVNSQEQkrLLMDLDISMRSVDCPYTVTFYGALFRE----GD-V 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGgSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNN-KTIHRDVKGNNILLTTEGGVKLVDFGVSAQL 175
Cdd:cd06617    76 WICMEVMDT-SLDKFYKKVYDKGLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFGISGYL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTRhRRNTSVGTPFWMAPEVIACEQQlDTTYDARCDTWSLGITAIELGDGDPPLADLH-PMRALFKIPRNPPPKLRQpE 254
Cdd:cd06617   155 VDSV-AKTIDAGCKPYMAPERINPELN-QKGYDVKSDVWSLGITMIELATGRFPYDSWKtPFQQLKQVVEEPSPQLPA-E 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767960106  255 LWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQIEGKDV 295
Cdd:cd06617   232 KFSPEFQDFVNKCLKKNYKERPNYPELLQHPFFELHLSKNT 272
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
21-286 9.72e-54

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 188.88  E-value: 9.72e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILD---PIHDIDEEIEAEYNILKALsDHPNVVRFYGIYfkkdkVNGDKLW 97
Cdd:cd14003     2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDkskLKEEIEEKIKREIEIMKLL-NHPNIIKLYEVI-----ETENKIY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVTDLVKgflKRGeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAqlTS 177
Cdd:cd14003    76 LVMEYASGGELFDYIV---NNG-RLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSN--EF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  178 TRHRR-NTSVGTPFWMAPEVIACEQqldttYDAR-CDTWSLGITAIELGDGDPPLADlHPMRALF-KIPR---NPPPKLr 251
Cdd:cd14003   150 RGGSLlKTFCGTPAYAAPEVLLGRK-----YDGPkADVWSLGVILYAMLTGYLPFDD-DNDSKLFrKILKgkyPIPSHL- 222
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767960106  252 qpelwSAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd14003   223 -----SPDARDLIRRMLVVDPSKRITIEEILNHPW 252
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
16-289 3.18e-53

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 189.04  E-value: 3.18e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDidEEIEAEYNILKALSD--HPNVVRFYgiyfkKDKVNG 93
Cdd:cd06659    18 DPRQLLENYVKIGEGSTGVVCIAREKHSGRQVAVKMMDLRKQ--QRRELLFNEVVIMRDyqHPNVVEMY-----KSYLVG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   94 DKLWLVLELCSGGSVTDLVKGFlkrgeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSA 173
Cdd:cd06659    91 EELWVLMEYLQGGALTDIVSQT-----RLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  174 QLTSTRHRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQP 253
Cdd:cd06659   166 QISKDVPKRKSLVGTPYWMAPEVIS-----RCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPPPKLKNS 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767960106  254 ELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQ 289
Cdd:cd06659   241 HKASPVLRDFLERMLVRDPQERATAQELLDHPFLLQ 276
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
27-286 5.05e-52

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 183.87  E-value: 5.05e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDE-EIE---AEYNILKALsDHPNVVRFYgIYFKKDkvngDKLWLVLEL 102
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRkEVEhtlNERNILERV-NHPFIVKLH-YAFQTE----EKLYLVLDY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGsvtDLVKgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRR 182
Cdd:cd05123    75 VPGG---ELFS-HLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  183 NTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPLADlHPMRALF-KIPRNPppkLRQPELWSAEFN 261
Cdd:cd05123   151 YTFCGTPEYLAPEVL-----LGKGYGKAVDWWSLGVLLYEMLTGKPPFYA-ENRKEIYeKILKSP---LKFPEYVSPEAK 221
                         250       260
                  ....*....|....*....|....*...
gi 767960106  262 DFISKCLTKDYEKRPT---VSELLQHKF 286
Cdd:cd05123   222 SLISGLLQKDPTKRLGsggAEEIKAHPF 249
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
22-287 4.37e-51

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 181.59  E-value: 4.37e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEE---IEAEYNILKALSdHPNVVRFYGIYFKKDKvngDKLWL 98
Cdd:cd08217     3 EVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEKEkqqLVSEVNILRELK-HPNIVRYYDRIVDRAN---TTLYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   99 VLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHN-----NKTIHRDVKGNNILLTTEGGVKLVDFGVSA 173
Cdd:cd08217    79 VMEYCEGGDLAQLIKKCKKENQYIPEEFIWKIFTQLLLALYECHNrsvggGKILHRDLKPANIFLDSDNNVKLGDFGLAR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  174 QLTSTRHRRNTSVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPP-LADLHPMRALfKIPRNPPPKLrq 252
Cdd:cd08217   159 VLSHDSSFAKTYVGTPYYMSPELLNEQ-----SYDEKSDIWSLGCLIYELCALHPPfQAANQLELAK-KIKEGKFPRI-- 230
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767960106  253 PELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd08217   231 PSRYSSELNEVIKSMLNVDPDKRPSVEELLQLPLI 265
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
22-288 1.06e-50

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 179.98  E-value: 1.06e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKIL--------DPIHDIDEEIEAEYNIlkalsDHPNVVRFYGIYFKKDKVng 93
Cdd:cd14007     3 EIGKPLGKGKFGNVYLAREKKSGFIVALKVIsksqlqksGLEHQLRREIEIQSHL-----RHPNILRLYGYFEDKKRI-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   94 dklWLVLELCSGGSVTDLvkgfLKRGERMSEPLIA-YILHEALmGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS 172
Cdd:cd14007    76 ---YLILEYAPNGELYKE----LKKQKRFDEKEAAkYIYQLAL-ALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWS 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLTStrHRRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRnppPKLRQ 252
Cdd:cd14007   148 VHAPS--NRRKTFCGTLDYLPPEMVEGKE-----YDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQN---VDIKF 217
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767960106  253 PELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFIT 288
Cdd:cd14007   218 PSSVSPEAKDLISKLLQKDPSKRLSLEQVLNHPWIK 253
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
21-287 5.78e-50

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 178.32  E-value: 5.78e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDE---EIEA---EYNILKALsDHPNVVRFYGIyfKKDKvngD 94
Cdd:cd06625     2 WKQGKLLGQGAFGQVYLCYDADTGRELAVKQVEIDPINTEaskEVKAlecEIQLLKNL-QHERIVQYYGC--LQDE---K 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 KLWLVLELCSGGSVTDLVKgflKRGErMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:cd06625    76 SLSIFMEYMPGGSVKDEIK---AYGA-LTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LTSTRHRRNTS--VGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPP-PKLr 251
Cdd:cd06625   152 LQTICSSTGMKsvTGTPYWMSPEVINGE-----GYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIATQPTnPQL- 225
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767960106  252 qPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06625   226 -PPHVSEDARDFLSLIFVRNKKQRPSAEELLSHSFV 260
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
16-298 7.89e-50

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 179.83  E-value: 7.89e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILD----PIHDIDEEIEAEYNILKALSdHPNVVRFYGIYFKKDKV 91
Cdd:cd06634    12 DPEKLFSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSysgkQSNEKWQDIIKEVKFLQKLR-HPNTIEYRGCYLREHTA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   92 ngdklWLVLELCSGgSVTDLVKGFLKRgerMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGV 171
Cdd:cd06634    91 -----WLVMEYCLG-SASDLLEVHKKP---LQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  172 SAQLTSTrhrrNTSVGTPFWMAPEVIACEQQldTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLr 251
Cdd:cd06634   162 ASIMAPA----NSFVGTPYWMAPEVILAMDE--GQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPAL- 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767960106  252 QPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQIEGKDVMLQ 298
Cdd:cd06634   235 QSGHWSEYFRNFVDSCLQKIPQDRPTSDVLLKHRFLLRERPPTVIMD 281
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
16-297 9.30e-50

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 179.86  E-value: 9.30e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDpiHDIDEEIEAEYNILKALS-----DHPNVVRFYGIYFKKDK 90
Cdd:cd06635    22 DPEKLFSDLREIGHGSFGAVYFARDVRTSEVVAIKKMS--YSGKQSNEKWQDIIKEVKflqriKHPNSIEYKGCYLREHT 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   91 VngdklWLVLELCSGgSVTDLVKGFLKRgerMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFG 170
Cdd:cd06635   100 A-----WLVMEYCLG-SASDLLEVHKKP---LQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  171 vSAQLTSTrhrRNTSVGTPFWMAPEVIACEQQldTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKL 250
Cdd:cd06635   171 -SASIASP---ANSFVGTPYWMAPEVILAMDE--GQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPTL 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767960106  251 RQPElWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQIEGKDVML 297
Cdd:cd06635   245 QSNE-WSDYFRNFVDSCLQKIPQDRPTSEELLKHMFVLRERPETVLI 290
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
27-287 1.96e-49

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 176.96  E-value: 1.96e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILD-PIHDID---------EEIEAEYNILKALSdHPNVVRFYGiyfkkDKVNGDKL 96
Cdd:cd06628     8 IGSGSFGSVYLGMNASSGELMAVKQVElPSVSAEnkdrkksmlDALQREIALLRELQ-HENIVQYLG-----SSSDANHL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLVKGFlkrGErMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL- 175
Cdd:cd06628    82 NIFLEYVPGGSVATLLNNY---GA-FEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLe 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 -----TSTRHRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKL 250
Cdd:cd06628   158 anslsTKNNGARPSLQGSVFWMAPEVVK-----QTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIGENASPTI 232
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767960106  251 rqPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06628   233 --PSNISSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
27-283 8.26e-49

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 174.26  E-value: 8.26e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVlnKKNGQKAAVKILDPIHDIDEEIEA---EYNILKALSdHPNVVRFYGIYfkkdkVNGDKLWLVLELC 103
Cdd:cd13999     1 IGSGSFGEVYKG--KWRGTDVAIKKLKVEDDNDELLKEfrrEVSILSKLR-HPNIVQFIGAC-----LSPPPLCIVTEYM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  104 SGGSVTDLVKgflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRRN 183
Cdd:cd13999    73 PGGSLYDLLH---KKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  184 TSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQPELWSaEFNDF 263
Cdd:cd13999   150 GVVGTPRWMAPEVL-----RGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLRPPIPPDCPP-ELSKL 223
                         250       260
                  ....*....|....*....|
gi 767960106  264 ISKCLTKDYEKRPTVSELLQ 283
Cdd:cd13999   224 IKRCWNEDPEKRPSFSEIVK 243
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
21-287 1.04e-48

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 174.88  E-value: 1.04e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILD-PIHDID----------EEIEAEYNILKALsDHPNVVRFYGiYFKKD 89
Cdd:cd06629     3 WVKGELIGKGTYGRVYLAMNATTGEMLAVKQVElPKTSSDradsrqktvvDALKSEIDTLKDL-DHPNIVQYLG-FEETE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   90 KVngdkLWLVLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDF 169
Cdd:cd06629    81 DY----FSIFLEYVPGGSIGSC----LRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  170 GVS--AQLTSTRHRRNTSVGTPFWMAPEVIACEQQldtTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKI--PRN 245
Cdd:cd06629   153 GISkkSDDIYGNNGATSMQGSVFWMAPEVIHSQGQ---GYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLgnKRS 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 767960106  246 PPPklrQPE--LWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06629   230 APP---VPEdvNLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
22-284 1.17e-48

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 174.22  E-value: 1.17e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    22 EITETIGKGTYGKVF----KVLNKKNGQKAAVKILDPIHDID--EEIEAEYNILKALsDHPNVVRFYGIYfkkdkVNGDK 95
Cdd:pfam07714    2 TLGEKLGEGAFGEVYkgtlKGEGENTKIKVAVKTLKEGADEEerEDFLEEASIMKKL-DHPNIVKLLGVC-----TQGEP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    96 LWLVLELCSGGSVTDlvkgFL-KRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:pfam07714   76 LYIVTEYMPGGDLLD----FLrKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRD 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   175 LTSTRHRRNTSVGT--PFWMAPEVIAceqqlDTTYDARCDTWSLGITAIEL-GDGDPPLADLHPMRALFKIPRNppPKLR 251
Cdd:pfam07714  152 IYDDDYYRKRGGGKlpIKWMAPESLK-----DGKFTSKSDVWSFGVLLWEIfTLGEQPYPGMSNEEVLEFLEDG--YRLP 224
                          250       260       270
                   ....*....|....*....|....*....|...
gi 767960106   252 QPELWSAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:pfam07714  225 QPENCPDELYDLMKQCWAYDPEDRPTFSELVED 257
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
21-283 1.03e-47

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 171.44  E-value: 1.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDpIHDID----EEIEAEYNILKALsDHPNVVRFYGIYfkkdkVNGDKL 96
Cdd:cd08529     2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQID-ISRMSrkmrEEAIDEARVLSKL-NSPYVIKYYDSF-----VDKGKL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLVKGflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:cd08529    75 NIVMEYAENGDLHSLIKS--QRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRHRRNTSVGTPFWMAPEViaCEqqlDTTYDARCDTWSLGITAIELGDGDppladlHPMRA------LFKIPRNPPPKL 250
Cdd:cd08529   153 DTTNFAQTIVGTPYYLSPEL--CE---DKPYNEKSDVWALGCVLYELCTGK------HPFEAqnqgalILKIVRGKYPPI 221
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767960106  251 RQPelWSAEFNDFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd08529   222 SAS--YSQDLSQLIDSCLTKDYRQRPDTTELLR 252
Pkinase pfam00069
Protein kinase domain;
21-287 1.55e-47

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 169.73  E-value: 1.55e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEA---EYNILKALSdHPNVVRFYGIYfkkdkVNGDKLW 97
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNilrEIKILKKLN-HPNIVRLYDAF-----EDKDNLY 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    98 LVLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLqhlhnnktihrdvkgnnillttEGGVKLVDFgvsaqlts 177
Cdd:pfam00069   75 LVLEYVEGGSLFDL----LSEKGAFSEREAKFIMKQILEGL----------------------ESGSSLTTF-------- 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   178 trhrrntsVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQPELWS 257
Cdd:pfam00069  121 --------VGTPWYMAPEVLGGNP-----YGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSNLS 187
                          250       260       270
                   ....*....|....*....|....*....|
gi 767960106   258 AEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:pfam00069  188 EEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
16-287 1.21e-46

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 169.83  E-value: 1.21e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVRFYGIYFKkdkvnGDK 95
Cdd:cd06658    19 DPREYLDSFIKIGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLV-----GDE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSGGSVTDLVKGflkrgERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL 175
Cdd:cd06658    94 LWVVMEFLEGGALTDIVTH-----TRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTRHRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQPEL 255
Cdd:cd06658   169 SKEVPKRKSLVGTPYWMAPEVIS-----RLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNLPPRVKDSHK 243
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767960106  256 WSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06658   244 VSSVLRGFLDLMLVREPSQRATAQELLQHPFL 275
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
27-287 1.58e-45

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 165.42  E-value: 1.58e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDP----IHDIDEEIEAEYNILKALsDHPNVVRFYGIYFKKDKVngdklWLVLEL 102
Cdd:cd14099     9 LGKGGFAKCYEVTDMSTGKVYAGKVVPKssltKPKQREKLKSEIKIHRSL-KHPNIVKFHDCFEDEENV-----YILLEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRR 182
Cdd:cd14099    83 CSNGSLMEL----LKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGERK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  183 NTSVGTPFWMAPEVIACEQqldtTYDARCDTWSLGITAIELGDGDPPL--ADLHPM-----RALFKIPRNPPpklrqpel 255
Cdd:cd14099   159 KTLCGTPNYIAPEVLEKKK----GHSFEVDIWSLGVILYTLLVGKPPFetSDVKETykrikKNEYSFPSHLS-------- 226
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767960106  256 WSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14099   227 ISDEAKDLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
16-289 1.68e-45

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 166.74  E-value: 1.68e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVRFYGIYFKkdkvnGDK 95
Cdd:cd06657    17 DPRTYLDNFIKIGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLV-----GDE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSGGSVTDLVKGflkrgERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL 175
Cdd:cd06657    92 LWVVMEFLEGGALTDIVTH-----TRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTRHRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQPEL 255
Cdd:cd06657   167 SKEVPRRKSLVGTPYWMAPELIS-----RLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPKLKNLHK 241
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767960106  256 WSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQ 289
Cdd:cd06657   242 VSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAK 275
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
22-287 8.61e-45

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 162.79  E-value: 8.61e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSD---HPNVVRFYGIYFKKdkvNGDKLWL 98
Cdd:cd05118     2 EVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKAALREIKLLKHLNDvegHPNIVKLLDVFEHR---GGNHLCL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   99 VLELCsGGSVTDLVKgflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG-VKLVDFGVSAQLTS 177
Cdd:cd05118    79 VFELM-GMNLYELIK---DYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGqLKLADFGLARSFTS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  178 TRHrrNTSVGTPFWMAPEVIACEQQldttYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRnpppklrqpELWS 257
Cdd:cd05118   155 PPY--TPYVATRWYRAPEVLLGAKP----YGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVR---------LLGT 219
                         250       260       270
                  ....*....|....*....|....*....|
gi 767960106  258 AEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd05118   220 PEALDLLSKMLKYDPAKRITASQALAHPYF 249
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
19-303 2.26e-44

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 163.10  E-value: 2.26e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDpiHDIDE----EIEAEYNIL-KALSdhPNVVRFYGIYFKKDKVng 93
Cdd:cd06622     1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIR--LELDEskfnQIIMELDILhKAVS--PYIVDFYGAFFIEGAV-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   94 dklWLVLELCSGGSVTDLVKGFLKRGeRMSEPLIAYILHEALMGLQHL---HNnkTIHRDVKGNNILLTTEGGVKLVDFG 170
Cdd:cd06622    75 ---YMCMEYMDAGSLDKLYAGGVATE-GIPEDVLRRITYAVVKGLKFLkeeHN--IIHRDVKPTNVLVNGNGQVKLCDFG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  171 VSAQLTSTRHRrnTSVGTPFWMAPEVIACEQQLDT-TYDARCDTWSLGITAIELGDGD---PPLADLHPMRALFKIPRNP 246
Cdd:cd06622   149 VSGNLVASLAK--TNIGCQSYMAPERIKSGGPNQNpTYTVQSDVWSLGLSILEMALGRypyPPETYANIFAQLSAIVDGD 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767960106  247 PPKLrqPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQIEGKDVMLQKQLTE 303
Cdd:cd06622   227 PPTL--PSGYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLVKYKNADVDMAEWVTG 281
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
27-295 1.54e-43

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 160.99  E-value: 1.54e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIE--AEYNILKALSDHPNVVRFYGIYFKKdkvnGDkLWLVLELCS 104
Cdd:cd06616    14 IGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDEKEQKRllMDLDVVMRSSDCPYIVKFYGALFRE----GD-CWICMELMD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  105 GgSVTDLVK-GFLKRGERMSEPLIAYILHEALMGLQHLHNN-KTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRhRR 182
Cdd:cd06616    89 I-SLDKFYKyVYEVLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGNIKLCDFGISGQLVDSI-AK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  183 NTSVGTPFWMAPEVIACEQQLDtTYDARCDTWSLGITAIELGDGDPPLADLHPM-RALFKIPRNPPPKLRQPE--LWSAE 259
Cdd:cd06616   167 TRDAGCRPYMAPERIDPSASRD-GYDVRSDVWSLGITLYEVATGKFPYPKWNSVfDQLTQVVKGDPPILSNSEerEFSPS 245
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767960106  260 FNDFISKCLTKDYEKRPTVSELLQHKFITQIEGKDV 295
Cdd:cd06616   246 FVNFVNLCLIKDESKRPKYKELLKHPFIKMYEERNV 281
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
27-287 6.86e-43

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 158.34  E-value: 6.86e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILdPIHDIDE--EIEAEYNILKALSdHPNVVRFYGI-----YFKkdkvngdklwLV 99
Cdd:cd06624    16 LGKGTFGVVYAARDLSTQVRIAIKEI-PERDSREvqPLHEEIALHSRLS-HKNIVQYLGSvsedgFFK----------IF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  100 LELCSGGSVTDLVK---GFLKRgermSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTT-EGGVKLVDFGVSAQL 175
Cdd:cd06624    84 MEQVPGGSLSALLRskwGPLKD----NENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTSKRL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTRHRRNTSVGTPFWMAPEVIACEQQldtTYDARCDTWSLGITAIELGDGDPPLADL-HPMRALFKI---PRNPPPklr 251
Cdd:cd06624   160 AGINPCTETFTGTLQYMAPEVIDKGQR---GYGPPADIWSLGCTIIEMATGKPPFIELgEPQAAMFKVgmfKIHPEI--- 233
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767960106  252 qPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd06624   234 -PESLSEEAKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
22-284 2.72e-41

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 153.32  E-value: 2.72e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALS--DHPNVVRFYGIYFkkdkvNGDKLWLV 99
Cdd:cd08530     3 KVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKEREDSVNEIRLLAsvNHPNIIRYKEAFL-----DGNRLCIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  100 LELCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLtsTR 179
Cdd:cd08530    78 MEYAPFGDLSKLISKRKKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVL--KK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  180 HRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPP-----LADLHpmralFKIPRNPPPKLrqPE 254
Cdd:cd08530   156 NLAKTQIGTPLYAAPEVWK-----GRPYDYKSDIWSLGCLLYEMATFRPPfeartMQELR-----YKVCRGKFPPI--PP 223
                         250       260       270
                  ....*....|....*....|....*....|
gi 767960106  255 LWSAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd08530   224 VYSQDLQQIIRSLLQVNPKKRPSCDKLLQS 253
MYSc_Myo24B cd14938
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
353-1040 4.88e-41

class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276898 [Multi-domain]  Cd Length: 713  Bit Score: 163.08  E-value: 4.88e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  353 TVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYigsKRTASPPHI------FAMADLGYQSMITYNsdQC 426
Cdd:cd14938     2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKY---KCIDCIEDLslneyhVVHNALKNLNELKRN--QS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  427 IVISGESGAGKTE-----------------------NAHLLVQQLTVLGKANNRTLQEKILQVNNLVEAFGNACTIINDN 483
Cdd:cd14938    77 IIISGESGSGKSEiakniinfiayqvkgsrrlptnlNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  484 SSRFGKYLEMKFTSSgAVVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGLAEK-KKLAHYKLPENKppRYLQNDHLR 562
Cdd:cd14938   157 SSRFSKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKfKKMYFLKNIENY--SMLNNEKGF 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  563 TvqdimNNSFYKSQYELIEQCFKVIGFTMEQLGSIYSILAAILNVGNIEF-------SSVATEHQ-----IDKSHISNHT 630
Cdd:cd14938   234 E-----KFSDYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIvkafrkkSLLMGKNQcgqniNYETILSELE 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  631 ALEN------------CASLLCIRADELQEALTSHCVVTRgETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLL 698
Cdd:cd14938   309 NSEDigldenvknlllACKLLSFDIETFVKYFTTNYIFND-SILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKC 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  699 KHDSSPSGNGDElsIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVFAWEQNEYlNED--VDARVIEYEDNWPLL 776
Cdd:cd14938   388 TQLQNININTNY--INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSY-NEDgiFCEYNSENIDNEPLY 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  777 DMFLQKPMGLLSLLDEESRFPKATDQ-----TLVEKFEGNlkSQYFWRPKRMEL--SFGIHHYAGKVLYNASGFLAKNRD 849
Cdd:cd14938   465 NLLVGPTEGSLFSLLENVSTKTIFDKsnlhsSIIRKFSRN--SKYIKKDDITGNkkTFVITHSCGDIIYNAENFVEKNID 542
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  850 TLPTDIVLLLRSSDNSVIRQL-VNHPLTKTGNLPHSKTKnvinYQMRTSEKLInlakgdtgeatrhaRETTNMKTQTVAS 928
Cdd:cd14938   543 ILTNRFIDMVKQSENEYMRQFcMFYNYDNSGNIVEEKRR----YSIQSALKLF--------------KRRYDTKNQMAVS 604
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  929 YFRYSLMDLLSKMVVGQPHFVRCIKPN-SERQARKYDKEKVLLQLRYTGILETARIRRLGFSHRILFANFIKRYYLL--C 1005
Cdd:cd14938   605 LLRNNLTELEKLQETTFCHFIVCMKPNeSKRELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKneD 684
                         730       740       750
                  ....*....|....*....|....*....|....*
gi 767960106 1006 YKSSEEPRMspdtcatILEKAGLDNWALGKTKVFL 1040
Cdd:cd14938   685 LKEKVEALI-------KSYQISNYEWMIGNNMIFL 712
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
22-298 1.00e-40

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 152.59  E-value: 1.00e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKIldpIHdIDEEIEAEYNILKALS-----DHPNVVRFYGIYFKKdkvNGDkL 96
Cdd:cd06620     8 ETLKDLGAGNGGSVSKVLHIPTGTIMAKKV---IH-IDAKSSVRKQILRELQilhecHSPYIVSFYGAFLNE---NNN-I 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVtdlvKGFLKRGERMSEPLIAYILHEALMGLQHLHN-NKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL 175
Cdd:cd06620    80 IICMEYMDCGSL----DKILKKKGPFPEEVLGKIAVAVLEGLTYLYNvHRIIHRDIKPSNILVNSKGQIKLCDFGVSGEL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTrhRRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPLAD--------LHPM---RALFKIPR 244
Cdd:cd06620   156 INS--IADTFVGTSTYMSPERIQGGK-----YSVKSDVWSLGLSIIELALGEFPFAGsnddddgyNGPMgilDLLQRIVN 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  245 NPPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHK-FITQIEGKDVMLQ 298
Cdd:cd06620   229 EPPPRLPKDRIFPKDLRDFVDRCLLKDPRERPSPQLLLDHDpFIQAVRASDVDLR 283
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
27-288 1.37e-40

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 151.74  E-value: 1.37e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKV-------------FKVLNKK---------------NGQKAAVKILDPIHDIDEEIeaeyNILKALsDHPNV 78
Cdd:cd14118     2 IGKGSYGIVklayneedntlyaMKILSKKkllkqagffrrppprRKPGALGKPLDPLDRVYREI----AILKKL-DHPNV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   79 VRFYGIYfkkDKVNGDKLWLVLELCSGGSV----TDlvkgflkrgERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGN 154
Cdd:cd14118    77 VKLVEVL---DDPNEDNLYMVFELVDKGAVmevpTD---------NPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  155 NILLTTEGGVKLVDFGVSAQLTSTRHRRNTSVGTPFWMAPEVIACEQQldtTYDARC-DTWSLGITAIELGDGDPPLADL 233
Cdd:cd14118   145 NLLLGDDGHVKIADFGVSNEFEGDDALLSSTAGTPAFMAPEALSESRK---KFSGKAlDIWAMGVTLYCFVFGRCPFEDD 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767960106  234 HPMrALFKIPRNPPPKL-RQPELwSAEFNDFISKCLTKDYEKRPTVSELLQHKFIT 288
Cdd:cd14118   222 HIL-GLHEKIKTDPVVFpDDPVV-SEQLKDLILRMLDKNPSERITLPEIKEHPWVT 275
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
22-295 1.37e-40

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 152.53  E-value: 1.37e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDE--EIEAEYNILKALSDHPNVVRFYGIYFKKDKVngdklWLV 99
Cdd:cd06618    18 ENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGNKEEnkRILMDLDVVLKSHDCPYIVKCYGYFITDSDV-----FIC 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  100 LELCSggsvTDLVKgfLKRgeRMSEPL-------IAYILHEALMGLQHLHNnkTIHRDVKGNNILLTTEGGVKLVDFGVS 172
Cdd:cd06618    93 MELMS----TCLDK--LLK--RIQGPIpedilgkMTVSIVKALHYLKEKHG--VIHRDVKPSNILLDESGNVKLCDFGIS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLTSTRhRRNTSVGTPFWMAPEVIacEQQLDTTYDARCDTWSLGITAIELGDGDPPLADLH-PMRALFKIPRNPPPKLR 251
Cdd:cd06618   163 GRLVDSK-AKTRSAGCAAYMAPERI--DPPDNPKYDIRADVWSLGISLVELATGQFPYRNCKtEFEVLTKILNEEPPSLP 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 767960106  252 QPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQIEGKDV 295
Cdd:cd06618   240 PNEGFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIRRYETAEV 283
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
25-284 1.43e-40

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 151.15  E-value: 1.43e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFK-VLNKKNGQK--AAVKILDPIHDIDE--EIEAEYNILKALsDHPNVVRFYGIYFKKDKvngdkLWLV 99
Cdd:cd00192     1 KKLGEGAFGEVYKgKLKGGDGKTvdVAVKTLKEDASESErkDFLKEARVMKKL-GHPNVVRLLGVCTEEEP-----LYLV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  100 LELCSGGsvtDLvKGFLKR---------GERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFG 170
Cdd:cd00192    75 MEYMEGG---DL-LDFLRKsrpvfpspePSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  171 VSAQLTSTRHRRNTSvGTPF---WMAPEVIaceqqLDTTYDARCDTWSLGITAIELG-DGDPPLADLHPMRALFKIPRNP 246
Cdd:cd00192   151 LSRDIYDDDYYRKKT-GGKLpirWMAPESL-----KDGIFTSKSDVWSFGVLLWEIFtLGATPYPGLSNEEVLEYLRKGY 224
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767960106  247 ppKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd00192   225 --RLPKPENCPDELYELMLSCWQLDPEDRPTFSELVER 260
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
21-287 1.30e-39

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 148.63  E-value: 1.30e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKIL--DP-IHDIDEEI---EAEYNILKALSdHPNVVRFYGIYFKKDKvngD 94
Cdd:cd06653     4 WRLGKLLGRGAFGEVYLCYDADTGRELAVKQVpfDPdSQETSKEVnalECEIQLLKNLR-HDRIVQYYGCLRDPEE---K 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 KLWLVLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHealmGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:cd06653    80 KLSIFVEYMPGGSVKDQLKAYGALTENVTRRYTRQILQ----GVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LtSTRHRRNTSV----GTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPP-PK 249
Cdd:cd06653   156 I-QTICMSGTGIksvtGTPYWMSPEVISGE-----GYGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIATQPTkPQ 229
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767960106  250 LrqPELWSAEFNDFISKCLTKDyEKRPTVSELLQHKFI 287
Cdd:cd06653   230 L--PDGVSDACRDFLRQIFVEE-KRRPTAEFLLRHPFV 264
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
27-286 2.35e-39

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 147.37  E-value: 2.35e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDpIHDID----EEIEAEYNILKALsDHPNVVRFYGIyfKKDKvngDKLWLVLEL 102
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEIS-RKKLNkklqENLESEIAILKSI-KHPNIVRLYDV--QKTE---DFIYLVLEY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGsvtDLVKgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG---VKLVDFGVSaqltstR 179
Cdd:cd14009    74 CAGG---DLSQ-YIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDdpvLKIADFGFA------R 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  180 HRRNTSV-----GTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPL-ADLHP------MRALFKIPRNPP 247
Cdd:cd14009   144 SLQPASMaetlcGSPLYMAPEILQFQK-----YDAKADLWSVGAILFEMLVGKPPFrGSNHVqllrniERSDAVIPFPIA 218
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767960106  248 PKLrqpelwSAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd14009   219 AQL------SPDCKDLLRRLLRRDPAERISFEEFFAHPF 251
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
22-286 2.46e-38

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 145.78  E-value: 2.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKILDpIHDIDEE--IEA--EYNILKALsDHPNVVRFYGIYFKKDKVNGDK-L 96
Cdd:cd07840     2 EKIAQIGEGTYGQVYKARNKKTGELVALKKIR-MENEKEGfpITAirEIKLLQKL-DHPNVVRLKEIVTSKGSAKYKGsI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSggsvTDLvKGFLKRGE-RMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL 175
Cdd:cd07840    80 YMVFEYMD----HDL-TGLLDNPEvKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLARPY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTRHRRNTS-VGTPFWMAPEVIACEqqldTTYDARCDTWSLGITAIELGDGDPPL------------------------ 230
Cdd:cd07840   155 TKENNADYTNrVITLWYRPPELLLGA----TRYGPEVDMWSVGCILAELFTGKPIFqgkteleqlekifelcgspteenw 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  231 --ADLHPMRALFKIPRNPPPKLRQ--PELWSAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd07840   231 pgVSDLPWFENLKPKKPYKRRLREvfKNVIDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
19-287 2.61e-38

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 144.32  E-value: 2.61e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEA---EYNILKALsDHPNVVRFYGiYFKKDKvngdk 95
Cdd:cd14002     1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELRNlrqEIEILRKL-NHPNIIEMLD-SFETKK----- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 lwlvlELCSggsVTDLVKG----FLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGV 171
Cdd:cd14002    74 -----EFVV---VTEYAQGelfqILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGF 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  172 SAQLTStrhrrNTSV-----GTPFWMAPEVIAcEQqldtTYDARCDTWSLGITAIELGDGDPP-----LADLHPMralfk 241
Cdd:cd14002   146 ARAMSC-----NTLVltsikGTPLYMAPELVQ-EQ----PYDHTADLWSLGCILYELFVGQPPfytnsIYQLVQM----- 210
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767960106  242 IPRNPppkLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14002   211 IVKDP---VKWPSNMSPEFKSFLQGLLNKDPSKRLSWPDLLEHPFV 253
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
22-283 2.85e-38

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 144.60  E-value: 2.85e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106     22 EITETIGKGTYGKVFK----VLNKKNGQKAAVKILDPIHDID--EEIEAEYNILKALsDHPNVVRFYGIYFKkdkvnGDK 95
Cdd:smart00219    2 TLGKKLGEGAFGEVYKgklkGKGGKKKVEVAVKTLKEDASEQqiEEFLREARIMRKL-DHPNVVKLLGVCTE-----EEP 75
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106     96 LWLVLELCSGGSVtdlvKGFL-KRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:smart00219   76 LYIVMEYMEGGDL----LSYLrKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRD 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    175 LTSTRHRRNTSVGTP-FWMAPEVIaceqqLDTTYDARCDTWSLGITAIEL-GDGDPPLADLHPMRALFKIP---RNPPPK 249
Cdd:smart00219  152 LYDDDYYRKRGGKLPiRWMAPESL-----KEGKFTSKSDVWSFGVLLWEIfTLGEQPYPGMSNEEVLEYLKngyRLPQPP 226
                           250       260       270
                    ....*....|....*....|....*....|....
gi 767960106    250 LRQPELWsaefnDFISKCLTKDYEKRPTVSELLQ 283
Cdd:smart00219  227 NCPPELY-----DLMLQCWAEDPEDRPTFSELVE 255
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
17-287 4.84e-38

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 144.03  E-value: 4.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   17 PSDtWEITETIGKGTYGKVFKVLNKKNGQKAAVKIL--DPIH-DIDEEI---EAEYNILKALSdHPNVVRFYGiyFKKDK 90
Cdd:cd06652     1 PTN-WRLGKLLGQGAFGRVYLCYDADTGRELAVKQVqfDPESpETSKEVnalECEIQLLKNLL-HERIVQYYG--CLRDP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   91 VNgDKLWLVLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHealmGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFG 170
Cdd:cd06652    77 QE-RTLSIFMEYMPGGSIKDQLKSYGALTENVTRKYTRQILE----GVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  171 VSAQLTS---TRHRRNTSVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPP 247
Cdd:cd06652   152 ASKRLQTiclSGTGMKSVTGTPYWMSPEVISGE-----GYGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIATQPT 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767960106  248 -PKLrqPELWSAEFNDFISKCLTkDYEKRPTVSELLQHKFI 287
Cdd:cd06652   227 nPQL--PAHVSDHCRDFLKRIFV-EAKLRPSADELLRHTFV 264
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
27-291 6.28e-38

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 143.90  E-value: 6.28e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILdPIHDID-----EEIEAEYNILkALSDHPNVVRFYgiY-FKKDKvngdKLWLVL 100
Cdd:cd05579     1 ISRGAYGRVYLAKKKSTGDLYAIKVI-KKRDMIrknqvDSVLAERNIL-SQAQNPFVVKLY--YsFQGKK----NLYLVM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCSGGsvtDLvKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS-------- 172
Cdd:cd05579    73 EYLPGG---DL-YSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSkvglvrrq 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 -------AQLTSTRHRRNTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKI--P 243
Cdd:cd05579   149 iklsiqkKSNGAPEKEDRRIVGTPDYLAPEIL-----LGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNIlnG 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767960106  244 RNPPPKLrqPELwSAEFNDFISKCLTKDYEKRP---TVSELLQHKFITQIE 291
Cdd:cd05579   224 KIEWPED--PEV-SDEAKDLISKLLTPDPEKRLgakGIEEIKNHPFFKGID 271
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
22-283 6.67e-38

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 143.46  E-value: 6.67e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106     22 EITETIGKGTYGKVFK-VLNKKNG---QKAAVKILDPIHDID--EEIEAEYNILKALsDHPNVVRFYGIYFKkdkvnGDK 95
Cdd:smart00221    2 TLGKKLGEGAFGEVYKgTLKGKGDgkeVEVAVKTLKEDASEQqiEEFLREARIMRKL-DHPNIVKLLGVCTE-----EEP 75
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106     96 LWLVLELCSGGSVtdlvKGFLK--RGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSA 173
Cdd:smart00221   76 LMIVMEYMPGGDL----LDYLRknRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSR 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    174 QLTSTRHRRNTSVGTP-FWMAPEVIaceqqLDTTYDARCDTWSLGITAIEL-GDGDPPLADLHPMRALFKIP---RNPPP 248
Cdd:smart00221  152 DLYDDDYYKVKGGKLPiRWMAPESL-----KEGKFTSKSDVWSFGVLLWEIfTLGEEPYPGMSNAEVLEYLKkgyRLPKP 226
                           250       260       270
                    ....*....|....*....|....*....|....*
gi 767960106    249 KLRQPELWsaefnDFISKCLTKDYEKRPTVSELLQ 283
Cdd:smart00221  227 PNCPPELY-----KLMLQCWAEDPEDRPTFSELVE 256
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
21-285 6.76e-38

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 143.63  E-value: 6.76e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIH---DIDEEIEAEYNILKALSdHPNVVRFYGIyfkkdKVNGDKLW 97
Cdd:cd14069     3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRapgDCPENIKKEVCIQKMLS-HKNVVRFYGH-----RREGEFQY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVTDLVK---GflkrgerMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:cd14069    77 LFLEYASGGELFDKIEpdvG-------MPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LTSTRHRR--NTSVGTPFWMAPEVIACEQqldttYDA-RCDTWSLGITAIELGDGDPPL---ADLHPMRALFKIPRN--- 245
Cdd:cd14069   150 FRYKGKERllNKMCGTLPYVAPELLAKKK-----YRAePVDVWSCGIVLFAMLAGELPWdqpSDSCQEYSDWKENKKtyl 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767960106  246 -PPPKLRQPELwsaefnDFISKCLTKDYEKRPTVSELLQHK 285
Cdd:cd14069   225 tPWKKIDTAAL------SLLRKILTENPNKRITIEDIKKHP 259
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
22-287 1.41e-37

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 143.39  E-value: 1.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKILdPIHDIDEEIEA----EYNILKALSdHPNVVRFYGIYFKKDKvngdkLW 97
Cdd:cd07829     2 EKLEKLGEGTYGVVYKAKDKKTGEIVALKKI-RLDNEEEGIPStalrEISLLKELK-HPNIVKLLDVIHTENK-----LY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSggsvTDLvKGFLK-RGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:cd07829    75 LVFEYCD----QDL-KKYLDkRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAFG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRHRRNTSVGTPFWMAPEVIaceqqL-DTTYDARCDTWSLG-ITAiELGDGDPPLA---DLHpmrALFKI--------- 242
Cdd:cd07829   150 IPLRTYTHEVVTLWYRAPEIL-----LgSKHYSTAVDIWSVGcIFA-ELITGKPLFPgdsEID---QLFKIfqilgtpte 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767960106  243 ----------------PRNPPPKLRQ--PELwSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd07829   221 eswpgvtklpdykptfPKWPKNDLEKvlPRL-DPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
22-286 1.93e-37

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 143.10  E-value: 1.93e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKILdPIHDI-----DEEIEAEYNILKALsDHPNVVRFYGIYfkKDKVNgdkL 96
Cdd:cd05580     4 EFLKTLGTGSFGRVRLVKHKDSGKYYALKIL-KKAKIiklkqVEHVLNEKRILSEV-RHPFIVNLLGSF--QDDRN---L 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:cd05580    77 YMVMEYVPGGELFSL----LRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 StrhRRNTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNpppKLRQPELW 256
Cdd:cd05580   153 D---RTYTLCGTPEYLAPEII-----LSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEG---KIRFPSFF 221
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767960106  257 SAEFNDFISKCLTKDYEKR-----PTVSELLQHKF 286
Cdd:cd05580   222 DPDAKDLIKRLLVVDLTKRlgnlkNGVEDIKNHPW 256
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
27-303 3.08e-37

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 144.58  E-value: 3.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDPIHD--IDEEIEAEYNILKALsDHPNVVRFYGIYfkkdKVNGDkLWLVLELCS 104
Cdd:PLN00034   82 IGSGAGGTVYKVIHRPTGRLYALKVIYGNHEdtVRRQICREIEILRDV-NHPNVVKCHDMF----DHNGE-IQVLLEFMD 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  105 GGSVtdlvkgflkRGERM-SEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRRN 183
Cdd:PLN00034  156 GGSL---------EGTHIaDEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMDPCN 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  184 TSVGTPFWMAPEVIACEQQlDTTYDARC-DTWSLGITAIELGDGDPPL--------ADLhpMRAlfkIPRNPPPKlrQPE 254
Cdd:PLN00034  227 SSVGTIAYMSPERINTDLN-HGAYDGYAgDIWSLGVSILEFYLGRFPFgvgrqgdwASL--MCA---ICMSQPPE--APA 298
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767960106  255 LWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQIEGKDVMLQKQLTE 303
Cdd:PLN00034  299 TASREFRHFISCCLQREPAKRWSAMQLLQHPFILRAQPGQGQGGPNLHQ 347
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
18-284 6.99e-37

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 140.99  E-value: 6.99e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   18 SDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILD-------------PIHDIDEEIEaeynILKALsDHPNVVRFYGI 84
Cdd:cd14084     5 RKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINkrkftigsrreinKPRNIETEIE----ILKKL-SHPCIIKIEDF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   85 YFKKDKVngdklWLVLELCSGGSVTDLVKGFLkrgeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTT---E 161
Cdd:cd14084    80 FDAEDDY-----YIVLELMEGGELFDRVVSNK----RLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSqeeE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  162 GGVKLVDFGVSAQLTSTRHRRnTSVGTPFWMAPEVIACEQQldTTYDARCDTWSLGITAIELGDGDPPLADLHP-MRALF 240
Cdd:cd14084   151 CLIKITDFGLSKILGETSLMK-TLCGTPTYLAPEVLRSFGT--EGYTRAVDCWSLGVILFICLSGYPPFSEEYTqMSLKE 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 767960106  241 KIPRNpppKLR-QPELW---SAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14084   228 QILSG---KYTfIPKAWknvSEEAKDLVKKMLVVDPSRRPSIEEALEH 272
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
21-287 7.41e-37

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 140.64  E-value: 7.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIH----DIDEEIEA--EYNILKALsDHPNVVRFYGIYfkkdkVNGD 94
Cdd:cd08222     2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVLKEISvgelQPDETVDAnrEAKLLSKL-DHPAIVKFHDSF-----VEKE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 KLWLVLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLtTEGGVKLVDFGVSAQ 174
Cdd:cd08222    76 SFCIVTEYCEGGDLDDKISEYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL-KNNVIKVGDFGISRI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LTSTRHRRNTSVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLrqPE 254
Cdd:cd08222   155 LMGTSDLATTFTGTPYYMSPEVLKHE-----GYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETPSL--PD 227
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767960106  255 LWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd08222   228 KYSKELNAIYSRMLNKDPALRPSAAEILKIPFI 260
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
21-286 1.13e-36

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 140.92  E-value: 1.13e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDiDEEIEA----EYNILKALSdHPNVVRFYGIYFKKDKvngdkL 96
Cdd:cd07833     3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKESED-DEDVKKtalrEVKVLRQLR-HENIVNLKEAFRRKGR-----L 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCsGGSVTDLVKGFlKRGerMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:cd07833    76 YLVFEYV-ERTLLELLEAS-PGG--LPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRHRRNTS-VGTPFWMAPEVIACeqqlDTTYDARCDTWSLGITAIELGDGDP-------------------PLADLHpM 236
Cdd:cd07833   152 ARPASPLTDyVATRWYRAPELLVG----DTNYGKPVDVWAIGCIMAELLDGEPlfpgdsdidqlyliqkclgPLPPSH-Q 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767960106  237 RALFKIPRN-----PPPKLRQP--ELWSAEFN----DFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd07833   227 ELFSSNPRFagvafPEPSQPESleRRYPGKVSspalDFLKACLRMDPKERLTCDELLQHPY 287
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
25-289 4.31e-36

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 138.86  E-value: 4.31e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQKAAVKI--LDPIHDIDEEIEAEYNILKAlSDHPNVVRFYGIYFKKDKVNgdklwLVLEL 102
Cdd:cd06619     7 EILGHGNGGTVYKAYHLLTRRILAVKVipLDITVELQKQIMSELEILYK-CDSPYIIGFYGAFFVENRIS-----ICTEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGSVtDLVKgflkrgeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRr 182
Cdd:cd06619    81 MDGGSL-DVYR-------KIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNSIAK- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  183 nTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPL-------ADLHPMRALFKIPRNPPPKLRQPEl 255
Cdd:cd06619   152 -TYVGTNAYMAPERISGEQ-----YGIHSDVWSLGISFMELALGRFPYpqiqknqGSLMPLQLLQCIVDEDPPVLPVGQ- 224
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767960106  256 WSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQ 289
Cdd:cd06619   225 FSEKFVHFITQCMRKQPKERPAPENLMDHPFIVQ 258
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
21-304 5.45e-36

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 138.92  E-value: 5.45e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPI-HDIDEEIEaeynILKALSDHPNVVRFYGIYfkkdkVNGDKLWLV 99
Cdd:cd14091     2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSkRDPSEEIE----ILLRYGQHPNIITLRDVY-----DDGNSVYLV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  100 LELCSGGsvtDLVKGFLKRGeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG----VKLVDFGVSAQL 175
Cdd:cd14091    73 TELLRGG---ELLDRILRQK-FFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGdpesLRICDFGFAKQL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 tstRHrRNTSVGTPFW----MAPEVIacEQQldtTYDARCDTWSLGITAIELGDGDPPladlhpmralFKIPRNPPP--- 248
Cdd:cd14091   149 ---RA-ENGLLMTPCYtanfVAPEVL--KKQ---GYDAACDIWSLGVLLYTMLAGYTP----------FASGPNDTPevi 209
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767960106  249 ---------KLRQPElW---SAEFNDFISKCLTKDYEKRPTVSELLQHKFITQiegKDVMLQKQLTEF 304
Cdd:cd14091   210 larigsgkiDLSGGN-WdhvSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIRN---RDSLPQRQLTDP 273
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
21-288 6.28e-36

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 137.95  E-value: 6.28e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKIL-------DPIHDIDEEIEAEYNILKALsDHPNVVRFYGIYFKKDKVNg 93
Cdd:cd06630     2 WLKGPLLGTGAFSSCYQARDVKTGTLMAVKQVsfcrnssSEQEEVVEAIREEIRMMARL-NHPNIVRMLGATQHKSHFN- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   94 dklwLVLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG-VKLVDFGVS 172
Cdd:cd06630    80 ----IFVEWMAGGSVASL----LSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQrLRIADFGAA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLTStrhrRNTS--------VGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPL-ADLHP--MRALFK 241
Cdd:cd06630   152 ARLAS----KGTGagefqgqlLGTIAFMAPEVLRGEQ-----YGRSCDVWSVGCVIIEMATAKPPWnAEKISnhLALIFK 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767960106  242 I--PRNPPPklrQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFIT 288
Cdd:cd06630   223 IasATTPPP---IPEHLSPGLRDVTLRCLELQPEDRPPARELLKHPVFT 268
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
22-286 6.96e-36

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 138.12  E-value: 6.96e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEE----IEAEYNILKALsDHPNVVRFYGIyFKKDkvngDKLW 97
Cdd:cd05581     4 KFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKkvkyVTIEKEVLSRL-AHPGIVKLYYT-FQDE----SKLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGsvtDLvKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 177
Cdd:cd05581    78 FVLEYAPNG---DL-LEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKVLGP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  178 T-----------------RHRRNTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELgdgdppLADLHPMRA-- 238
Cdd:cd05581   154 DsspestkgdadsqiaynQARAASFVGTAEYVSPELL-----NEKPAGKSSDLWALGCIIYQM------LTGKPPFRGsn 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  239 ---LFK--------IPRNPPPKLRqpelwsaefnDFISKCLTKDYEKRPTVS------ELLQHKF 286
Cdd:cd05581   223 eylTFQkivkleyeFPENFPPDAK----------DLIQKLLVLDPSKRLGVNenggydELKAHPF 277
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
21-287 7.65e-36

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 137.38  E-value: 7.65e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILdPIHDIDEE-----IEAEYNILKaLSDHPNVVRFYGIYfkkdkVNGDK 95
Cdd:cd14081     3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIV-NKEKLSKEsvlmkVEREIAIMK-LIEHPNVLKLYDVY-----ENKKY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSGGSVTDLVkgfLKRGeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVsAQL 175
Cdd:cd14081    76 LYLVLEYVSGGELFDYL---VKKG-RLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGM-ASL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTRHRRNTSVGTPFWMAPEVIACEQqldttYDAR-CDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPpklRQPE 254
Cdd:cd14081   151 QPEGSLLETSCGSPHYACPEVIKGEK-----YDGRkADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVF---HIPH 222
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767960106  255 LWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14081   223 FISPDAQDLLRRMLEVNPEKRITIEEIKKHPWF 255
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
35-302 8.60e-36

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 138.97  E-value: 8.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   35 VFKVLNKKNGQKAAVKILDPIHDIDEE---IEAEYNILKALSdHPNVVRFYGIYfkkdkVNGDKLWLVLELCSGGSVTDL 111
Cdd:cd08216    16 VHLAKHKPTNTLVAVKKINLESDSKEDlkfLQQEILTSRQLQ-HPNILPYVTSF-----VVDNDLYVVTPLMAYGSCRDL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  112 VKGFLKRGerMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRRNTSVGTP-- 189
Cdd:cd08216    90 LKTHFPEG--LPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVKHGKRQRVVHDFPks 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  190 -----FWMAPEVIacEQQLdTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKL-----------RQP 253
Cdd:cd08216   168 seknlPWLSPEVL--QQNL-LGYNEKSDIYSVGITACELANGVVPFSDMPATQMLLEKVRGTTPQLldcstypleedSMS 244
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  254 E---------------------LWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQIEGKDVMLQKQLT 302
Cdd:cd08216   245 QsedsstehpnnrdtrdipyqrTFSEAFHQFVELCLQRDPELRPSASQLLAHSFFKQCRRSNTSLLDLLK 314
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
15-286 9.23e-36

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 137.91  E-value: 9.23e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   15 PDPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKIL--DPIH-DIDEEI---EAEYNILKALSdHPNVVRFYGIYfkk 88
Cdd:cd06651     3 PSAPINWRRGKLLGQGAFGRVYLCYDVDTGRELAAKQVqfDPESpETSKEVsalECEIQLLKNLQ-HERIVQYYGCL--- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   89 dKVNGDK-LWLVLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHealmGLQHLHNNKTIHRDVKGNNILLTTEGGVKLV 167
Cdd:cd06651    79 -RDRAEKtLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILE----GMSYLHSNMIVHRDIKGANILRDSAGNVKLG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  168 DFGVSAQL-----TSTRHRRNTsvGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKI 242
Cdd:cd06651   154 DFGASKRLqticmSGTGIRSVT--GTPYWMSPEVISGE-----GYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKI 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767960106  243 ---PRNPPpklrQPELWSAEFNDFIsKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd06651   227 atqPTNPQ----LPSHISEHARDFL-GCIFVEARHRPSAEELLRHPF 268
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
21-283 1.25e-35

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 137.02  E-value: 1.25e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDpIHDID-----EEIEAEYNILKALsDHPNVVRFYGIYFKkdkvnGDK 95
Cdd:cd08224     2 YEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQ-IFEMMdakarQDCLKEIDLLQQL-NHPNIIKYLASFIE-----NNE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL 175
Cdd:cd08224    75 LNIVLELADAGDLSRLIKHFKKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRFF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTRHRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPL-ADLHPMRALF-KIPRNPPPKLRqP 253
Cdd:cd08224   155 SSKTTAAHSLVGTPYYMSPERIR-----EQGYDFKSDIWSLGCLLYEMAALQSPFyGEKMNLYSLCkKIEKCEYPPLP-A 228
                         250       260       270
                  ....*....|....*....|....*....|
gi 767960106  254 ELWSAEFNDFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd08224   229 DLYSQELRDLVAACIQPDPEKRPDISYVLD 258
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
21-286 2.23e-35

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 136.71  E-value: 2.23e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEA---------EYNILKALSDHPNVVRFYGIY----Fk 87
Cdd:cd14093     5 YEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSSENEAeelreatrrEIEILRQVSGHPNIIELHDVFesptF- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   88 kdkvngdkLWLVLELCSGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLV 167
Cdd:cd14093    84 --------IFLVFELCRKGELFD----YLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKIS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  168 DFGVSAQLTSTRHRRNTsVGTPFWMAPEVIACEQQLDTT-YDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIpRNP 246
Cdd:cd14093   152 DFGFATRLDEGEKLREL-CGTPGYLAPEVLKCSMYDNAPgYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNI-MEG 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 767960106  247 PPKLRQPElW---SAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd14093   230 KYEFGSPE-WddiSDTAKDLISKLLVVDPKKRLTAEEALEHPF 271
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
27-284 2.78e-35

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 135.47  E-value: 2.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILdPIHDID-EEIEAEYNILKALsDHPNVVRFYGIYfkkdkVNGDKLWLVLELCSG 105
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKFI-PKRDKKkEAVLREISILNQL-QHPRIIQLHEAY-----ESPTELVLILELCSG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  106 GsvtDLVKGFLKRGErMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG--VKLVDFGVSAQLTSTRHRRN 183
Cdd:cd14006    74 G---ELLDRLAERGS-LSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSpqIKIIDFGLARKLNPGEELKE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  184 TsVGTPFWMAPEVIacEQQLDTTYdarCDTWSLGITAIELGDGDPPLADLHPMRALFKIpRNPPPKLRQP--ELWSAEFN 261
Cdd:cd14006   150 I-FGTPEFVAPEIV--NGEPVSLA---TDMWSIGVLTYVLLSGLSPFLGEDDQETLANI-SACRVDFSEEyfSSVSQEAK 222
                         250       260
                  ....*....|....*....|...
gi 767960106  262 DFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14006   223 DFIRKLLVKEPRKRPTAQEALQH 245
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
18-295 6.67e-35

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 136.41  E-value: 6.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   18 SDTWEITEtIGKGTYGKVFKVLNKKNGQKAAVKIldpIH-----DIDEEIEAEYNILKALSDhPNVVRFYGIYFKKDKVN 92
Cdd:cd06615     1 DDFEKLGE-LGAGNGGVVTKVLHRPSGLIMARKL---IHleikpAIRNQIIRELKVLHECNS-PYIVGFYGAFYSDGEIS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   93 gdklwLVLELCSGGSVtDLVkgfLKRGERMSEPLIAYILHEALMGLQHLHNN-KTIHRDVKGNNILLTTEGGVKLVDFGV 171
Cdd:cd06615    76 -----ICMEHMDGGSL-DQV---LKKAGRIPENILGKISIAVLRGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  172 SAQLTSTrhRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGD---PP-----LADLH--------- 234
Cdd:cd06615   147 SGQLIDS--MANSFVGTRSYMSPERLQ-----GTHYTVQSDIWSLGLSLVEMAIGRypiPPpdakeLEAMFgrpvsegea 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  235 ----------------PMrALFK----IPRNPPPKLRQpELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQIEGKD 294
Cdd:cd06615   220 keshrpvsghppdsprPM-AIFElldyIVNEPPPKLPS-GAFSDEFQDFVDKCLKKNPKERADLKELTKHPFIKRAELEE 297

                  .
gi 767960106  295 V 295
Cdd:cd06615   298 V 298
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
21-284 1.93e-34

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 133.75  E-value: 1.93e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDP--IHDIDEEIEA---EYNILKALsDHPNVVRFYGIYfkkdkVNGDK 95
Cdd:cd14098     2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKrkVAGNDKNLQLfqrEINILKSL-EHPGIVRLIDWY-----EDDQH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHealmGLQHLHNNKTIHRDVKGNNILLTTEGG--VKLVDFGVsA 173
Cdd:cd14098    76 IYLVMEYVEGGDLMDFIMAWGAIPEQHARELTKQILE----AMAYTHSMGITHRDLKPENILITQDDPviVKISDFGL-A 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  174 QLTSTRHRRNTSVGTPFWMAPEVI-ACEQQLDTTYDARCDTWSLGITAIELGDGDPPLA-DLH-PMRALFKIPRNPPPKL 250
Cdd:cd14098   151 KVIHTGTFLVTFCGTMAYLAPEILmSKEQNLQGGYSNLVDMWSVGCLVYVMLTGALPFDgSSQlPVEKRIRKGRYTQPPL 230
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767960106  251 RQPELwSAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14098   231 VDFNI-SEEAIDFILRLLDVDPEKRMTAAQALDH 263
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
22-287 2.64e-34

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 133.15  E-value: 2.64e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKILDPiHDIDEEIEA-----EYNILKALsDHPNVVRFYgiYFKKDkvnGDKL 96
Cdd:cd05578     3 QILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNK-QKCIEKDSVrnvlnELEILQEL-EHPFLVNLW--YSFQD---EEDM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGsvtDLvKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:cd05578    76 YMVVDLLLGG---DL-RYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 sTRHRRNTSVGTPFWMAPEVIACeqqldTTYDARCDTWSLGITAIELGDGDPP-----LADLHPMRALFKIPRNPppklr 251
Cdd:cd05578   152 -DGTLATSTSGTKPYMAPEVFMR-----AGYSFAVDWWSLGVTAYEMLRGKRPyeihsRTSIEEIRAKFETASVL----- 220
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767960106  252 QPELWSAEFNDFISKCLTKDYEKR-PTVSELLQHKFI 287
Cdd:cd05578   221 YPAGWSEEAIDLINKLLERDPQKRlGDLSDLKNHPYF 257
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
27-284 3.63e-34

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 132.51  E-value: 3.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVK-ILDPIHDIDEEIEA--EYNILKALSDHPNVVRFYGIYFKkdkvnGDKLWLVLELC 103
Cdd:cd13997     8 IGSGSFSEVFKVRSKVDGCLYAVKkSKKPFRGPKERARAlrEVEAHAALGQHPNIVRYYSSWEE-----GGHLYIQMELC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  104 SGGSVTDLVKGfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTStrhRRN 183
Cdd:cd13997    83 ENGSLQDALEE-LSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLET---SGD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  184 TSVGTPFWMAPEVIaceqQLDTTYDARCDTWSLGITAIELGDGDPpladlhpmralfkIPRNPP--PKLRQPEL------ 255
Cdd:cd13997   159 VEEGDSRYLAPELL----NENYTHLPKADIFSLGVTVYEAATGEP-------------LPRNGQqwQQLRQGKLplppgl 221
                         250       260       270
                  ....*....|....*....|....*....|
gi 767960106  256 -WSAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd13997   222 vLSQELTRLLKVMLDPDPTRRPTADQLLAH 251
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
21-287 1.20e-33

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 131.23  E-value: 1.20e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYN--ILKALSDHPNVVRFYGIYfkkdKVNGdKLWL 98
Cdd:cd08225     2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKevILLAKMKHPNIVTFFASF----QENG-RLFI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   99 VLELCSGGsvtDLVKGF-LKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGV-KLVDFGVSAQLT 176
Cdd:cd08225    77 VMEYCDGG---DLMKRInRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRHRRNTSVGTPFWMAPEViaCEQQldtTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKI------PRNPPpkl 250
Cdd:cd08225   154 DSMELAYTCVGTPYYLSPEI--CQNR---PYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKIcqgyfaPISPN--- 225
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767960106  251 rqpelWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd08225   226 -----FSRDLRSLISQLFKVSPRDRPSITSILKRPFL 257
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
19-306 1.49e-33

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 132.87  E-value: 1.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKI--LDPIHDIDEEIEAEYNILKAlSDHPNVVRFYGIYFKKDKVNgdkl 96
Cdd:cd06650     5 DDFEKISELGAGNGGVVFKVSHKPSGLVMARKLihLEIKPAIRNQIIRELQVLHE-CNSPYIVGFYGAFYSDGEIS---- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 wLVLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHL-HNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL 175
Cdd:cd06650    80 -ICMEHMDGGSLDQV----LKKAGRIPEQILGKVSIAVIKGLTYLrEKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTrhRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDG----DPPLA-------------------- 231
Cdd:cd06650   155 IDS--MANSFVGTRSYMSPERLQ-----GTHYSVQSDIWSMGLSLVEMAVGrypiPPPDAkelelmfgcqvegdaaetpp 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  232 --------------DLHPMRALFK----IPRNPPPKLrQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQIEGK 293
Cdd:cd06650   228 rprtpgrplssygmDSRPPMAIFElldyIVNEPPPKL-PSGVFSLEFQDFVNKCLIKNPAERADLKQLMVHAFIKRSDAE 306
                         330
                  ....*....|...
gi 767960106  294 DVMLQKQLTEFIG 306
Cdd:cd06650   307 EVDFAGWLCSTIG 319
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
20-281 1.75e-33

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 131.09  E-value: 1.75e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   20 TWEITETIGKGTYGKVFKVLNKKNGQK----AAVKILDPIHDIDE--------EIEAEYNILKALSDHPNVVRFYGIYfk 87
Cdd:cd08528     1 EYAVLELLGSGAFGCVYKVRKKSNGQTllalKEINMTNPAFGRTEqerdksvgDIISEVNIIKEQLRHPNIVRYYKTF-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   88 kdkVNGDKLWLVLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTI-HRDVKGNNILLTTEGGVKL 166
Cdd:cd08528    79 ---LENDRLYIVMELIEGAPLGEHFSSLKEKNEHFTEDRIWNIFVQMVLALRYLHKEKQIvHRDLKPNNIMLGEDDKVTI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  167 VDFGVSAQLTSTRHRRNTSVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPR-- 244
Cdd:cd08528   156 TDFGLAKQKGPESSKMTSVVGTILYSCPEIVQNE-----PYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEae 230
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767960106  245 -NPPPKLRqpelWSAEFNDFISKCLTKDYEKRPTVSEL 281
Cdd:cd08528   231 yEPLPEGM----YSDDITFVIRSCLTPDPEARPDIVEV 264
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
21-287 2.37e-33

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 130.47  E-value: 2.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHD-IDEEIEaEYNILKALS-----DHPNVVRFYG-IYFKKDkvng 93
Cdd:cd14133     1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDyLDQSLD-EIRLLELLNkkdkaDKYHIVRLKDvFYFKNH---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   94 dkLWLVLELCsGGSVTDLVKGFLKRGerMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLT--TEGGVKLVDFGV 171
Cdd:cd14133    76 --LCIVFELL-SQNLYEFLKQNKFQY--LSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLAsySRCQIKIIDFGS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  172 SAQLTStrhRRNTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPR---NPPP 248
Cdd:cd14133   151 SCFLTQ---RLYSYIQSRYYRAPEVI-----LGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGtigIPPA 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 767960106  249 KLrqpeLWSA-----EFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14133   223 HM----LDQGkaddeLFVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
19-286 2.81e-33

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 132.79  E-value: 2.81e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKIL--DPIHDIDEE--IEAEYNILkALSDHPNVVRFYgiYFKKDKvngD 94
Cdd:cd05573     1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILrkSDMLKREQIahVRAERDIL-ADADSPWIVRLH--YAFQDE---D 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 KLWLVLELCSGGsvtDLVkGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:cd05573    75 HLYLVMEYMPGG---DLM-NLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LTST-----------------------------RHRRNTSVGTPFWMAPEVIACeqqldTTYDARCDTWSLGITAIELGD 225
Cdd:cd05573   151 MNKSgdresylndsvntlfqdnvlarrrphkqrRVRAYSAVGTPDYIAPEVLRG-----TGYGPECDWWSLGVILYEMLY 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767960106  226 GDPPLADLHPMRALFKI---------PRNPPpklrqpelWSAEFNDFISKCLTkDYEKR-PTVSELLQHKF 286
Cdd:cd05573   226 GFPPFYSDSLVETYSKImnwkeslvfPDDPD--------VSPEAIDLIRRLLC-DPEDRlGSAEEIKAHPF 287
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
22-284 2.88e-33

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 129.74  E-value: 2.88e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVK-ILDPI---HDIDEEIEAEYNILKaLSDHPNVVRFYGIYFKKDKvngdkLW 97
Cdd:cd14050     4 TILSKLGEGSFGEVFKVRSREDGKLYAVKrSRSRFrgeKDRKRKLEEVERHEK-LGEHPNCVRFIKAWEEKGI-----LY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGsvtdlVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLtS 177
Cdd:cd14050    78 IQTELCDTS-----LQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVEL-D 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  178 TRHRRNTSVGTPFWMAPEViaceqqLDTTYDARCDTWSLGITAIELGdgdpplADLHpmralfkIPRNPP--PKLRQPEL 255
Cdd:cd14050   152 KEDIHDAQEGDPRYMAPEL------LQGSFTKAADIFSLGITILELA------CNLE-------LPSGGDgwHQLRQGYL 212
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767960106  256 -------WSAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14050   213 peeftagLSPELRSIIKLMMDPDPERRPTAEDLLAL 248
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
27-284 3.34e-33

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 129.68  E-value: 3.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILD-----PIHDIDEEIEAEYNILKALsDHPNVVRFYGIYFKKDKvngDKLWLVLE 101
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAVKILKkrklrRIPNGEANVKREIQILRRL-NHRNVIKLVDVLYNEEK---QKLYMVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  102 LCSGGSVTDLvkgflkrgerMSEPLIAYILHEA-------LMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:cd14119    77 YCVGGLQEML----------DSAPDKRLPIWQAhgyfvqlIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LT--STRHRRNTSVGTPFWMAPEvIAceqQLDTTYDAR-CDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPppkLR 251
Cdd:cd14119   147 LDlfAEDDTCTTSQGSPAFQPPE-IA---NGQDSFSGFkVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGE---YT 219
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767960106  252 QPELWSAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14119   220 IPDDVDPDLQDLLRGMLEKDPEKRFTIEQIRQH 252
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
22-286 4.96e-33

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 129.96  E-value: 4.96e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKIL-DPIHDIDE-----EIEAeyniLKALSDHPNVVRFYGIYFKKDKvngdk 95
Cdd:cd07830     2 KVIKQLGDGTFGSVYLARNKETGELVAIKKMkKKFYSWEEcmnlrEVKS----LRKLNEHPNIVKLKEVFRENDE----- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSGgSVTDLVKgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSaql 175
Cdd:cd07830    73 LYFVFEYMEG-NLYQLMK--DRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLA--- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 tstRHRRN-----TSVGTPFWMAPEVIaceqqL-DTTYDARCDTWSLGITAIELGDGDP--------------------P 229
Cdd:cd07830   147 ---REIRSrppytDYVSTRWYRAPEIL-----LrSTSYSSPVDIWALGCIMAELYTLRPlfpgsseidqlykicsvlgtP 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  230 LADLHP-----MRAL-FKIPRNPPPKLRQ--PELwSAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd07830   219 TKQDWPegyklASKLgFRFPQFAPTSLHQliPNA-SPEAIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
21-286 7.78e-33

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 129.70  E-value: 7.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDpIHDIDEEIEA----EYNILKAL--SDHPNVVRFYGIYFKKDKVNGD 94
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVR-VPLSEEGIPLstirEIALLKQLesFEHPNVVRLLDVCHGPRTDREL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 KLWLVLELCSggsvTDLvKGFLKR----GerMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFG 170
Cdd:cd07838    80 KLTLVFEHVD----QDL-ATYLDKcpkpG--LPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  171 VSAqlTSTRHRRNTSVGTPFWM-APEVIaceqqLDTTYDARCDTWSLGITAIEL--------GDGDP------------P 229
Cdd:cd07838   153 LAR--IYSFEMALTSVVVTLWYrAPEVL-----LQSSYATPVDMWSVGCIFAELfnrrplfrGSSEAdqlgkifdviglP 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767960106  230 LADLHPMRALFKI---PRNPPPKLRQ--PELwSAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd07838   226 SEEEWPRNSALPRssfPSYTPRPFKSfvPEI-DEEGLDLLKKMLTFNPHKRISAFEALQHPY 286
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
14-287 1.55e-31

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 125.16  E-value: 1.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   14 FPDP-SDTWEITET-IGKGTYGKVFKVLNKKNGQKAAVKILDP---IHDIDEEIEAEYNILKALSDHPNVVRFYGIYfkk 88
Cdd:cd14106     1 STENiNEVYTVESTpLGRGKFAVVRKCIHKETGKEYAAKFLRKrrrGQDCRNEILHEIAVLELCKDCPRVVNLHEVY--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   89 dkVNGDKLWLVLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTE---GGVK 165
Cdd:cd14106    78 --ETRSELILILELAAGGELQTL----LDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEfplGDIK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  166 LVDFGVSAQLTSTRHRRNTsVGTPFWMAPEVIaceqqldtTYDARC---DTWSLGITAIELGDGDPPLADLHPMRALFKI 242
Cdd:cd14106   152 LCDFGISRVIGEGEEIREI-LGTPDYVAPEIL--------SYEPISlatDMWSIGVLTYVLLTGHSPFGGDDKQETFLNI 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767960106  243 PRNpppKLRQPE-LW---SAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14106   223 SQC---NLDFPEeLFkdvSPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
27-290 2.03e-31

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 124.81  E-value: 2.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVF---KVLNKKNGQKAAVKILDPIHDID-----EEIEAEYNILKALSDHPNVVRFYgiY-FKKDKvngdKLW 97
Cdd:cd05583     2 LGTGAYGKVFlvrKVGGHDAGKLYAMKVLKKATIVQkaktaEHTMTERQVLEAVRQSPFLVTLH--YaFQTDA----KLH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVtdlvkgF--LKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ- 174
Cdd:cd05583    76 LILDYVNGGEL------FthLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEf 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LTSTRHRRNTSVGTPFWMAPEVIaceQQLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPR-----NPPpk 249
Cdd:cd05583   150 LPGENDRAYSFCGTIEYMAPEVV---RGGSDGHDKAVDWWSLGVLTYELLTGASPFTVDGERNSQSEISKrilksHPP-- 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767960106  250 lrQPELWSAEFNDFISKCLTKDYEKR-----PTVSELLQHKFITQI 290
Cdd:cd05583   225 --IPKTFSAEAKDFILKLLEKDPKKRlgagpRGAHEIKEHPFFKGL 268
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
23-286 2.10e-31

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 125.10  E-value: 2.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   23 ITETIGKGTYGKVFKVLNKKNGQKAAvkildpIHDID----EEIEAEYNILKALsDHPNVVRFYGIYfkkDKVNgdKLWL 98
Cdd:cd14010     4 LYDEIGRGKHSVVYKGRRKGTIEFVA------IKCVDkskrPEVLNEVRLTHEL-KHPNVLKFYEWY---ETSN--HLWL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   99 VLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT-- 176
Cdd:cd14010    72 VVEYCTGGDLETL----LRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARREGei 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 --------------STRHRRNTSVGTPFWMAPEVIaceQQLDTTYDArcDTWSLGITAIELGDGDPP--------LADlh 234
Cdd:cd14010   148 lkelfgqfsdegnvNKVSKKQAKRGTPYYMAPELF---QGGVHSFAS--DLWALGCVLYEMFTGKPPfvaesfteLVE-- 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767960106  235 pmralfKIPRNPPPKLRQPELW--SAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd14010   221 ------KILNEDPPPPPPKVSSkpSPDFKSLLKGLLEKDPAKRLSWDELVKHPF 268
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
27-287 2.48e-31

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 124.73  E-value: 2.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVfKVLNKKN---GQKAAVKIL--DPIHDIDEEIEA----EYNILKALSdHPNVVRFYGIyfkkDKVNGDKLW 97
Cdd:cd13994     1 IGKGATSVV-RIVTKKNprsGVLYAVKEYrrRDDESKRKDYVKrltsEYIISSKLH-HPNIVKVLDL----CQDLHGKWC 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT- 176
Cdd:cd13994    75 LVMEYCPGGDLFTL----IEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFGm 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 ---STRHRRNTSVGTPFWMAPEVIaceQQLdtTYDAR-CDTWSLGITAIELGDGDPPLADLHPMRALFKIPRN------- 245
Cdd:cd13994   151 paeKESPMSAGLCGSEPYMAPEVF---TSG--SYDGRaVDVWSCGIVLFALFTGRFPWRSAKKSDSAYKAYEKsgdftng 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 767960106  246 --PPPKLRQPELWSaefnDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd13994   226 pyEPIENLLPSECR----RLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
23-284 7.01e-31

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 123.94  E-value: 7.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   23 ITETIGKGTYGKVFKVLNKKNGQKAAVK-ILdpIHDIDEEIEAEYNI-LKALSDHPNVVRFYGIYFKKDKVNGDKLWLVL 100
Cdd:cd13986     4 IQRLLGEGGFSFVYLVEDLSTGRLYALKkIL--CHSKEDVKEAMREIeNYRLFNHPNILRLLDSQIVKEAGGKKEVYLLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTI---HRDVKGNNILLTTEGGVKLVDFG----VSA 173
Cdd:cd13986    82 PYYKRGSLQDEIERRLVKGTFFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDDEPILMDLGsmnpARI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  174 QLTSTRHRRNTSV-----GTPFWMAPEVIACEqqLDTTYDARCDTWSLGIT--AI---------ELGDGDpPLAdLHPMR 237
Cdd:cd13986   162 EIEGRREALALQDwaaehCTMPYRAPELFDVK--SHCTIDEKTDIWSLGCTlyALmygespferIFQKGD-SLA-LAVLS 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767960106  238 ALFKIPRNPPpklrqpelWSAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd13986   238 GNYSFPDNSR--------YSEELHQLVKSMLVVNPAERPSIDDLLSR 276
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
22-286 1.14e-30

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 122.71  E-value: 1.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNgQKAAVKILDpIHDIDEEIEAEY----NILKALSDHPNVVRFYGiYfkkdKVNG--DK 95
Cdd:cd14131     4 EILKQLGKGGSSKVYKVLNPKK-KIYALKRVD-LEGADEQTLQSYkneiELLKKLKGSDRIIQLYD-Y----EVTDedDY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELcsgGSvTDLvKGFL--KRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTtEGGVKLVDFGVSA 173
Cdd:cd14131    77 LYMVMEC---GE-IDL-ATILkkKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLV-KGRLKLIDFGIAK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  174 QLTS--TRHRRNTSVGTPFWMAPEVIAceqqlDTTYDAR----------CDTWSLGITAIELGDGDPPLADL-HPMRALF 240
Cdd:cd14131   151 AIQNdtTSIVRDSQVGTLNYMSPEAIK-----DTSASGEgkpkskigrpSDVWSLGCILYQMVYGKTPFQHItNPIAKLQ 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767960106  241 KIPrNPPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd14131   226 AII-DPNHEIEFPDIPNPDLIDVMKRCLQRDPKKRPSIPELLNHPF 270
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
21-282 1.43e-30

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 122.00  E-value: 1.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVK-ILDPIHDIDEEIEAEYNILKALSDHPNVVRFygiyfkKDKVNGD-KLWL 98
Cdd:cd08219     2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKeIRLPKSSSAVEDSRKEAVLLAKMKHPNIVAF------KESFEADgHLYI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   99 VLELCSGGSVTDLVKgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST 178
Cdd:cd08219    76 VMEYCDGGDLMQKIK--LQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  179 RHRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELgdgdppLADLHPMRA------LFKIPRNPPPKLrq 252
Cdd:cd08219   154 GAYACTYVGTPYYVPPEIWE-----NMPYNNKSDIWSLGCILYEL------CTLKHPFQAnswknlILKVCQGSYKPL-- 220
                         250       260       270
                  ....*....|....*....|....*....|
gi 767960106  253 PELWSAEFNDFISKCLTKDYEKRPTVSELL 282
Cdd:cd08219   221 PSHYSYELRSLIKQMFKRNPRSRPSATTIL 250
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
25-287 1.61e-30

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 121.95  E-value: 1.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQKAA---VKILD----PIHDIDEEIEaeynILKALsDHPNVVRFYGIYFKKDKVNgdkLW 97
Cdd:cd13983     7 EVLGRGSFKTVYRAFDTEEGIEVAwneIKLRKlpkaERQRFKQEIE----ILKSL-KHPNIIKFYDSWESKSKKE---VI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVtdlvKGFLKRGERMSEPLIAYILHEALMGLQHLHNNK--TIHRDVKGNNILLT-TEGGVKLVDFGVSAQ 174
Cdd:cd13983    79 FITELMTSGTL----KQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINgNTGEVKIGDLGLATL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LtstRHRRNTSV-GTPFWMAPEViaceqqLDTTYDARCDTWSLGITAIELGDGDPPLADL-HPMRALFKIPRNPPP---- 248
Cdd:cd13983   155 L---RQSFAKSViGTPEFMAPEM------YEEHYDEKVDIYAFGMCLLEMATGEYPYSECtNAAQIYKKVTSGIKPesls 225
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767960106  249 KLRQPELwsaefNDFISKCLTKDyEKRPTVSELLQHKFI 287
Cdd:cd13983   226 KVKDPEL-----KDFIEKCLKPP-DERPSARELLEHPFF 258
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
21-287 1.73e-30

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 121.84  E-value: 1.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDpIHDID----EEIEAEYNILKALSdHPNVVRfYGIYFKKDKvngdKL 96
Cdd:cd08218     2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEIN-ISKMSpkerEESRKEVAVLSKMK-HPNIVQ-YQESFEENG----NL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLVKGflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:cd08218    75 YIVMDYCDGGDLYKRINA--QRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRHRRNTSVGTPFWMAPEViaCEQQldtTYDARCDTWSLGITAIELgdgdppLADLHPMRA------LFKIPRNPPPKL 250
Cdd:cd08218   153 STVELARTCIGTPYYLSPEI--CENK---PYNNKSDIWALGCVLYEM------CTLKHAFEAgnmknlVLKIIRGSYPPV 221
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767960106  251 rqPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd08218   222 --PSRYSYDLRSLVSQLFKRNPRDRPSINSILEKPFI 256
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
21-284 1.75e-30

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 121.74  E-value: 1.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDP----IHDIDEEIEAEYNILKALsDHPNVVRFYGIYFKKDKVNgdkl 96
Cdd:cd14663     2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKeqvaREGMVEQIKREIAIMKLL-RHPNIVELHEVMATKTKIF---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 wLVLELCSGGSVTDLVKgflkRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQlt 176
Cdd:cd14663    77 -FVMELVTGGELFSKIA----KNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSAL-- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 sTRHRR-----NTSVGTPFWMAPEVIAceqqlDTTYD-ARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNpppKL 250
Cdd:cd14663   150 -SEQFRqdgllHTTCGTPNYVAPEVLA-----RRGYDgAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKG---EF 220
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767960106  251 RQPELWSAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14663   221 EYPRWFSPGAKSLIKRILDPNPSTRITVEQIMAS 254
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
21-287 2.36e-30

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 121.72  E-value: 2.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPI---HD---IDEEIEAeyniLKALSdHPNVVRFYGIYFKKDKVngd 94
Cdd:cd14078     5 YELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKalgDDlprVKTEIEA----LKNLS-HQHICRLYHVIETDNKI--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 klWLVLELCSGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:cd14078    77 --FMVLEYCPGGELFD----YIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LTS-TRHRRNTSVGTPFWMAPEVIACEQQLdttyDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNpppKLRQP 253
Cdd:cd14078   151 PKGgMDHHLETCCGSPAYAAPELIQGKPYI----GSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSG---KYEEP 223
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767960106  254 ELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14078   224 EWLSPSSKLLLDQMLQVDPKKRITVKELLNHPWV 257
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
22-291 2.46e-30

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 123.57  E-value: 2.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEE----IEAEYNILkALSDHPNVVRFYgiYFKKDKVNgdkLW 97
Cdd:cd05601     4 EVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEevsfFEEERDIM-AKANSPWITKLQ--YAFQDSEN---LY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGsvtDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 177
Cdd:cd05601    78 LVMEYHPGG---DLLSLLSRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  178 TRHRRNTS-VGTPFWMAPEVIaceQQLDT----TYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIpRNPPPKLRQ 252
Cdd:cd05601   155 DKTVTSKMpVGTPDYIAPEVL---TSMNGgskgTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNI-MNFKKFLKF 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767960106  253 PE--LWSAEFNDFISKCLTkDYEKRPTVSELLQHKFITQIE 291
Cdd:cd05601   231 PEdpKVSESAVDLIKGLLT-DAKERLGYEGLCCHPFFSGID 270
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
19-288 2.73e-30

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 122.38  E-value: 2.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKV-------------FKVLNKKN--------------GQKAA----VKILDPIHDIDEEIEaeyn 67
Cdd:cd14199     2 NQYKLKDEIGKGSYGVVklayneddntyyaMKVLSKKKlmrqagfprrppprGARAApegcTQPRGPIERVYQEIA---- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   68 ILKALsDHPNVVRFYGIYfkkDKVNGDKLWLVLELCSGGSVTDLvkgflKRGERMSEPLIAYILHEALMGLQHLHNNKTI 147
Cdd:cd14199    78 ILKKL-DHPNVVKLVEVL---DDPSEDHLYMVFELVKQGPVMEV-----PTLKPLSEDQARFYFQDLIKGIEYLHYQKII 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  148 HRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRRNTSVGTPFWMAPEVIAcEQQLDTTYDArCDTWSLGITAIELGDGD 227
Cdd:cd14199   149 HRDVKPSNLLVGEDGHIKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLS-ETRKIFSGKA-LDVWAMGVTLYCFVFGQ 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767960106  228 PPLADLHPMRALFKIPRNPPPKLRQPELwSAEFNDFISKCLTKDYEKRPTVSELLQHKFIT 288
Cdd:cd14199   227 CPFMDERILSLHSKIKTQPLEFPDQPDI-SDDLKDLLFRMLDKNPESRISVPEIKLHPWVT 286
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
19-302 3.00e-30

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 122.44  E-value: 3.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPI-HDIDEEIEaeynILKALSDHPNVVRFYGIYfkkdkVNGDKLW 97
Cdd:cd14175     1 DGYVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSkRDPSEEIE----ILLRYGQHPNIITLKDVY-----DDGKHVY 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVTDLVKgflkRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG----VKLVDFGVSA 173
Cdd:cd14175    72 LVTELMRGGELLDKIL----RQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESGnpesLRICDFGFAK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  174 QLTSTRHRRNTSVGTPFWMAPEVIacEQQldtTYDARCDTWSLGITAIELGDGDPPLADLhpmralfkiPRNPPPKLRQp 253
Cdd:cd14175   148 QLRAENGLLMTPCYTANFVAPEVL--KRQ---GYDEGCDIWSLGILLYTMLAGYTPFANG---------PSDTPEEILT- 212
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767960106  254 ELWSAEFN--------------DFISKCLTKDYEKRPTVSELLQHKFITQiegKDVMLQKQLT 302
Cdd:cd14175   213 RIGSGKFTlsggnwntvsdaakDLVSKMLHVDPHQRLTAKQVLQHPWITQ---KDKLPQSQLN 272
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
27-301 5.97e-30

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 122.51  E-value: 5.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVF---KVLNKKNGQKAAVKIL----------DPIHdideeIEAEYNILKALSdHPNVVRFygIY-FKkdkvN 92
Cdd:cd05584     4 LGKGGYGKVFqvrKTTGSDKGKIFAMKVLkkasivrnqkDTAH-----TKAERNILEAVK-HPFIVDL--HYaFQ----T 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   93 GDKLWLVLELCSGGSVtdlvkgF--LKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFG 170
Cdd:cd05584    72 GGKLYLILEYLSGGEL------FmhLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  171 VSAQLTSTRHRRNTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPR---NPP 247
Cdd:cd05584   146 LCKESIHDGTVTHTFCGTIEYMAPEIL-----TRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKgklNLP 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767960106  248 PKLrqpelwSAEFNDFISKCLTKDYEKR----PTVSELLQ-HKFITQIEGKDVmLQKQL 301
Cdd:cd05584   221 PYL------TNEARDLLKKLLKRNVSSRlgsgPGDAEEIKaHPFFRHINWDDL-LAKKV 272
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
22-283 9.67e-30

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 120.15  E-value: 9.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEA--------EYNILKALSDHPNVVRFYGIYfkkdkVNG 93
Cdd:cd13993     3 QLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKDGNDfqklpqlrEIDLHRRVSRHPNIITLHDVF-----ETE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   94 DKLWLVLELCSGGSVTDLVKgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG-VKLVDFGVS 172
Cdd:cd13993    78 VAIYIVLEYCPNGDLFEAIT--ENRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEGtVKLCDFGLA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 aqlTSTRHRRNTSVGTPFWMAPEVIACEQQLDTTYDAR-CDTWSLGITAIELGDGDPPLADLHPMRALF-KIPRNPPPKL 250
Cdd:cd13993   156 ---TTEKISMDFGVGSEFYMAPECFDEVGRSLKGYPCAaGDIWSLGIILLNLTFGRNPWKIASESDPIFyDYYLNSPNLF 232
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767960106  251 RQPELWSAEFNDFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd13993   233 DVILPMSDDFYNLLRQIFTVNPNNRILLPELQL 265
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
19-288 1.11e-29

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 119.68  E-value: 1.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVF-------------KVLNKKNGQKAAVKildpiHDIDEEIEAEYNIlkalsDHPNVVRFYGiY 85
Cdd:cd14116     5 EDFEIGRPLGKGKFGNVYlarekqskfilalKVLFKAQLEKAGVE-----HQLRREVEIQSHL-----RHPNILRLYG-Y 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   86 FKkdkvNGDKLWLVLELCSGGSVTdlvkGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVK 165
Cdd:cd14116    74 FH----DATRVYLILEYAPLGTVY----RELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  166 LVDFGVSAQLTSTrhRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPL-ADLH--PMRALFKI 242
Cdd:cd14116   146 IADFGWSVHAPSS--RRTTLCGTLDYLPPEMIE-----GRMHDEKVDLWSLGVLCYEFLVGKPPFeANTYqeTYKRISRV 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767960106  243 prnpppKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFIT 288
Cdd:cd14116   219 ------EFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPWIT 258
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
27-281 1.61e-29

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 118.99  E-value: 1.61e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFK-VLNKKNGQ--KAAVKILDPIHDI--DEEIEAEYNILKALsDHPNVVRFYGIyfkkdkVNGDKLWLVLE 101
Cdd:cd05060     3 LGHGNFGSVRKgVYLMKSGKevEVAVKTLKQEHEKagKKEFLREASVMAQL-DHPCIVRLIGV------CKGEPLMLVME 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  102 LCSGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL--TSTR 179
Cdd:cd05060    76 LAPLGPLLK----YLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALgaGSDY 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  180 HRRNTSVGTPF-WMAPEVIACeqqldTTYDARCDTWSLGITAIE-LGDGDPPLADLHPMRALFKIPRNppPKLRQPELWS 257
Cdd:cd05060   152 YRATTAGRWPLkWYAPECINY-----GKFSSKSDVWSYGVTLWEaFSYGAKPYGEMKGPEVIAMLESG--ERLPRPEECP 224
                         250       260
                  ....*....|....*....|....
gi 767960106  258 AEFNDFISKCLTKDYEKRPTVSEL 281
Cdd:cd05060   225 QEIYSIMLSCWKYRPEDRPTFSEL 248
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
21-291 1.69e-29

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 119.36  E-value: 1.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDID----EEIEAEYNILKALsDHPNVVRFYGIYFKKDKVNgdkl 96
Cdd:cd08228     4 FQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDakarQDCVKEIDLLKQL-NHPNVIKYLDSFIEDNELN---- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 wLVLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:cd08228    79 -IVLELADAGDLSQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRHRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPL-ADLHPMRAL-FKIPRNPPPKLRQpE 254
Cdd:cd08228   158 SKTTAAHSLVGTPYYMSPERIH-----ENGYNFKSDIWSLGCLLYEMAALQSPFyGDKMNLFSLcQKIEQCDYPPLPT-E 231
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767960106  255 LWSAEFNDFISKCLTKDYEKRPTVSELlqHKFITQIE 291
Cdd:cd08228   232 HYSEKLRELVSMCIYPDPDQRPDIGYV--HQIAKQMH 266
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
374-493 2.01e-29

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 115.91  E-value: 2.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  374 ILIALNPFQSLGLYSTKHSKL-YIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGKTENAHLLVQQLTVL- 451
Cdd:cd01363     1 VLVRVNPFKELPIYRDSKIIVfYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVa 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767960106  452 --GKANNRT------------LQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEM 493
Cdd:cd01363    81 fnGINKGETegwvylteitvtLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
23-284 2.09e-29

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 118.91  E-value: 2.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   23 ITETIGKGTYGKVFKVLNKKNGQKAAVKILD----PIHDIDEEIEAEYNILKaLSDHPNVVRFYG-IYFKKDkvngdkLW 97
Cdd:cd14079     6 LGKTLGVGSFGKVKLAEHELTGHKVAVKILNrqkiKSLDMEEKIRREIQILK-LFRHPHIIRLYEvIETPTD------IF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVTDLVkgfLKRGeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 177
Cdd:cd14079    79 MVMEYVSGGELFDYI---VQKG-RLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIMRD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  178 TRHRRnTSVGTPFWMAPEVIACEqqldtTYDA-RCDTWSLGITAIELGDGDPPLADLH-PMraLFKiprnpppKLRQ--- 252
Cdd:cd14079   155 GEFLK-TSCGSPNYAAPEVISGK-----LYAGpEVDVWSCGVILYALLCGSLPFDDEHiPN--LFK-------KIKSgiy 219
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767960106  253 --PELWSAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14079   220 tiPSHLSPGARDLIKRMLVVDPLKRITIPEIRQH 253
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
27-288 2.17e-29

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 118.88  E-value: 2.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKI------LDPiHDiDEEIEAEYNILKALsDHPNVVRFYGIYfkkdkVNGDKLWLVL 100
Cdd:cd14187    15 LGKGGFAKCYEITDADTKEVFAGKIvpksllLKP-HQ-KEKMSMEIAIHRSL-AHQHVVGFHGFF-----EDNDFVYVVL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRH 180
Cdd:cd14187    87 ELCRRRSLLEL----HKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  181 RRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRN--PPPKLRQPELWSa 258
Cdd:cd14187   163 RKKTLCGTPNYIAPEVLS-----KKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNeySIPKHINPVAAS- 236
                         250       260       270
                  ....*....|....*....|....*....|
gi 767960106  259 efndFISKCLTKDYEKRPTVSELLQHKFIT 288
Cdd:cd14187   237 ----LIQKMLQTDPTARPTINELLNDEFFT 262
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
27-286 2.22e-29

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 118.87  E-value: 2.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDPIHDID----EEIEAEYNILKALsDHPNVVRFYGIYfkKDKVNgdkLWLVLEL 102
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQtrqqEHIFSEKEILEEC-NSPFIVKLYRTF--KDKKY---LYMLMEY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGSVTDLVKgflKRGeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTStRHRR 182
Cdd:cd05572    75 CLGGELWTILR---DRG-LFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGS-GRKT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  183 NTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPLA--DLHPMRaLFKIPRNPPPKLRQPELWSAEF 260
Cdd:cd05572   150 WTFCGTPEYVAPEII-----LNKGYDFSVDYWSLGILLYELLTGRPPFGgdDEDPMK-IYNIILKGIDKIEFPKYIDKNA 223
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767960106  261 NDFISKCLTKDYEKR-----PTVSELLQHKF 286
Cdd:cd05572   224 KNLIKQLLRRNPEERlgylkGGIRDIKKHKW 254
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
23-287 2.31e-29

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 118.82  E-value: 2.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   23 ITETIGKGTYGKVFKVLNKK--NGQKAAVKILDPIHDIDEEIEA----EYNILKALsDHPNVVRFYGIyFKKdkvnGDKL 96
Cdd:cd14080     4 LGKTIGEGSYSKVKLAEYTKsgLKEKVACKIIDKKKAPKDFLEKflprELEILRKL-RHPNIIQVYSI-FER----GSKV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGsvtDLVKGFLKRGeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:cd14080    78 FIFMEYAEHG---DLLEYIQKRG-ALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRHRRN--TSVGTPFWMAPEVIaceqqLDTTYDAR-CDTWSLGITAIELGDGDPPLADLHpMRALFKIPRNP----PPK 249
Cdd:cd14080   154 DDDGDVLskTFCGSAAYAAPEIL-----QGIPYDPKkYDIWSLGVILYIMLCGSMPFDDSN-IKKMLKDQQNRkvrfPSS 227
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767960106  250 LRQPelwSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14080   228 VKKL---SPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
27-290 2.83e-29

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 120.01  E-value: 2.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKIL--DPIHDiDEEIEA---EYNILKALSDHPNVVRFYGIyFKKDkvngDKLWLVLE 101
Cdd:cd05570     3 LGKGSFGKVMLAERKKTDELYAIKVLkkEVIIE-DDDVECtmtEKRVLALANRHPFLTGLHAC-FQTE----DRLYFVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  102 LCSGGsvtDLVkgF-LKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRH 180
Cdd:cd05570    77 YVNGG---DLM--FhIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIWGGN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  181 RRNTSVGTPFWMAPEVIaCEQQldttYDARCDTWSLGITAIELGDGDPPLaDLHPMRALFKIPRNPPPKLrqPELWSAEF 260
Cdd:cd05570   152 TTSTFCGTPDYIAPEIL-REQD----YGFSVDWWALGVLLYEMLAGQSPF-EGDDEDELFEAILNDEVLY--PRWLSREA 223
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767960106  261 NDFISKCLTKDYEKR----PT-VSELLQHKFITQI 290
Cdd:cd05570   224 VSILKGLLTKDPARRlgcgPKgEADIKAHPFFRNI 258
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
19-302 3.24e-29

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 119.45  E-value: 3.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILD----PIHDIdEEIEAEYNILKALSdHPNVVRFYGIyFKKDKVNgd 94
Cdd:cd14086     1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINtkklSARDH-QKLEREARICRLLK-HPNIVRLHDS-ISEEGFH-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 klWLVLELCSGGsvtDLVKGFLKRgERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTE---GGVKLVDFGV 171
Cdd:cd14086    76 --YLVFDLVTGG---ELFEDIVAR-EFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKskgAAVKLADFGL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  172 SAQLTSTRHRRNTSVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPL--ADLHPMRALFKIPRNPPPk 249
Cdd:cd14086   150 AIEVQGDQQAWFGFAGTPGYLSPEVLRKD-----PYGKPVDIWACGVILYILLVGYPPFwdEDQHRLYAQIKAGAYDYP- 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767960106  250 lrQPElWS---AEFNDFISKCLTKDYEKRPTVSELLQHKFITQIEGKDVMLQKQLT 302
Cdd:cd14086   224 --SPE-WDtvtPEAKDLINQMLTVNPAKRITAAEALKHPWICQRDRVASMVHRQET 276
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
21-288 3.94e-29

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 118.90  E-value: 3.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKV-------------FKVLNKKN--------------GQKAA----VKILDPIHDIDEEIEaeynIL 69
Cdd:cd14200     2 YKLQSEIGKGSYGVVklaynesddkyyaMKVLSKKKllkqygfprrppprGSKAAqgeqAKPLAPLERVYQEIA----IL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   70 KALsDHPNVVRFYGIYfkkDKVNGDKLWLVLELCSGGSVTDLvkgflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHR 149
Cdd:cd14200    78 KKL-DHVNIVKLIEVL---DDPAEDNLYMVFDLLRKGPVMEV-----PSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  150 DVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRRNTSVGTPFWMAPEVIACEQQldtTYDARC-DTWSLGITAIELGDGDP 228
Cdd:cd14200   149 DIKPSNLLLGDDGHVKIADFGVSNQFEGNDALLSSTAGTPAFMAPETLSDSGQ---SFSGKAlDVWAMGVTLYCFVYGKC 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  229 PLADLHPMRALFKIPRNPPPKLRQPELwSAEFNDFISKCLTKDYEKRPTVSELLQHKFIT 288
Cdd:cd14200   226 PFIDEFILALHNKIKNKPVEFPEEPEI-SEELKDLILKMLDKNPETRITVPEIKVHPWVT 284
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
22-309 6.26e-29

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 119.54  E-value: 6.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKILDPiHDI-----DEEIEAEYNILKALSdHPNVVRFYGIYFKKDKVngdkl 96
Cdd:PTZ00263   21 EMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKK-REIlkmkqVQHVAQEKSILMELS-HPFIVNMMCSFQDENRV----- 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:PTZ00263   94 YFLLEFVVGGELFT----HLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVP 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 StrhRRNTSVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNpppKLRQPELW 256
Cdd:PTZ00263  170 D---RTFTLCGTPEYLAPEVIQSK-----GHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAG---RLKFPNWF 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767960106  257 SAEFNDFISKCLTKDYEKR-----PTVSELLQHKFITQIEGkDVMLQKQLTEFIGIHQ 309
Cdd:PTZ00263  239 DGRARDLVKGLLQTDHTKRlgtlkGGVADVKNHPYFHGANW-DKLYARYYPAPIPVRV 295
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
27-290 6.30e-29

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 117.58  E-value: 6.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILdPIHDIDEE-----IEAEYNILKALSDHPNVVRFYGIYfkkdkVNGDKLWLVLE 101
Cdd:cd05611     4 ISKGAFGSVYLAKKRSTGDYFAIKVL-KKSDMIAKnqvtnVKAERAIMMIQGESPYVAKLYYSF-----QSKDYLYLVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  102 LCSGGSVTDLVK--GFLkrgermSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTR 179
Cdd:cd05611    78 YLNGGDCASLIKtlGGL------PEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLEKR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  180 HRRNTsVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPP--PKlRQPELWS 257
Cdd:cd05611   152 HNKKF-VGTPDYLAPETI-----LGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRInwPE-EVKEFCS 224
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767960106  258 AEFNDFISKCLTKDYEKR---PTVSELLQHKFITQI 290
Cdd:cd05611   225 PEAVDLINRLLCMDPAKRlgaNGYQEIKSHPFFKSI 260
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
22-286 6.92e-29

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 119.26  E-value: 6.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEE----IEAEYNILkALSDHPNVVRFYgiYFKKDKVNgdkLW 97
Cdd:cd05599     4 EPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEqvahVRAERDIL-AEADNPWVVKLY--YSFQDEEN---LY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 177
Cdd:cd05599    78 LIMEFLPGGDMMTL----LMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGLKK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  178 TrHRRNTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPLADLHPM---------RALFKIPrnPPP 248
Cdd:cd05599   154 S-HLAYSTVGTPDYIAPEVF-----LQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQetcrkimnwRETLVFP--PEV 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767960106  249 KLrqpelwSAEFNDFISKCLTkDYEKR---PTVSELLQHKF 286
Cdd:cd05599   226 PI------SPEAKDLIERLLC-DAEHRlgaNGVEEIKSHPF 259
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
21-287 8.32e-29

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 117.14  E-value: 8.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILdPIHDID-EEIEAEYNILKALS--DHPNVVRFYGiYFKKDKVngdkLW 97
Cdd:cd08220     2 YEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQI-PVEQMTkEERQAALNEVKVLSmlHHPNIIEYYE-SFLEDKA----LM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVTDLVKGflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG-VKLVDFGVSAQLt 176
Cdd:cd08220    76 IVMEYAPGGTLFEYIQQ--RKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTvVKIGDFGISKIL- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRHRRNTSVGTPFWMAPEViaCEQQldtTYDARCDTWSLGITAIEL--------GDGDPPLAdLHPMRALFkiprNPPp 248
Cdd:cd08220   153 SSKSKAYTVVGTPCYISPEL--CEGK---PYNQKSDIWALGCVLYELaslkrafeAANLPALV-LKIMRGTF----API- 221
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767960106  249 klrqPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd08220   222 ----SDRYSEELRHLILSMLHLDPNKRPTLSEIMAQPII 256
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
27-285 1.61e-28

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 116.26  E-value: 1.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKIL--DPIHDIDEEIEAEYNilkalsdHPNVVRFYGIYFKKDKVNgdklwLVLELCS 104
Cdd:cd13995    12 IPRGAFGKVYLAQDTKTKKRMACKLIpvEQFKPSDVEIQACFR-------HENIAELYGALLWEETVH-----LFMEAGE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  105 GGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVkLVDFGVSAQLTSTRHRRNT 184
Cdd:cd13995    80 GGSVLEK----LESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV-LVDFGLSVQMTEDVYVPKD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  185 SVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPLADLHPMRA----LFKIPRNPPPKLRQPELWSAEF 260
Cdd:cd13995   155 LRGTEIYMSPEVILCR-----GHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAypsyLYIIHKQAPPLEDIAQDCSPAM 229
                         250       260
                  ....*....|....*....|....*
gi 767960106  261 NDFISKCLTKDYEKRPTVSELLQHK 285
Cdd:cd13995   230 RELLEAALERNPNHRSSAAELLKHE 254
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
21-288 1.70e-28

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 117.29  E-value: 1.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVK-I-LDPIHDIDEEIEA----EYNILKALSdHPNVVRFYGIYFKKDKVNgd 94
Cdd:cd07841     2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKkIkLGERKEAKDGINFtalrEIKLLQELK-HPNIIGLLDVFGHKSNIN-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 klwLVLELCSggsvTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:cd07841    79 ---LVFEFME----TDLEKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LTSTRHRRNTSVGTPFWMAPEVI-ACEQqldttYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKI--------PRN 245
Cdd:cd07841   152 FGSPNRKMTHQVVTRWYRAPELLfGARH-----YGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIfealgtptEEN 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  246 PPP----------KLRQPELWSAEFN-------DFISKCLTKDYEKRPTVSELLQHKFIT 288
Cdd:cd07841   227 WPGvtslpdyvefKPFPPTPLKQIFPaasddalDLLQRLLTLNPNKRITARQALEHPYFS 286
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
20-286 3.44e-28

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 116.45  E-value: 3.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   20 TWEITETIGKGTYGKVFKVLNKKNGQKAAVK--ILDPihdidEEIEAEYNILKALsDHPNVVRFYGIYFKKDKVNGDK-L 96
Cdd:cd14137     5 SYTIEKVIGSGSFGVVYQAKLLETGEVVAIKkvLQDK-----RYKNRELQIMRRL-KHPNIVKLKYFFYSSGEKKDEVyL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLElCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGV-KLVDFGvSAQL 175
Cdd:cd14137    79 NLVME-YMPETLYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPETGVlKLCDFG-SAKR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TsTRHRRNTS-VGTPFWMAPEVIACEqqldTTYDARCDTWSLG-ITAiEL--------GD-------------GDPPLAD 232
Cdd:cd14137   157 L-VPGEPNVSyICSRYYRAPELIFGA----TDYTTAIDIWSAGcVLA-ELllgqplfpGEssvdqlveiikvlGTPTREQ 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  233 LH---PMRALFKIPRNPPPklrqpeLWSAEFN--------DFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd14137   231 IKamnPNYTEFKFPQIKPH------PWEKVFPkrtppdaiDLLSKILVYNPSKRLTALEALAHPF 289
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
17-299 3.45e-28

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 116.49  E-value: 3.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   17 PSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILD----------PIHDIDEEIEAEYNIlkalsDHPNVVRFYGIYf 86
Cdd:cd14094     1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDvakftsspglSTEDLKREASICHML-----KHPHIVELLETY- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   87 kkdkvNGDK-LWLVLELCSGgsvTDLVKGFLKR---GERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTE- 161
Cdd:cd14094    75 -----SSDGmLYMVFEFMDG---ADLCFEIVKRadaGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKe 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  162 --GGVKLVDFGVSAQLTSTRHRRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPL----ADLHP 235
Cdd:cd14094   147 nsAPVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREP-----YGKPVDVWGCGVILFILLSGCLPFygtkERLFE 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767960106  236 MRALFKIPRNPPpklrQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQiegKDVMLQK 299
Cdd:cd14094   222 GIIKGKYKMNPR----QWSHISESAKDLVRRMLMLDPAERITVYEALNHPWIKE---RDRYAYR 278
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
23-287 4.02e-28

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 115.18  E-value: 4.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   23 ITETIGKGTYGKVFKVLNKKNGQKAAVK------ILDP--IHDID-EEIEAEYNILKAL--SDHPNVVRFYGIYfkkdkv 91
Cdd:cd14004     4 ILKEMGEGAYGQVNLAIYKSKGKEVVIKfifkerILVDtwVRDRKlGTVPLEIHILDTLnkRSHPNIVKLLDFF------ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   92 nGDKLWLVLELCSGGSVTDLVKgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGV 171
Cdd:cd14004    78 -EDDEFYYLVMEKHGSGMDLFD-FIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  172 SAQLTSTRHrrNTSVGTPFWMAPEVIACEQqldttYDAR-CDTWSLGITAIELGDGDPPLADLHPMRAlfkiprnppPKL 250
Cdd:cd14004   156 AAYIKSGPF--DTFVGTIDYAAPEVLRGNP-----YGGKeQDIWALGVLLYTLVFKENPFYNIEEILE---------ADL 219
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767960106  251 RQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14004   220 RIPYAVSEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
21-287 5.40e-28

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 114.94  E-value: 5.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSdHPNVVRFYGIYFKKDKVngdklWLVL 100
Cdd:cd14087     3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREVCESELNVLRRVR-HTNIIQLIEVFETKERV-----YMVM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCSGGSVTDLVkgfLKRGeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLT---TEGGVKLVDFGVSAQLTS 177
Cdd:cd14087    77 ELATGGELFDRI---IAKG-SFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYhpgPDSKIMITDFGLASTRKK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  178 TRHR-RNTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNppPKLRQPELW 256
Cdd:cd14087   153 GPNClMKTTCGTPEYIAPEIL-----LRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRA--KYSYSGEPW 225
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767960106  257 SAEFN---DFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14087   226 PSVSNlakDFIDRLLTVNPGERLSATQALKHPWI 259
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
19-309 5.69e-28

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 115.58  E-value: 5.69e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDID----EEIEAEYNILKALsDHPNVVRFygIYFKKDKVNgd 94
Cdd:cd14209     1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKlkqvEHTLNEKRILQAI-NFPFLVKL--EYSFKDNSN-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 kLWLVLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:cd14209    76 -LYMVMEYVPGGEMFSH----LRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LtstRHRRNTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNpppKLRQPE 254
Cdd:cd14209   151 V---KGRTWTLCGTPEYLAPEII-----LSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSG---KVRFPS 219
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  255 LWSAEFNDFISKCLTKDYEKR-----PTVSELLQHKFItqiegkdvmlqkQLTEFIGIHQ 309
Cdd:cd14209   220 HFSSDLKDLLRNLLQVDLTKRfgnlkNGVNDIKNHKWF------------ATTDWIAIYQ 267
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
22-283 6.38e-28

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 115.08  E-value: 6.38e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKILdPIHDIDEEIEAEYNILKALS--DHPNVVRFYGIYfkkdkVNGDKLWLV 99
Cdd:cd13996     9 EEIELLGSGGFGSVYKVRNKVDGVTYAIKKI-RLTEKSSASEKVLREVKALAklNHPNIVRYYTAW-----VEEPPLYIQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  100 LELCSGGSVTD-LVKGFlkRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTE-GGVKLVDFG------- 170
Cdd:cd13996    83 MELCEGGTLRDwIDRRN--SSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDdLQVKIGDFGlatsign 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  171 --VSAQLTSTRHRRNTS-----VGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELgdgdppladLHPMRALF--- 240
Cdd:cd13996   161 qkRELNNLNNNNNGNTSnnsvgIGTPLYASPEQLDGEN-----YNEKADIYSLGIILFEM---------LHPFKTAMers 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767960106  241 KIPRNpppkLRQ---PELWSAEFN---DFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd13996   227 TILTD----LRNgilPESFKAKHPkeaDLIQSLLSKNPEERPSAEQLLR 271
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
19-309 7.16e-28

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 116.30  E-value: 7.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKI--LDPIHDIDEEIEAEYNILKAlSDHPNVVRFYGIYFKKDKVNgdkl 96
Cdd:cd06649     5 DDFERISELGAGNGGVVTKVQHKPSGLIMARKLihLEIKPAIRNQIIRELQVLHE-CNSPYIVGFYGAFYSDGEIS---- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 wLVLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTI-HRDVKGNNILLTTEGGVKLVDFGVSAQL 175
Cdd:cd06649    80 -ICMEHMDGGSLDQV----LKEAKRIPEEILGKVSIAVLRGLAYLREKHQImHRDVKPSNILVNSRGEIKLCDFGVSGQL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTrhRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDG----DPPLA-------------------- 231
Cdd:cd06649   155 IDS--MANSFVGTRSYMSPERLQ-----GTHYSVQSDIWSMGLSLVELAIGrypiPPPDAkeleaifgrpvvdgeegeph 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  232 ------------------DLHPMRALFK----IPRNPPPKLRQpELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQ 289
Cdd:cd06649   228 sisprprppgrpvsghgmDSRPAMAIFElldyIVNEPPPKLPN-GVFTPDFQEFVNKCLIKNPAERADLKMLMNHTFIKR 306
                         330       340
                  ....*....|....*....|
gi 767960106  290 IEGKDVMLQKQLTEFIGIHQ 309
Cdd:cd06649   307 SEVEEVDFAGWLCKTLRLNQ 326
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
25-285 7.61e-28

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 114.31  E-value: 7.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYnilkALSDHPNVVRFYGIYfkKDKVNGDK-LWLVLELC 103
Cdd:cd14089     7 QVLGLGINGKVLECFHKKTGEKFALKVLRDNPKARREVELHW----RASGCPHIVRIIDVY--ENTYQGRKcLLVVMECM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  104 SGGsvtDLVKGFLKRGER-MSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG---VKLVDFGVsAQLTSTR 179
Cdd:cd14089    81 EGG---ELFSRIQERADSaFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPnaiLKLTDFGF-AKETTTK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  180 HRRNTSVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPLADLHPMRalfkIPRNPPPKLRQ------- 252
Cdd:cd14089   157 KSLQTPCYTPYYVAPEVLGPE-----KYDKSCDMWSLGVIMYILLCGYPPFYSNHGLA----ISPGMKKRIRNgqyefpn 227
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767960106  253 PElWSA---EFNDFISKCLTKDYEKRPTVSELLQHK 285
Cdd:cd14089   228 PE-WSNvseEAKDLIRGLLKTDPSERLTIEEVMNHP 262
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
25-286 8.15e-28

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 115.07  E-value: 8.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQKAAVKILD---------PIHDIDEEIEAEYNILKALSDHPNVVRFYGIYfkkdkVNGDK 95
Cdd:cd14181    16 EVIGRGVSSVVRRCVHRHTGQEFAVKIIEvtaerlspeQLEEVRSSTLKEIHILRQVSGHPSIITLIDSY-----ESSTF 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL 175
Cdd:cd14181    91 IFLVFDLMRRGELFD----YLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTRHRRNTsVGTPFWMAPEVIACeqQLDTT---YDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIpRNPPPKLRQ 252
Cdd:cd14181   167 EPGEKLREL-CGTPGYLAPEILKC--SMDEThpgYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMI-MEGRYQFSS 242
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767960106  253 PElW---SAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd14181   243 PE-WddrSSTVKDLISRLLVVDPEIRLTAEQALQHPF 278
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
21-284 8.70e-28

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 114.02  E-value: 8.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKIL--DPIHD------IDEEIEaeynILKALsDHPNVVRFYGIYFKKDKVn 92
Cdd:cd14073     3 YELLETLGKGTYGKVKLAIERATGREVAIKSIkkDKIEDeqdmvrIRREIE----IMSSL-NHPHIIRIYEVFENKDKI- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   93 gdklWLVLELCSGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS 172
Cdd:cd14073    77 ----VIVMEYASGGELYD----YISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 aQLTSTRHRRNTSVGTPFWMAPEVIAceqqlDTTYDA-RCDTWSLGITAIELGDGDPPLaDLHPMRALFK-IP----RNP 246
Cdd:cd14073   149 -NLYSKDKLLQTFCGSPLYASPEIVN-----GTPYQGpEVDCWSLGVLLYTLVYGTMPF-DGSDFKRLVKqISsgdyREP 221
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767960106  247 PPKLRQPELwsaefndfISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14073   222 TQPSDASGL--------IRWMLTVNPKRRATIEDIANH 251
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
21-287 9.31e-28

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 114.19  E-value: 9.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDP--IHDID--EEIEAEYNILKALSdHPNVVRFYGiYFKkdkvNGDKL 96
Cdd:cd14186     3 FKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKkaMQKAGmvQRVRNEVEIHCQLK-HPSILELYN-YFE----DSNYV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLVKgflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:cd14186    77 YLVLEMCHNGEMSRYLK---NRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRHRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNpppKLRQPELW 256
Cdd:cd14186   154 MPHEKHFTMCGTPNYISPEIAT-----RSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLA---DYEMPAFL 225
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767960106  257 SAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14186   226 SREAQDLIHQLLRKNPADRLSLSSVLDHPFM 256
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
19-286 9.67e-28

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 114.78  E-value: 9.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKIL-----DP-IHDIDEEieaEYNILKALSdHPNVVRFYGIYFKKDKvn 92
Cdd:cd07847     1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIKKFvesedDPvIKKIALR---EIRMLKQLK-HPNLVNLIEVFRRKRK-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   93 gdkLWLVLELCSGGSVTDLVKGflKRGerMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS 172
Cdd:cd07847    75 ---LHLVFEYCDHTVLNELEKN--PRG--VPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLTSTRHRRNTSVGTPFWMAPEVIACeqqlDTTYDARCDTWSLGITAIELGDGDP----------------PLADLHPM 236
Cdd:cd07847   148 RILTGPGDDYTDYVATRWYRAPELLVG----DTQYGPPVDVWAIGCVFAELLTGQPlwpgksdvdqlylirkTLGDLIPR 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767960106  237 -RALF---------KIPRNP---PPKLRQPELWSAEFNdFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd07847   224 hQQIFstnqffkglSIPEPEtrePLESKFPNISSPALS-FLKGCLQMDPTERLSCEELLEHPY 285
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
22-290 1.00e-27

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 116.09  E-value: 1.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVK-ILDPIHDIDE------EIEaeynILKALsDHPNVVRFYGIYFKKDKVNGD 94
Cdd:cd07834     3 ELLKPIGSGAYGVVCSAYDKRTGRKVAIKkISNVFDDLIDakrilrEIK----ILRHL-KHENIIGLLDILRPPSPEEFN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 KLWLVLELCSggsvTDLVKgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS-- 172
Cdd:cd07834    78 DVYIVTELME----TDLHK-VIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLArg 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 -------AQLTS---TRHRRntsvgtpfwmAPEVIACEQQldttYDARCDTWSLGITAIEL--------GD--------- 225
Cdd:cd07834   153 vdpdedkGFLTEyvvTRWYR----------APELLLSSKK----YTKAIDIWSVGCIFAELltrkplfpGRdyidqlnli 218
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767960106  226 ----GDPPLADLHP------MRALFKIPRNPPPKLRQ-PELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQI 290
Cdd:cd07834   219 vevlGTPSEEDLKFissekaRNYLKSLPKKPKKPLSEvFPGASPEAIDLLEKMLVFNPKKRITADEALAHPYLAQL 294
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
21-287 1.07e-27

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 113.69  E-value: 1.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSD--HPNVVRFygiyfkKDKVNGDK--L 96
Cdd:cd08223     2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKlkHPNIVSY------KESFEGEDgfL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLVKGflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:cd08223    76 YIVMGFCEGGDLYTRLKE--QKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRHRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIElgdgdppLADL-HPMRA------LFKIPRNPPPK 249
Cdd:cd08223   154 SSSDMATTLIGTPYYMSPELFS-----NKPYNHKSDVWALGCCVYE-------MATLkHAFNAkdmnslVYKILEGKLPP 221
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767960106  250 LrqPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd08223   222 M--PKQYSPELGELIKAMLHQDPEKRPSVKRILRQPYI 257
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
27-281 1.53e-27

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 113.76  E-value: 1.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQkaaVKILDPIHDIDEEIEA----EYNILKALsDHPNVVRFYGIYFKKDKVNgdklwLVLEL 102
Cdd:cd14154     1 LGKGFFGQAIKVTHRETGE---VMVMKELIRFDEEAQRnflkEVKVMRSL-DHPNVLKFIGVLYKDKKLN-----LITEY 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGSVTDLVKGflkrgerMSEPLI----AYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS------ 172
Cdd:cd14154    72 IPGGTLKDVLKD-------MARPLPwaqrVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLArlivee 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 -----AQLTSTRHR---------RNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIEL---GDGDPPLadlhp 235
Cdd:cd14154   145 rlpsgNMSPSETLRhlkspdrkkRYTVVGNPYWMAPEMLN-----GRSYDEKVDIFSFGIVLCEIigrVEADPDY----- 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767960106  236 mralfkIPRNPPPKLRQPELWS-------AEFNDFISKCLTKDYEKRPTVSEL 281
Cdd:cd14154   215 ------LPRTKDFGLNVDSFREkfcagcpPPFFKLAFLCCDLDPEKRPPFETL 261
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
13-286 2.19e-27

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 114.39  E-value: 2.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   13 NFP--DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVK-ILdpihdIDEEIEA-------EYNILKALSdHPNVVRFY 82
Cdd:cd07865     4 EFPfcDEVSKYEKLAKIGQGTFGEVFKARHRKTGQIVALKkVL-----MENEKEGfpitalrEIKILQLLK-HENVVNLI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   83 GI-YFKKDKVNGDK--LWLVLELCSggsvTDLVkGFLKRGE-RMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILL 158
Cdd:cd07865    78 EIcRTKATPYNRYKgsIYLVFEFCE----HDLA-GLLSNKNvKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  159 TTEGGVKLVDFGV----SAQLTSTRHRRNTSVGTPFWMAPEVIACEQQldttYDARCDTWSLGITAIELGDGDP------ 228
Cdd:cd07865   153 TKDGVLKLADFGLarafSLAKNSQPNRYTNRVVTLWYRPPELLLGERD----YGPPIDMWGAGCIMAEMWTRSPimqgnt 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  229 --------------------PLADLHPMRALFKIPRNppPKLRQPELWSAEFN-----DFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd07865   229 eqhqltlisqlcgsitpevwPGVDKLELFKKMELPQG--QKRKVKERLKPYVKdpyalDLIDKLLVLDPAKRIDADTALN 306

                  ...
gi 767960106  284 HKF 286
Cdd:cd07865   307 HDF 309
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
21-288 2.58e-27

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 113.58  E-value: 2.58e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVK--ILDPIHD-IDEEIEAEYNILKALSDHPNVVRFYGIYfkkdkVNGDKLW 97
Cdd:cd07832     2 YKILGRIGEGAHGIVFKAKDRETGETVALKkvALRKLEGgIPNQALREIKALQACQGHPYVVKLRDVF-----PHGTGFV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCsGGSVTDLvkgfLKRGER-MSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVsAQLT 176
Cdd:cd07832    77 LVFEYM-LSSLSEV----LRDEERpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGL-ARLF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRHRRNTS--VGTPFWMAPEVIACEQQldttYDARCDTWSLGITAIELGDGDP--------------------PLADLH 234
Cdd:cd07832   151 SEEDPRLYShqVATRWYRAPELLYGSRK----YDEGVDLWAVGCIFAELLNGSPlfpgendieqlaivlrtlgtPNEKTW 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767960106  235 P-MRAL---FKI--PRNPPPKLRQ--PELWSAEFnDFISKCLTKDYEKRPTVSELLQHKFIT 288
Cdd:cd07832   227 PeLTSLpdyNKItfPESKGIRLEEifPDCSPEAI-DLLKGLLVYNPKKRLSAEEALRHPYFF 287
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
28-282 2.67e-27

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 112.36  E-value: 2.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   28 GKGTYGKVFKVLNKKNGQKAAVKILDpihdideEIEAEYNILKALSdHPNVVRFYGIYfkkdkVNGDKLWLVLELCSGGS 107
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDKEVAVKKLL-------KIEKEAEILSVLS-HRNIIQFYGAI-----LEAPNYGIVTEYASYGS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  108 VTDLVKGflKRGERMSEPLIAYILHEALMGLQHLHNN---KTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRrnT 184
Cdd:cd14060    69 LFDYLNS--NESEEMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFGASRFHSHTTHM--S 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  185 SVGTPFWMAPEVIaceQQLDTTydARCDTWSLGITAIELGDGDPPLADLHPMR-ALFKIPRNPPPKLrqPELWSAEFNDF 263
Cdd:cd14060   145 LVGTFPWMAPEVI---QSLPVS--ETCDTYSYGVVLWEMLTREVPFKGLEGLQvAWLVVEKNERPTI--PSSCPRSFAEL 217
                         250
                  ....*....|....*....
gi 767960106  264 ISKCLTKDYEKRPTVSELL 282
Cdd:cd14060   218 MRRCWEADVKERPSFKQII 236
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
19-289 2.72e-27

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 113.09  E-value: 2.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILD----------PIHDIDEEIEAEYNILKALSDHPNVVRFYGIYFKK 88
Cdd:cd14182     3 EKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDitgggsfspeEVQELREATLKEIDILRKVSGHPNIIQLKDTYETN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   89 DKvngdkLWLVLELCSGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVD 168
Cdd:cd14182    83 TF-----FFLVFDLMKKGELFD----YLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  169 FGVSAQLTSTRhRRNTSVGTPFWMAPEVIACEQQLD-TTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIpRNPP 247
Cdd:cd14182   154 FGFSCQLDPGE-KLREVCGTPGYLAPEIIECSMDDNhPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMI-MSGN 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 767960106  248 PKLRQPElW---SAEFNDFISKCLTKDYEKRPTVSELLQHKFITQ 289
Cdd:cd14182   232 YQFGSPE-WddrSDTVKDLISRFLVVQPQKRYTAEEALAHPFFQQ 275
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
19-287 3.16e-27

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 113.16  E-value: 3.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDI-DEEIEAEYNILKALSdHPNVVRFYGIYFKKDKvngdkLW 97
Cdd:cd14166     3 ETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSrDSSLENEIAVLKRIK-HENIVTLEDIYESTTH-----YY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVTDLVkgfLKRGErMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNIL-LTTEGGVKLV--DFGVSAQ 174
Cdd:cd14166    77 LVMQLVSGGELFDRI---LERGV-YTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLyLTPDENSKIMitDFGLSKM 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 ltSTRHRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRaLFKIPRNPPPKLRQPe 254
Cdd:cd14166   153 --EQNGIMSTACGTPGYVAPEVLA-----QKPYSKAVDCWSIGVITYILLCGYPPFYEETESR-LFEKIKEGYYEFESP- 223
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767960106  255 LW---SAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14166   224 FWddiSESAKDFIRHLLEKNPSKRYTCEKALSHPWI 259
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
18-284 3.22e-27

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 112.97  E-value: 3.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   18 SDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKildPIHDIDEEIEAEYNILKALsDHPNVVRFYGIY----------FK 87
Cdd:cd14047     5 RQDFKEIELIGSGGFGQVFKAKHRIDGKTYAIK---RVKLNNEKAEREVKALAKL-DHPNIVRYNGCWdgfdydpetsSS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   88 KDKVNGDK-LWLVLELCSGGSVTDLVKgflKRGERMSEPLIAY-ILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVK 165
Cdd:cd14047    81 NSSRSKTKcLFIQMEFCEKGTLESWIE---KRNGEKLDKVLALeIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  166 LVDFGVSAQLTSTrHRRNTSVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDgdpPLADLHPMRALFKIPRN 245
Cdd:cd14047   158 IGDFGLVTSLKND-GKRTKSKGTLSYMSPEQISSQ-----DYGKEVDIYALGLILFELLH---VCDSAFEKSKFWTDLRN 228
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767960106  246 PPPKLRQPELWSAEfNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14047   229 GILPDIFDKRYKIE-KTIIKKMLSKKPEDRPNASEILRT 266
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
27-287 3.96e-27

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 111.93  E-value: 3.96e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDPIHDID-EEIEAEYNILKALsDHPNVVRFYGIYFKKDKVNgdklwLVLELCSG 105
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDrEDVRNEIEIMNQL-RHPRLLQLYDAFETPREMV-----LVMEYVAG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  106 GSVTDLVkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG--VKLVDFGVsAQltstRHRRN 183
Cdd:cd14103    75 GELFERV---VDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTGnqIKIIDFGL-AR----KYDPD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  184 TSV----GTPFWMAPEVIACEQQLDTTydarcDTWSLG-ITAIEL-------GDGD-PPLADLhpMRALFKIprnpppkl 250
Cdd:cd14103   147 KKLkvlfGTPEFVAPEVVNYEPISYAT-----DMWSVGvICYVLLsglspfmGDNDaETLANV--TRAKWDF-------- 211
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 767960106  251 rQPELW---SAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14103   212 -DDEAFddiSDEAKDFISKLLVKDPRKRMSAAQCLQHPWL 250
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
18-284 4.49e-27

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 112.08  E-value: 4.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   18 SDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILD--PIHDIDEEIEAEYNILKALSdHPNVVRFYGIYfkkdkVNGDK 95
Cdd:cd14083     2 RDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDkkALKGKEDSLENEIAVLRKIK-HPNIVQLLDIY-----ESKSH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSGGSVTDLV--KGFLKrgERMSEPLIAYILHealmGLQHLHNNKTIHRDVKGNNIL-LTTEGGVKLV--DFG 170
Cdd:cd14083    76 LYLVMELVTGGELFDRIveKGSYT--EKDASHLIRQVLE----AVDYLHSLGIVHRDLKPENLLyYSPDEDSKIMisDFG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  171 VSAqlTSTRHRRNTSVGTPFWMAPEVIAceQQldtTYDARCDTWSLGITAIELGDGDPPLADlhpmralfkipRNPPPKL 250
Cdd:cd14083   150 LSK--MEDSGVMSTACGTPGYVAPEVLA--QK---PYGKAVDCWSIGVISYILLCGYPPFYD-----------ENDSKLF 211
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767960106  251 RQPELWSAEFN------------DFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14083   212 AQILKAEYEFDspywddisdsakDFIRHLMEKDPNKRYTCEQALEH 257
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
65-287 6.47e-27

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 111.75  E-value: 6.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   65 EYNILkALSDHPNVVRFYGIYfkkdkVNGDKLWLVLELCSGGSVTDlvKGFLKRGERMSEPLIAYILHEALMGLQHLHNN 144
Cdd:cd08221    49 EIDIL-SLLNHDNIITYYNHF-----LDGESLFIEMEYCNGGNLHD--KIAQQKNQLFPEEVVLWYLYQIVSAVSHIHKA 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  145 KTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELG 224
Cdd:cd08221   121 GILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSMAESIVGTPYYMSPELVQGVK-----YNFKSDIWAVGCVLYELL 195
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767960106  225 DGDPPLADLHPMRALFKIPRNPPPKLRqpELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd08221   196 TLKRTFDATNPLRLAVKIVQGEYEDID--EQYSEEIIQLVHDCLHQDPEDRPTAEELLERPLL 256
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
44-291 9.10e-27

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 113.04  E-value: 9.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   44 GQKAAVKILDPIHDIDEEIEAEYN--ILKALSDHPNVVRFYGIYfkkdkVNGDKLWLVLELCSGGSVTDLVKGFLKRGer 121
Cdd:cd08226    25 GTLVTVKITNLDNCSEEHLKALQNevVLSHFFRHPNIMTHWTVF-----TEGSWLWVISPFMAYGSARGLLKTYFPEG-- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  122 MSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVdfGVSAQLTSTRHRRNTSVGTPF---------WM 192
Cdd:cd08226    98 MNEALIGNILYGAIKALNYLHQNGCIHRSVKASHILISGDGLVSLS--GLSHLYSMVTNGQRSKVVYDFpqfstsvlpWL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  193 APEVIaceQQLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPP------------------------- 247
Cdd:cd08226   176 SPELL---RQDLHGYNVKSDIYSVGITACELARGQVPFQDMRRTQMLLQKLKGPPyspldifpfpelesrmknsqsgmds 252
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767960106  248 -----------------PKLRQP--ELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQIE 291
Cdd:cd08226   253 gigesvatssmtrtmtsERLQTPssKTFSPAFHNLVELCLQQDPEKRPSASSLLSHSFFKQVK 315
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
19-287 1.03e-26

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 111.27  E-value: 1.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKIL--DPIHDIDEEIEAEYNILKALSdHPNVVRFYGIYfkkdkVNGDKL 96
Cdd:cd14167     3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIakKALEGKETSIENEIAVLHKIK-HPNIVALDDIY-----ESGGHL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLV--KGFLKrgERMSEPLIAYILHealmGLQHLHNNKTIHRDVKGNNIL---LTTEGGVKLVDFGV 171
Cdd:cd14167    77 YLIMQLVSGGELFDRIveKGFYT--ERDASKLIFQILD----AVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  172 SaQLTSTRHRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRaLFKIPRNPPPKLR 251
Cdd:cd14167   151 S-KIEGSGSVMSTACGTPGYVAPEVLA-----QKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAK-LFEQILKAEYEFD 223
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767960106  252 QPeLW---SAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14167   224 SP-YWddiSDSAKDFIQHLMEKDPEKRFTCEQALQHPWI 261
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
21-286 1.55e-26

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 111.21  E-value: 1.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKIL-DPIHDIDE-----EIEAeyniLKALSDHPNVVRFYGIYFkkDKVNGd 94
Cdd:cd07831     1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMkKHFKSLEQvnnlrEIQA----LRRLSPHPNILRLIEVLF--DRKTG- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 KLWLVLELCSGgSVTDLVKGflkRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEgGVKLVDFGvSAQ 174
Cdd:cd07831    74 RLALVFELMDM-NLYELIKG---RKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKLADFG-SCR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LTSTRHRRNTSVGTPFWMAPEVIACeqqlDTTYDARCDTWSLG---------------------ITAIELGDGDPP---L 230
Cdd:cd07831   148 GIYSKPPYTEYISTRWYRAPECLLT----DGYYGPKMDIWAVGcvffeilslfplfpgtneldqIAKIHDVLGTPDaevL 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767960106  231 ADLHPMRAL-FKIPRNPPPKLRQ--PELwSAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd07831   224 KKFRKSRHMnYNFPSKKGTGLRKllPNA-SAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
19-287 1.91e-26

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 110.49  E-value: 1.91e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDID-------EEIEAEYNILKALSdHPNVVRFYGIYFKKDKV 91
Cdd:cd14194     5 DYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSsrrgvsrEDIEREVSILKEIQ-HPNVITLHEVYENKTDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   92 ngdklWLVLELCSGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG----VKLV 167
Cdd:cd14194    84 -----ILILELVAGGELFD----FLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVpkprIKII 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  168 DFGVSAQLTSTRHRRNTsVGTPFWMAPEVIACEqqldtTYDARCDTWSLG-ITAIELGDGDP--------PLADLHPMRA 238
Cdd:cd14194   155 DFGLAHKIDFGNEFKNI-FGTPEFVAPEIVNYE-----PLGLEADMWSIGvITYILLSGASPflgdtkqeTLANVSAVNY 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767960106  239 LFkiprnpppklrQPELW---SAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14194   229 EF-----------EDEYFsntSALAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
21-299 2.15e-26

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 111.25  E-value: 2.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVF---KVLNKKNGQKAAVKILDPIHDID-----EEIEAEYNILKALSDHPNVVRFYgIYFKKDKvn 92
Cdd:cd05613     2 FELLKVLGTGAYGKVFlvrKVSGHDAGKLYAMKVLKKATIVQkaktaEHTRTERQVLEHIRQSPFLVTLH-YAFQTDT-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   93 gdKLWLVLELCSGGsvtDLVKGFLKRgERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS 172
Cdd:cd05613    79 --KLHLILDYINGG---ELFTHLSQR-ERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLTSTRHRRNTSV-GTPFWMAPEVIaceQQLDTTYDARCDTWSLGITAIELGDGDPPL---ADLHPMRALFK-IPRNPP 247
Cdd:cd05613   153 KEFLLDENERAYSFcGTIEYMAPEIV---RGGDSGHDKAVDWWSLGVLMYELLTGASPFtvdGEKNSQAEISRrILKSEP 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767960106  248 PklrQPELWSAEFNDFISKCLTKDYEKR----PT-VSELLQHKFITQIEGKDVMLQK 299
Cdd:cd05613   230 P---YPQEMSALAKDIIQRLLMKDPKKRlgcgPNgADEIKKHPFFQKINWDDLAAKK 283
MYSc_Myo33 cd14894
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...
463-985 2.82e-26

class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276859 [Multi-domain]  Cd Length: 871  Bit Score: 117.54  E-value: 2.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  463 ILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTS-----SGAVVGAQISEYLLEKSRVIHQA------IGEKNFHIFYY 531
Cdd:cd14894   249 VLDSNIVLEAFGHATTSMNLNSSRFGKMTTLQVAFglhpwEFQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  532 IYAGLAE------KKKLAHYKLPENKPPRYLQNDHLRTVQDIMNNSFYKSQYELIEQC---FKVIGFTMEQLGSIYSILA 602
Cdd:cd14894   329 MVAGVNAfpfmrlLAKELHLDGIDCSALTYLGRSDHKLAGFVSKEDTWKKDVERWQQVidgLDELNVSPDEQKTIFKVLS 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  603 AILNVGNIEFSSVATEHQIDKSHISNHTALENCASLLCI-RADELQEALTSHCVVTRGETIIRPNTVEKA--TDVRDAMA 679
Cdd:cd14894   409 AVLWLGNIELDYREVSGKLVMSSTGALNAPQKVVELLELgSVEKLERMLMTKSVSLQSTSETFEVTLEKGqvNHVRDTLA 488
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  680 KTLYGRLFSWIVNCINSLLKHDS-SPSGNGDELS-----------IGILDIFGFENFKKNSFEQLCINIANEQIqYYYNQ 747
Cdd:cd14894   489 RLLYQLAFNYVVFVMNEATKMSAlSTDGNKHQMDsnasapeavslLKIVDVFGFEDLTHNSLDQLCINYLSEKL-YAREE 567
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  748 HVFAweqneyLNEDVDARVIEYEDNWPLLDMFlQKPMGLLSLLDEESRFPKATDQTLVEKFEGN---------LKSQYFW 818
Cdd:cd14894   568 QVIA------VAYSSRPHLTARDSEKDVLFIY-EHPLGVFASLEELTILHQSENMNAQQEEKRNklfvrniydRNSSRLP 640
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  819 RPKRM-------------ELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNHPlTKTGNLPHSK 885
Cdd:cd14894   641 EPPRVlsnakrhtpvllnVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNES-SQLGWSPNTN 719
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  886 TKNVINYQMRTSeklinlakgdtgeatrharettnmKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDK 965
Cdd:cd14894   720 RSMLGSAESRLS------------------------GTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNN 775
                         570       580
                  ....*....|....*....|
gi 767960106  966 EKVLLQLRYTGILETARIRR 985
Cdd:cd14894   776 DLVEQQCRSQRLIRQMEICR 795
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
18-301 3.85e-26

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 111.65  E-value: 3.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   18 SDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPI-HDIDEEIEaeynILKALSDHPNVVRFYGIYfkkdkVNGDKL 96
Cdd:cd14176    18 TDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSkRDPTEEIE----ILLRYGQHPNIITLKDVY-----DDGKYV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLVKgflkRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG----VKLVDFGVS 172
Cdd:cd14176    89 YVVTELMKGGELLDKIL----RQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGnpesIRICDFGFA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLTSTRHRRNTSVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPLADLhpmralfkiPRNPPPKLrQ 252
Cdd:cd14176   165 KQLRAENGLLMTPCYTANFVAPEVLERQ-----GYDAACDIWSLGVLLYTMLTGYTPFANG---------PDDTPEEI-L 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767960106  253 PELWSAEFN--------------DFISKCLTKDYEKRPTVSELLQHKFITQiegKDVMLQKQL 301
Cdd:cd14176   230 ARIGSGKFSlsggywnsvsdtakDLVSKMLHVDPHQRLTAALVLRHPWIVH---WDQLPQYQL 289
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
25-286 4.06e-26

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 109.33  E-value: 4.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQKAAVKIL--------DPIHDIDEEIEaeyniLKALSDHPNVVRFYgiYFKKDKVNgdkL 96
Cdd:cd14188     7 KVLGKGGFAKCYEMTDLTTNKVYAAKIIphsrvskpHQREKIDKEIE-----LHRILHHKHVVQFY--HYFEDKEN---I 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:cd14188    77 YILLEYCSRRSMAHI----LKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRHRRNTSVGTPFWMAPEVI-----ACEQqldttydarcDTWSLGITAIELGDGDPPLADLHpMRALFKIPRNppPKLR 251
Cdd:cd14188   153 PLEHRRRTICGTPNYLSPEVLnkqghGCES----------DIWALGCVMYTMLLGRPPFETTN-LKETYRCIRE--ARYS 219
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767960106  252 QPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd14188   220 LPSSLLAPAKHLIASMLSKNPEDRPSLDEIIRHDF 254
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
18-287 5.30e-26

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 109.31  E-value: 5.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   18 SDTWEIT-ETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNIlkalSDHPNVVRFYGIYfkKDKVNGDK- 95
Cdd:cd14172     2 TDDYKLSkQVLGLGVNGKVLECFHRRTGQKCALKLLYDSPKARREVEHHWRA----SGGPHIVHILDVY--ENMHHGKRc 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSGGsvtDLVKGFLKRGER-MSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTE---GGVKLVDFGV 171
Cdd:cd14172    76 LLIIMECMEGG---ELFSRIQERGDQaFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKekdAVLKLTDFGF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  172 SAQlTSTRHRRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPLAD-----LHP-MRALFKIPRN 245
Cdd:cd14172   153 AKE-TTVQNALQTPCYTPYYVAPEVLGPEK-----YDKSCDMWSLGVIMYILLCGFPPFYSntgqaISPgMKRRIRMGQY 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767960106  246 PPPKLRQPELwSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14172   227 GFPNPEWAEV-SEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
18-302 5.71e-26

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 109.72  E-value: 5.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   18 SDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILD-PIHDIDEEIEaeynILKALSDHPNVVRFYGIYfkkdkVNGDKL 96
Cdd:cd14178     2 TDGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDkSKRDPSEEIE----ILLRYGQHPNIITLKDVY-----DDGKFV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLVKgflkRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG----VKLVDFGVS 172
Cdd:cd14178    73 YLVMELMRGGELLDRIL----RQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESGnpesIRICDFGFA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLTSTRHRRNTSVGTPFWMAPEVIacEQQldtTYDARCDTWSLGITAIELGDGDPPLADLhpmralfkiPRNPPPKLrQ 252
Cdd:cd14178   149 KQLRAENGLLMTPCYTANFVAPEVL--KRQ---GYDAACDIWSLGILLYTMLAGFTPFANG---------PDDTPEEI-L 213
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767960106  253 PELWSAEF--------------NDFISKCLTKDYEKRPTVSELLQHKFITQiegKDVMLQKQLT 302
Cdd:cd14178   214 ARIGSGKYalsggnwdsisdaaKDIVSKMLHVDPHQRLTAPQVLRHPWIVN---REYLSQNQLS 274
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
19-299 5.85e-26

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 109.83  E-value: 5.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDpIHDI-----DEEIEAEYNILKALSdHPNVVRFYGIYfkKDKVNg 93
Cdd:cd05612     1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMA-IPEVirlkqEQHVHNEKRVLKEVS-HPFIIRLFWTE--HDQRF- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   94 dkLWLVLELCSGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSA 173
Cdd:cd05612    76 --LYMLMEYVPGGELFS----YLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  174 QLtstRHRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNpppKLRQP 253
Cdd:cd05612   150 KL---RDRTWTLCGTPEYLAPEVIQ-----SKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAG---KLEFP 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767960106  254 ELWSAEFNDFISKCLTKDYEKR-----PTVSELLQHKFITQIEGKDVMLQK 299
Cdd:cd05612   219 RHLDLYAKDLIKKLLVVDRTRRlgnmkNGADDVKNHRWFKSVDWDDVPQRK 269
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
21-284 7.06e-26

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 108.57  E-value: 7.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEE--IEAEYNILKALsDHPNVVRFYGIYFKKDKvngdkLWL 98
Cdd:cd14095     2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEhmIENEVAILRRV-KHPNIVQLIEEYDTDTE-----LYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   99 VLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHealmGLQHLHNNKTIHRDVKGNNILLTTEG----GVKLVDFGVSAQ 174
Cdd:cd14095    76 VMELVKGGDLFDAITSSTKFTERDASRMVTDLAQ----ALKYLHSLSIVHRDIKPENLLVVEHEdgskSLKLADFGLATE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LTSTRHrrnTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLG-ITAIELGdGDPPladlhpmralFKIPRNpppklRQP 253
Cdd:cd14095   152 VKEPLF---TVCGTPTYVAPEILA-----ETGYGLKVDIWAAGvITYILLC-GFPP----------FRSPDR-----DQE 207
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767960106  254 ELWSA------EF------------NDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14095   208 ELFDLilagefEFlspywdnisdsaKDLISRMLVVDPEKRYSAGQVLDH 256
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
21-287 1.01e-25

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 107.86  E-value: 1.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHdIDEE----IEAEYNILKALsDHPNVVRFYGIYFKKDKvngdkL 96
Cdd:cd14071     2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQ-LDEEnlkkIYREVQIMKML-NHPHIIKLYQVMETKDM-----L 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:cd14071    75 YLVTEYASNGEIFD----YLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRHrRNTSVGTPFWMAPEVIACEQqldttYDA-RCDTWSLGITAIELGDGDPPL--ADLHPMRAlfkipRNPPPKLRQP 253
Cdd:cd14071   151 PGEL-LKTWCGSPPYAAPEVFEGKE-----YEGpQLDIWSLGVVLYVLVCGALPFdgSTLQTLRD-----RVLSGRFRIP 219
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767960106  254 ELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14071   220 FFMSTDCEHLIRRMLVLDPSKRLTIEQIKKHKWM 253
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
19-287 1.06e-25

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 108.41  E-value: 1.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIE----AEYNILKALSdHPNVVRFYGiYFKKDKvngd 94
Cdd:cd14117     6 DDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEhqlrREIEIQSHLR-HPNILRLYN-YFHDRK---- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 KLWLVLELCSGGsvtDLVKGfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:cd14117    80 RIYLILEYAPRG---ELYKE-LQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVH 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LTSTrhRRNTSVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRnppPKLRQPE 254
Cdd:cd14117   156 APSL--RRRTMCGTLDYLPPEMIEGR-----THDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVK---VDLKFPP 225
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767960106  255 LWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14117   226 FLSDGSRDLISKLLRYHPSERLPLKGVMEHPWV 258
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
21-286 1.13e-25

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 108.66  E-value: 1.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDiDEEIEA----EYNILKALSdHPNVVRFYGIYFKKDKvngdkL 96
Cdd:cd07846     3 YENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESED-DKMVKKiamrEIKMLKQLR-HENLVNLIEVFRRKKR-----W 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLVKGFLKRGERMSEPliayILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:cd07846    76 YLVFEFVDHTVLDDLEKYPNGLDESRVRK----YLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRHRRNTSVGTPFWMAPEVIACeqqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKI-------------- 242
Cdd:cd07846   152 APGEVYTDYVATRWYRAPELLVG----DTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIikclgnliprhqel 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767960106  243 -PRNPP------PKLRQPE-------LWSAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd07846   228 fQKNPLfagvrlPEVKEVEplerrypKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
27-284 1.18e-25

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 107.96  E-value: 1.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILdpIHDIDE-EIEAEYNILKALSdHPNVVRFYGIYFKKDKVNgdklwLVLELCSG 105
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMKEL--KRFDEQrSFLKEVKLMRRLS-HPNILRFIGVCVKDNKLN-----FITEYVNG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  106 GSVTDLVKgflkrgeRMSEPLI----AYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLV---DFGVSAQL--- 175
Cdd:cd14065    73 GTLEELLK-------SMDEQLPwsqrVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRNAvvaDFGLAREMpde 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 ---TSTRHRRNTSVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPLADLHPMRALF---------KIP 243
Cdd:cd14065   146 ktkKPDRKKRLTVVGSPYWMAPEMLRGE-----SYDEKVDVFSFGIVLCEIIGRVPADPDYLPRTMDFgldvrafrtLYV 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767960106  244 RNPPPklrqpelwsaEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14065   221 PDCPP----------SFLPLAIRCCQLDPEKRPSFVELEHH 251
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
25-286 1.22e-25

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 107.76  E-value: 1.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQKA-AVKILD-------PIHDIDEEIEaeynILKALsDHPNVVRFygiyfkKD-KVNGDK 95
Cdd:cd14121     1 EKLGSGTYATVYKAYRKSGAREVvAVKCVSksslnkaSTENLLTEIE----LLKKL-KHPHIVEL------KDfQWDEEH 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSGGsvtDLVKgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGV--KLVDFGVSA 173
Cdd:cd14121    70 IYLIMEYCSGG---DLSR-FIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPvlKLADFGFAQ 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  174 QLTSTRHrrNTSV-GTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPP-----LADLHPmralfKIPRNPP 247
Cdd:cd14121   146 HLKPNDE--AHSLrGSPLYMAPEMI-----LKKKYDARVDLWSVGVILYECLFGRAPfasrsFEELEE-----KIRSSKP 213
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767960106  248 PKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd14121   214 IEIPTRPELSADCRDLLLRLLQRDPDRRISFEEFFAHPF 252
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
19-287 1.40e-25

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 108.12  E-value: 1.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHD-------IDEEIEAEYNILKALSdHPNVVRFYGIYFKKDKV 91
Cdd:cd14196     5 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgvSREEIEREVSILRQVL-HPNIITLHDVYENRTDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   92 ngdklWLVLELCSGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG----VKLV 167
Cdd:cd14196    84 -----VLILELVSGGELFD----FLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  168 DFGVSAQLTSTRHRRNTsVGTPFWMAPEVIACEqqldtTYDARCDTWSLG-ITAIELGDGDPPLADlhpmralfkiprNP 246
Cdd:cd14196   155 DFGLAHEIEDGVEFKNI-FGTPEFVAPEIVNYE-----PLGLEADMWSIGvITYILLSGASPFLGD------------TK 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767960106  247 PPKLRQPELWSAEFN------------DFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14196   217 QETLANITAVSYDFDeeffshtselakDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
23-291 1.43e-25

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 108.19  E-value: 1.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   23 ITETIGKGTYGKVFKVLNKKNGQKAAVK--ILDPIHDIDEEIEaEYNILKALSDHPNVVRFYGIYFKKDKvNGDKLWLVL 100
Cdd:cd13985     4 VTKQLGEGGFSYVYLAHDVNTGRRYALKrmYFNDEEQLRVAIK-EIEIMKRLCGHPNIVQYYDSAILSSE-GRKEVLLLM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCsGGSVTDLVKGFLKRgeRMSEPLIAYILHEALMGLQHLHNNKT--IHRDVKGNNILLTTEGGVKLVDFGvSA----- 173
Cdd:cd13985    82 EYC-PGSLVDILEKSPPS--PLSEEEVLRIFYQICQAVGHLHSQSPpiIHRDIKIENILFSNTGRFKLCDFG-SAttehy 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  174 QLTSTRH--------RRNTsvgTPFWMAPEVIacEQQLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRAL---FKI 242
Cdd:cd13985   158 PLERAEEvniieeeiQKNT---TPMYRAPEMI--DLYSKKPIGEKADIWALGCLLYKLCFFKLPFDESSKLAIVagkYSI 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767960106  243 PRNPppklrqpeLWSAEFNDFISKCLTKDYEKRPTVSELLQhkFITQIE 291
Cdd:cd13985   233 PEQP--------RYSPELHDLIRHMLTPDPAERPDIFQVIN--IITKDT 271
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
21-284 2.51e-25

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 106.96  E-value: 2.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDP--IHDIDEEIEAEYNILKALSdHPNVVRFYGIYfKKDKvngdKLWL 98
Cdd:cd14185     2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKskLKGKEDMIESEILIIKSLS-HPNIVKLFEVY-ETEK----EIYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   99 VLELCSGGSVTDLVKGFLKrgerMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLT----TEGGVKLVDFGVSAQ 174
Cdd:cd14185    76 ILEYVRGGDLFDAIIESVK----FTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQhnpdKSTTLKLADFGLAKY 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LTSTRHrrnTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADlhPMR---ALFKIPRNPPPKLR 251
Cdd:cd14185   152 VTGPIF---TVCGTPTYVAPEILS-----EKGYGLEVDMWAAGVILYILLCGFPPFRS--PERdqeELFQIIQLGHYEFL 221
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767960106  252 QPeLW---SAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14185   222 PP-YWdniSEAAKDLISRLLVVDPEKRYTAKQVLQH 256
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
21-287 2.89e-25

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 107.91  E-value: 2.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFK-VLNKKNGQKAAVKILDP--IHDIDEEIEAEYNILKALS-----DHPNVVRFygIYFKKDKVN 92
Cdd:cd14096     3 YRLINKIGEGAFSNVYKaVPLRNTGKPVAIKVVRKadLSSDNLKGSSRANILKEVQimkrlSHPNIVKL--LDFQESDEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   93 gdkLWLVLELCSGGSVTDLVKgflkRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTT------------ 160
Cdd:cd14096    81 ---YYIVLELADGGEIFHQIV----RLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPipfipsivklrk 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  161 ---------EGG------------VKLVDFGVSAQLTSTRHRrnTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGIT 219
Cdd:cd14096   154 adddetkvdEGEfipgvggggigiVKLADFGLSKQVWDSNTK--TPCGTVGYTAPEVVKDER-----YSKKVDMWALGCV 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767960106  220 AIELGDGDPPLADLHPMRALFKIPRNPPPKLRQpelW----SAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14096   227 LYTLLCGFPPFYDESIETLTEKISRGDYTFLSP---WwdeiSKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
27-283 3.63e-25

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 106.37  E-value: 3.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVlnKKNGQKAAVKILDpihdIDEEIEAEYNILKALS--DHPNVVRFYGIyfkkdKVNGDKLWLVLELCS 104
Cdd:cd14058     1 VGRGSFGVVCKA--RWRNQIVAVKIIE----SESEKKAFEVEVRQLSrvDHPNIIKLYGA-----CSNQKPVCLVMEYAE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  105 GGSVTDLVKGflkrgermSEPLIAYILHEAL-------MGLQHLHNNK---TIHRDVKGNNILLTTEGGV-KLVDFGVSA 173
Cdd:cd14058    70 GGSLYNVLHG--------KEPKPIYTAAHAMswalqcaKGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTVlKICDFGTAC 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  174 QLTStrHRRNTSvGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPLADLH--PMRALFKIPRNPPPKLR 251
Cdd:cd14058   142 DIST--HMTNNK-GSAAWMAPEVFEGSK-----YSEKCDVFSWGIILWEVITRRKPFDHIGgpAFRIMWAVHNGERPPLI 213
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767960106  252 Q--PElwsaEFNDFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd14058   214 KncPK----PIESLMTRCWSKDPEKRPSMKEIVK 243
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
11-287 3.80e-25

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 106.93  E-value: 3.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   11 FDNFPDPSdtweiTETIGKGTYGKVFKVLNKKNGQKAAVKILDPI---HDIDEEIEAEYNILKALSDHPNVVRFYGIYfk 87
Cdd:cd14198     5 FNNFYILT-----SKELGRGKFAVVRQCISKSTGQEYAAKFLKKRrrgQDCRAEILHEIAVLELAKSNPRVVNLHEVY-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   88 kdkVNGDKLWLVLELCSGGSVTDLVKGFLkrGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTT---EGGV 164
Cdd:cd14198    78 ---ETTSEIILILEYAAGGEIFNLCVPDL--AEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSiypLGDI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  165 KLVDFGVSAQLTSTRHRRNTsVGTPFWMAPEVIACEQQLDTTydarcDTWSLGITAIELGDGDPPLADLHPMRALFKI-- 242
Cdd:cd14198   153 KIVDFGMSRKIGHACELREI-MGTPEYLAPEILNYDPITTAT-----DMWNIGVIAYMLLTHESPFVGEDNQETFLNIsq 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 767960106  243 -----PRNPPPKLRQPELwsaefnDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14198   227 vnvdySEETFSSVSQLAT------DFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
27-302 3.89e-25

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 108.13  E-value: 3.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDP--IHDIDEE--IEAEYNILKALSDHPNVVrfyGIYFKKDkvNGDKLWLVLEL 102
Cdd:cd05604     4 IGKGSFGKVLLAKRKRDGKYYAVKVLQKkvILNRKEQkhIMAERNVLLKNVKHPFLV---GLHYSFQ--TTDKLYFVLDF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGSVtdlvkgF--LKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRH 180
Cdd:cd05604    79 VNGGEL------FfhLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  181 RRNTSVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPL--ADLHPM-RALFKIPRNPPPKLRQPElWS 257
Cdd:cd05604   153 TTTTFCGTPEYLAPEVIRKQ-----PYDNTVDWWCLGSVLYEMLYGLPPFycRDTAEMyENILHKPLVLRPGISLTA-WS 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767960106  258 aefndFISKCLTKDYEKRPTVS----ELLQHKFITQIEGKDvMLQKQLT 302
Cdd:cd05604   227 -----ILEELLEKDRQLRLGAKedflEIKNHPFFESINWTD-LVQKKIP 269
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
62-291 4.21e-25

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha, stabilized through ATP and MO25, may be needed to activate LKB1. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. The STRAD alpha subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 108.11  E-value: 4.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   62 IEAEYNILKaLSDHPNVVRFYGIYfkkdkVNGDKLWLVLELCSGGSVTDLVKGFLKRGerMSEPLIAYILHEALMGLQHL 141
Cdd:cd08227    46 LQGELHVSK-LFNHPNIVPYRATF-----IADNELWVVTSFMAYGSAKDLICTHFMDG--MSELAIAYILQGVLKALDYI 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  142 HNNKTIHRDVKGNNILLTTEGGVKLVdfGVSAQLTSTRHRRNTSVGTPF---------WMAPEVIaceQQLDTTYDARCD 212
Cdd:cd08227   118 HHMGYVHRSVKASHILISVDGKVYLS--GLRSNLSMINHGQRLRVVHDFpkysvkvlpWLSPEVL---QQNLQGYDAKSD 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  213 TWSLGITAIELGDGDPPLADLHPMRALFK--------------IP-----------------------RNPPPKLRQPEL 255
Cdd:cd08227   193 IYSVGITACELANGHVPFKDMPATQMLLEklngtvpclldtttIPaeeltmkpsrsgansglgesttvSTPRPSNGESSS 272
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767960106  256 ------WSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQIE 291
Cdd:cd08227   273 hpynrtFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIK 314
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
19-287 4.31e-25

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 107.12  E-value: 4.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEIT-ETIGKGTYGKVFKVLNKKNGQKAAVKILDPI-HDIDEEIEAEYNILKALSDHPNVVRFYGiYFKKDkvngDKL 96
Cdd:cd14090     1 DLYKLTgELLGEGAYASVQTCINLYTGKEYAVKIIEKHpGHSRSRVFREVETLHQCQGHPNILQLIE-YFEDD----ERF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVtdlvkgfLKRGER---MSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGV---KLVDFG 170
Cdd:cd14090    76 YLVFEKMRGGPL-------LSHIEKrvhFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVspvKICDFD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  171 VSA--QLTSTRHRRNTS------VGTPFWMAPEVIACEQQLDTTYDARCDTWSLGITAIELGDGDPPLAD---------- 232
Cdd:cd14090   149 LGSgiKLSSTSMTPVTTpelltpVGSAEYMAPEVVDAFVGEALSYDKRCDLWSLGVILYIMLCGYPPFYGrcgedcgwdr 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767960106  233 -----------LHPMR-ALFKIPRnpppklRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14090   229 geacqdcqellFHSIQeGEYEFPE------KEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPWV 289
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
24-284 7.32e-25

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 107.00  E-value: 7.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   24 TETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIeaeyNILKALSDHPNVVRFYGIYfkKDKVNgdkLWLVLELC 103
Cdd:cd14092    11 EEALGDGSFSVCRKCVHKKTGQEFAVKIVSRRLDTSREV----QLLRLCQGHPNIVKLHEVF--QDELH---TYLVMELL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  104 SGGSVTDLVKgflkRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG---VKLVDFGVsAQLTSTRH 180
Cdd:cd14092    82 RGGELLERIR----KKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDdaeIKIVDFGF-ARLKPENQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  181 RRNTSVGTPFWMAPEVIACEQQlDTTYDARCDTWSLGITAIELGDGDPPladLHPmralfKIPRNPPPKLRQ-------- 252
Cdd:cd14092   157 PLKTPCFTLPYAAPEVLKQALS-TQGYDESCDLWSLGVILYTMLSGQVP---FQS-----PSRNESAAEIMKriksgdfs 227
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767960106  253 --PELW---SAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14092   228 fdGEEWknvSSEAKSLIQGLLTVDPSKRLTMSELRNH 264
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
19-287 8.28e-25

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 105.65  E-value: 8.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHD-------IDEEIEAEYNILKALsDHPNVVRFYGIYFKKDKV 91
Cdd:cd14105     5 DFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSkasrrgvSREDIEREVSILRQV-LHPNIITLHDVFENKTDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   92 ngdklWLVLELCSGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEG----GVKLV 167
Cdd:cd14105    84 -----VLILELVAGGELFD----FLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNvpipRIKLI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  168 DFGVSAQLTSTRHRRNTsVGTPFWMAPEVIACEqqldtTYDARCDTWSLG-ITAIELGDGDPPLADLHpMRALFKIPR-N 245
Cdd:cd14105   155 DFGLAHKIEDGNEFKNI-FGTPEFVAPEIVNYE-----PLGLEADMWSIGvITYILLSGASPFLGDTK-QETLANITAvN 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767960106  246 PPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14105   228 YDFDDEYFSNTSELAKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
27-284 8.40e-25

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 104.88  E-value: 8.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFkvLNKKNGQKAAVKildpihDIDEEIEAEYNILKALsDHPNVVRFYGIYfkkdkVNGDKLWLVLELCSGG 106
Cdd:cd14059     1 LGSGAQGAVF--LGKFRGEEVAVK------KVRDEKETDIKHLRKL-NHPNIIKFKGVC-----TQAPCYCILMEYCPYG 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  107 SVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLtSTRHRRNTSV 186
Cdd:cd14059    67 QLYEV----LRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKEL-SEKSTKMSFA 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  187 GTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNpPPKLRQPELWSAEFNDFISK 266
Cdd:cd14059   142 GTVAWMAPEVIRNE-----PCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSN-SLQLPVPSTCPDGFKLLMKQ 215
                         250
                  ....*....|....*...
gi 767960106  267 CLTKDYEKRPTVSELLQH 284
Cdd:cd14059   216 CWNSKPRNRPSFRQILMH 233
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
19-289 8.65e-25

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 106.66  E-value: 8.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEIT-ETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNIlkalSDHPNVVRFYGIYfkKDKVNGDK-L 96
Cdd:cd14170     1 DDYKVTsQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRA----SQCPHIVRIVDVY--ENLYAGRKcL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGsvtDLVKGFLKRGER-MSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTE---GGVKLVDFGVs 172
Cdd:cd14170    75 LIVMECLDGG---ELFSRIQDRGDQaFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGF- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLTSTRHRRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPLADLH------PMRALFKIPRNP 246
Cdd:cd14170   151 AKETTSHNSLTTPCYTPYYVAPEVLGPEK-----YDKSCDMWSLGVIMYILLCGYPPFYSNHglaispGMKTRIRMGQYE 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 767960106  247 PPKLRQPELwSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQ 289
Cdd:cd14170   226 FPNPEWSEV-SEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQ 267
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
21-287 9.59e-25

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 105.29  E-value: 9.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEA---EYNILKALsDHPNVVRFYGIyFKKDKvngdKLW 97
Cdd:cd14072     2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKlfrEVRIMKIL-NHPNIVKLFEV-IETEK----TLY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 177
Cdd:cd14072    76 LVMEYASGGEVFD----YLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  178 TrHRRNTSVGTPFWMAPEVIACEQqldttYDA-RCDTWSLGITAIELGDGDPPL--ADLHPMRAlfKIPRNpppKLRQPE 254
Cdd:cd14072   152 G-NKLDTFCGSPPYAAPELFQGKK-----YDGpEVDVWSLGVILYTLVSGSLPFdgQNLKELRE--RVLRG---KYRIPF 220
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767960106  255 LWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14072   221 YMSTDCENLLKKFLVLNPSKRGTLEQIMKDRWM 253
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
21-279 1.03e-24

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 106.27  E-value: 1.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEA----EYNILKALsDHPNVVRFYGIYFKKDKVNgdkl 96
Cdd:cd08229    26 FRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARAdcikEIDLLKQL-NHPNVIKYYASFIEDNELN---- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 wLVLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:cd08229   101 -IVLELADAGDLSRMIKHFKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFS 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRHRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPL-ADLHPMRALF-KIPRNPPPKLrQPE 254
Cdd:cd08229   180 SKTTAAHSLVGTPYYMSPERIH-----ENGYNFKSDIWSLGCLLYEMAALQSPFyGDKMNLYSLCkKIEQCDYPPL-PSD 253
                         250       260
                  ....*....|....*....|....*
gi 767960106  255 LWSAEFNDFISKCLTKDYEKRPTVS 279
Cdd:cd08229   254 HYSEELRQLVNMCINPDPEKRPDIT 278
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
106-294 1.11e-24

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 102.48  E-value: 1.11e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    106 GSVTDLVKgflKRGERMSEPLIAYILHEALMGLQHLHNNKtihrdvKGNNILLTTEGGVKLvdFGVSAQLTstrhrRNTS 185
Cdd:smart00750    1 VSLADILE---VRGRPLNEEEIWAVCLQCLGALRELHRQA------KSGNILLTWDGLLKL--DGSVAFKT-----PEQS 64
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    186 VGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQ-----PELWSA-- 258
Cdd:smart00750   65 RPDPYFMAPEVIQGQS-----YTEKADIYSLGITLYEALDYELPYNEERELSAILEILLNGMPADDPrdrsnLEGVSAar 139
                           170       180       190
                    ....*....|....*....|....*....|....*.
gi 767960106    259 EFNDFISKCLTKDYEKRPTVSELLQHKFITQIEGKD 294
Cdd:smart00750  140 SFEDFMRLCASRLPQRREAANHYLAHCRALFAETLE 175
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
23-305 1.18e-24

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 107.27  E-value: 1.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   23 ITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDID----EEIEAEYNILkALSDHPNVVRfygIYFKKDKVNgdKLWL 98
Cdd:cd05610     8 IVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINknmvHQVQAERDAL-ALSKSPFIVH---LYYSLQSAN--NVYL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   99 VLELCSGGSVTDLVKGFLKRGERMSEPLIAyilhEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS------ 172
Cdd:cd05610    82 VMEYLIGGDVKSLLHIYGYFDEEMAVKYIS----EVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSkvtlnr 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 ------------------------AQL----------TSTRHRRNTSV-------------GTPFWMAPEVIaceqqLDT 205
Cdd:cd05610   158 elnmmdilttpsmakpkndysrtpGQVlslisslgfnTPTPYRTPKSVrrgaarvegerilGTPDYLAPELL-----LGK 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  206 TYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHK 285
Cdd:cd05610   233 PHGPAVDWWALGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPEGEEELSVNAQNAIEILLTMDPTKRAGLKELKQHP 312
                         330       340
                  ....*....|....*....|
gi 767960106  286 FITQIEGKDvmLQKQLTEFI 305
Cdd:cd05610   313 LFHGVDWEN--LQNQTMPFI 330
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
22-284 1.83e-24

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 105.14  E-value: 1.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVK--ILDPIHDIDEEIEAEYNILKALsDHPNVVRFYGIYFKKDKvngdkLWLV 99
Cdd:cd14046     9 EELQVLGKGAFGQVVKVRNKLDGRYYAIKkiKLRSESKNNSRILREVMLLSRL-NHQHVVRYYQAWIERAN-----LYIQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  100 LELCSGGSVTDLVKgflkRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS------- 172
Cdd:cd14046    83 MEYCEKSTLRDLID----SGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLAtsnklnv 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 -------AQLTSTRHRRN----TSVGTPFWMAPEViacEQQLDTTYDARCDTWSLGITAIELgdGDPP---LADLHPMRA 238
Cdd:cd14046   159 elatqdiNKSTSAALGSSgdltGNVGTALYVAPEV---QSGTKSTYNEKVDMYSLGIIFFEM--CYPFstgMERVQILTA 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767960106  239 LFKIPRNPPPKLRQPElwSAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14046   234 LRSVSIEFPPDFDDNK--HSKQAKLIRWLLNHDPAKRPSAQELLKS 277
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
25-284 1.85e-24

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 105.20  E-value: 1.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKK-NGQKAAVKILDPIHDIDEEIE---AEYNILKALSD--HPNVVRFYGIYfkkdkVNGDKLWL 98
Cdd:cd14052     6 ELIGSGEFSQVYKVSERVpTGKVYAVKKLKPNYAGAKDRLrrlEEVSILRELTLdgHDNIVQLIDSW-----EYHGHLYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   99 VLELCSGGSVTdlvkGFLK---RGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL 175
Cdd:cd14052    81 QTELCENGSLD----VFLSelgLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVW 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTRHRRNTsvGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIE----------------LGDGD----PPLADLHP 235
Cdd:cd14052   157 PLIRGIERE--GDREYIAPEILS-----EHMYDKPADIFSLGLILLEaaanvvlpdngdawqkLRSGDlsdaPRLSSTDL 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767960106  236 MRAlFKIPRNPPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14052   230 HSA-SSPSSNPPPDPPNMPILSGSLDRVVRWMLSPEPDRRPTADDVLAT 277
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
27-286 1.95e-24

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 105.78  E-value: 1.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEE----IEAEYNILkALSDHPNVVRFYGIYfkkdkVNGDKLWLVLEL 102
Cdd:cd05574     9 LGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNkvkrVLTEREIL-ATLDHPFLPTLYASF-----QTSTHLCFVMDY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGSVTDLvkgfLKR--GERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRH 180
Cdd:cd05574    83 CPGGELFRL----LQKqpGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKQSSVTPP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  181 RR-----------------------------NTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLA 231
Cdd:cd05574   159 PVrkslrkgsrrssvksieketfvaepsarsNSFVGTEEYIAPEVIK-----GDGHGSAVDWWTLGILLYEMLYGTTPFK 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767960106  232 DlHPMRALFK-IPRNPppkLRQPELW--SAEFNDFISKCLTKDYEKR----PTVSELLQHKF 286
Cdd:cd05574   234 G-SNRDETFSnILKKE---LTFPESPpvSSEAKDLIRKLLVKDPSKRlgskRGASEIKRHPF 291
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
21-241 2.41e-24

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 104.27  E-value: 2.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKkNGQKAAVKIL--DPIHDIDE--EIEAEYNILKALSdHPNVVRFYGIYfkkdkVNGDKL 96
Cdd:cd14161     5 YEFLETLGKGTYGRVKKARDS-SGRLVAIKSIrkDRIKDEQDllHIRREIEIMSSLN-HPHIISVYEVF-----ENSSKI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSaQLT 176
Cdd:cd14161    78 VIVMEYASRGDLYD----YISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLS-NLY 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  177 STRHRRNTSVGTPFWMAPEVIACEQQLdttyDARCDTWSLGITAIELGDGDPPLaDLHPMRALFK 241
Cdd:cd14161   153 NQDKFLQTYCGSPLYASPEIVNGRPYI----GPEVDSWSLGVLLYILVHGTMPF-DGHDYKILVK 212
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
22-289 2.87e-24

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 106.10  E-value: 2.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVK-ILDPIHDideEIEA-----EYNILKALSDHPNVVRFYGIYfKKDkvNGDK 95
Cdd:cd07852    10 EILKKLGKGAYGIVWKAIDKKTGEVVALKkIFDAFRN---ATDAqrtfrEIMFLQELNDHPNIIKLLNVI-RAE--NDKD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSggsvTDL--V--KGFLKRGERMsepliaYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGV 171
Cdd:cd07852    84 IYLVFEYME----TDLhaVirANILEDIHKQ------YIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  172 SAQLTSTRHRRNTS-----VGTPFWMAPEV-IACeqqldTTYDARCDTWSLG-------------------------ITA 220
Cdd:cd07852   154 ARSLSQLEEDDENPvltdyVATRWYRAPEIlLGS-----TRYTKGVDMWSVGcilgemllgkplfpgtstlnqlekiIEV 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767960106  221 IelgdGDPPLADLHPMRA------LFKIPRNPPPKLRQ-PELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQ 289
Cdd:cd07852   229 I----GRPSAEDIESIQSpfaatmLESLPPSRPKSLDElFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVAQ 300
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
19-287 3.48e-24

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 104.61  E-value: 3.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDpihdIDEEIEA-------EYNILKALSdHPNVVRFYGIYFKKdkv 91
Cdd:cd07843     5 DEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLK----MEKEKEGfpitslrEINILLKLQ-HPNIVTVKEVVVGS--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   92 NGDKLWLVLELcsggsVTDLVKGFLkrgERMSEPL----IAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLV 167
Cdd:cd07843    77 NLDKIYMVMEY-----VEHDLKSLM---ETMKQPFlqseVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKIC 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  168 DFGVSAQLTSTRHRRNTSVGTPFWMAPEVIACEQQldttYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKI----- 242
Cdd:cd07843   149 DFGLAREYGSPLKPYTQLVVTLWYRAPELLLGAKE----YSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIfkllg 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767960106  243 ------------------------PRNPPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd07843   225 tptekiwpgfselpgakkktftkyPYNQLRKKFPALSLSDNGFDLLNRLLTYDPAKRISAEDALKHPYF 293
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
27-291 3.55e-24

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 105.39  E-value: 3.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDP-IHDIDEEIE---AEYNILKALSDHPNVVRFYGIYFKKDKvngdkLWLVLEL 102
Cdd:cd05619    13 LGKGSFGKVFLAELKGTNQFFAIKALKKdVVLMDDDVEctmVEKRVLSLAWEHPFLTHLFCTFQTKEN-----LFFVMEY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGsvtDLVKgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRR 182
Cdd:cd05619    88 LNGG---DLMF-HIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGDAKT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  183 NTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPLADlHPMRALFKIPRNPPPKLrqPELWSAEFND 262
Cdd:cd05619   164 STFCGTPDYIAPEIL-----LGQKYNTSVDWWSFGVLLYEMLIGQSPFHG-QDEEELFQSIRMDNPFY--PRWLEKEAKD 235
                         250       260       270
                  ....*....|....*....|....*....|
gi 767960106  263 FISKCLTKDYEKRPTV-SELLQHKFITQIE 291
Cdd:cd05619   236 ILVKLFVREPERRLGVrGDIRQHPFFREIN 265
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
27-281 3.63e-24

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 103.88  E-value: 3.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQkaaVKILDPIHDIDEEIE----AEYNILKALsDHPNVVRFYGIYFKKDKVNgdklwLVLEL 102
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGE---VMVMKELIRFDEETQrtflKEVKVMRCL-EHPNVLKFIGVLYKDKRLN-----FITEY 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGSVTDLVKGFLKR---GERMSepliayILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS------- 172
Cdd:cd14221    72 IKGGTLRGIIKSMDSHypwSQRVS------FAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLArlmvdek 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 -------AQLTSTRHRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIEL---GDGDPplaDLHPMRALFKI 242
Cdd:cd14221   146 tqpeglrSLKKPDRKKRYTVVGNPYWMAPEMIN-----GRSYDEKVDVFSFGIVLCEIigrVNADP---DYLPRTMDFGL 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767960106  243 ----------PRNPPPKlrqpelwsaeFNDFISKCLTKDYEKRPTVSEL 281
Cdd:cd14221   218 nvrgfldrycPPNCPPS----------FFPIAVLCCDLDPEKRPSFSKL 256
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
27-286 4.43e-24

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 103.47  E-value: 4.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILdPIHDID-----EEIEAEYNILKALSdHPNVVRFyGIYFKkdkvNGDKLWLVLE 101
Cdd:cd14189     9 LGKGGFARCYEMTDLATNKTYAVKVI-PHSRVAkphqrEKIVNEIELHRDLH-HKHVVKF-SHHFE----DAENIYIFLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  102 LCSGGSVTDLVKGflkrGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHR 181
Cdd:cd14189    82 LCSRKSLAHIWKA----RHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  182 RNTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPL--ADL-HPMRALFKIPRNPPPKLRQPElwsa 258
Cdd:cd14189   158 KKTICGTPNYLAPEVL-----LRQGHGPESDVWSLGCVMYTLLCGNPPFetLDLkETYRCIKQVKYTLPASLSLPA---- 228
                         250       260
                  ....*....|....*....|....*...
gi 767960106  259 efNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd14189   229 --RHLLAGILKRNPGDRLTLDQILEHEF 254
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
26-299 4.51e-24

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 105.09  E-value: 4.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   26 TIGKGTYGKVFKVLNKKNGQKAAVKIL--DPIHDIDEE--IEAEYNILKALSDHPNVVrfyGIYFKKDkvNGDKLWLVLE 101
Cdd:cd05575     2 VIGKGSFGKVLLARHKAEGKLYAVKVLqkKAILKRNEVkhIMAERNVLLKNVKHPFLV---GLHYSFQ--TKDKLYFVLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  102 LCSGGSVtdlvkgF--LKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTR 179
Cdd:cd05575    77 YVNGGEL------FfhLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  180 HRRNTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPL--ADLHPM--RALFKiprnpppKLRQPEL 255
Cdd:cd05575   151 DTTSTFCGTPEYLAPEVL-----RKQPYDRTVDWWCLGAVLYEMLYGLPPFysRDTAEMydNILHK-------PLRLRTN 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 767960106  256 WSAEFNDFISKCLTKDYEKR----PTVSELLQHKFITQIEGKDVMLQK 299
Cdd:cd05575   219 VSPSARDLLEGLLQKDRTKRlgsgNDFLEIKNHSFFRPINWDDLEAKK 266
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
27-287 5.96e-24

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 103.17  E-value: 5.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNK-KNGQKAAVKILDPIHDIDEE--IEAEYNILKALSdHPNVVRFYGIYFKKDKVngdklWLVLELC 103
Cdd:cd14202    10 IGHGAFAVVFKGRHKeKHDLEVAVKCINKKNLAKSQtlLGKEIKILKELK-HENIVALYDFQEIANSV-----YLVMEYC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  104 SGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG---------VKLVDFGVSAQ 174
Cdd:cd14202    84 NGGDLAD----YLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGGrksnpnnirIKIADFGFARY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LTSTRhRRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPLADLHP--MRALFKIPRNPPPKLrq 252
Cdd:cd14202   160 LQNNM-MAATLCGSPMYMAPEVIMSQH-----YDAKADLWSIGTIIYQCLTGKAPFQASSPqdLRLFYEKNKSLSPNI-- 231
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767960106  253 PELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14202   232 PRETSSHLRQLLLGLLQRNQKDRMDFDEFFHHPFL 266
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
21-287 5.96e-24

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 102.88  E-value: 5.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIhDIDEEIEA----EYNILKaLSDHPNVVRFYGIYFKKdkvngDKL 96
Cdd:cd14074     5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKT-KLDDVSKAhlfqEVRCMK-LVQHPNVVRLYEVIDTQ-----TKL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLVkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILL-TTEGGVKLVDFGVSAQL 175
Cdd:cd14074    78 YLILELGDGGDMYDYI---MKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTRhRRNTSVGTPFWMAPEVIaceqqLDTTYDA-RCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNpppKLRQPE 254
Cdd:cd14074   155 QPGE-KLETSCGSLAYSAPEIL-----LGDEYDApAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDC---KYTVPA 225
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767960106  255 LWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14074   226 HVSPECKDLIRRMLIRDPKKRASLEEIENHPWL 258
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
25-283 5.97e-24

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 102.81  E-value: 5.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFK-VLNKKNGQ--KAAVKILDPI----HDIDEEIEAEYNILKALsDHPNVVRFYGIyfkkdkVNGDKLW 97
Cdd:cd05040     1 EKLGDGSFGVVRRgEWTTPSGKviQVAVKCLKSDvlsqPNAMDDFLKEVNAMHSL-DHPNLIRLYGV------VLSSPLM 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVTDLVKgflKRGERMsepLIAYILHEAL---MGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:cd05040    74 MVTELAPLGSLLDRLR---KDQGHF---LISTLCDYAVqiaNGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 L-------TSTRHRRntsvgTPF-WMAPEVIACEQqldttYDARCDTWSLGITAIEL-GDGDPPLADLHPMRALFKIPRN 245
Cdd:cd05040   148 LpqnedhyVMQEHRK-----VPFaWCAPESLKTRK-----FSHASDVWMFGVTLWEMfTYGEEPWLGLNGSQILEKIDKE 217
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767960106  246 pPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd05040   218 -GERLERPDDCPQDIYNVMLQCWAHKPADRPTFVALRD 254
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
60-286 9.18e-24

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 102.44  E-value: 9.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   60 EEIEAEYNILKALSdHPNVVRFYGI-YFKKDKVNGDKLWLVLELCSGGSVTDLVK--GFLKrgermSEPLIAYILhEALM 136
Cdd:cd14012    43 QLLEKELESLKKLR-HPNLVSYLAFsIERRGRSDGWKVYLLTEYAPGGSLSELLDsvGSVP-----LDTARRWTL-QLLE 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  137 GLQHLHNNKTIHRDVKGNNILL---TTEGGVKLVDFGVSAQLTSTRHRRN-TSVGTPFWMAPEVIaceqQLDTTYDARCD 212
Cdd:cd14012   116 ALEYLHRNGVVHKSLHAGNVLLdrdAGTGIVKLTDYSLGKTLLDMCSRGSlDEFKQTYWLPPELA----QGSKSPTRKTD 191
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767960106  213 TWSLGITAIELGDGDPPLadlhpMRALFKIPRNPPPKLrqpelwSAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd14012   192 VWDLGLLFLQMLFGLDVL-----EKYTSPNPVLVSLDL------SASLQDFLSKCLSLDPKKRPTALELLPHEF 254
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
21-299 1.04e-23

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 104.23  E-value: 1.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVF---KVLNKKNGQKAAVKILDPIHDIDEEIEAEY-----NILKALSDHPNVVRFYgIYFKKDKvn 92
Cdd:cd05614     2 FELLKVLGTGAYGKVFlvrKVSGHDANKLYAMKVLRKAALVQKAKTVEHtrterNVLEHVRQSPFLVTLH-YAFQTDA-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   93 gdKLWLVLELCSGGsvtDLVKGFLKRgERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS 172
Cdd:cd05614    79 --KLHLILDYVSGG---ELFTHLYQR-DHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQ-LTSTRHRRNTSVGTPFWMAPEVIACEqqldTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPR-----NP 246
Cdd:cd05614   153 KEfLTEEKERTYSFCGTIEYMAPEIIRGK----SGHGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSEVSRrilkcDP 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767960106  247 PpklrQPELWSAEFNDFISKCLTKDYEKR----PT-VSELLQHKFITQIEGKDVMLQK 299
Cdd:cd05614   229 P----FPSFIGPVARDLLQKLLCKDPKKRlgagPQgAQEIKEHPFFKGLDWEALALRK 282
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
27-286 1.12e-23

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 102.06  E-value: 1.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKN-GQKAAVKILDP--IHDIDEEIEAEYNILKALSdHPNVVRFYgiyfkKDKVNGDKLWLVLELC 103
Cdd:cd14120     1 IGHGAFAVVFKGRHRKKpDLPVAIKCITKknLSKSQNLLGKEIKILKELS-HENVVALL-----DCQETSSSVYLVMEYC 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  104 SGGSVTD--LVKGFLkrgermSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG---------VKLVDFGVS 172
Cdd:cd14120    75 NGGDLADylQAKGTL------SEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGrkpspndirLKIADFGFA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 aqltstRHRRN-----TSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPLADLHP--MRALFKIPRN 245
Cdd:cd14120   149 ------RFLQDgmmaaTLCGSPMYMAPEVIMSLQ-----YDAKADLWSIGTIVYQCLTGKAPFQAQTPqeLKAFYEKNAN 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767960106  246 PPPKLrqPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd14120   218 LRPNI--PSGTSPALKDLLLGLLKRNPKDRIDFEDFFSHPF 256
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
24-282 1.23e-23

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 102.46  E-value: 1.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   24 TETIGKGTYGKVFKVLNKknGQKAAVKILDPIHDIDEEIEAEYNILKALS-DHPNVVRFYGIYFKKDKVNGDklWLVLEL 102
Cdd:cd13979     8 QEPLGSGGFGSVYKATYK--GETVAVKIVRRRRKNRASRQSFWAELNAARlRHENIVRVLAAETGTDFASLG--LIIMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGSVTDLVKGflkrgerMSEPLIAY----ILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST 178
Cdd:cd13979    84 CGNGTLQQLIYE-------GSEPLPLAhrilISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLGEG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  179 R---HRRNTSVGTPFWMAPEVIaceQQLDTTydARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLrqPEL 255
Cdd:cd13979   157 NevgTPRSHIGGTYTYRAPELL---KGERVT--PKADIYSFGITLWQMLTRELPYAGLRQHVLYAVVAKDLRPDL--SGL 229
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767960106  256 WSAEFND----FISKCLTKDYEKRPTVSELL 282
Cdd:cd13979   230 EDSEFGQrlrsLISRCWSAQPAERPNADESL 260
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
21-286 1.31e-23

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 101.89  E-value: 1.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSdHPNVVRFYGiYFKKDKVngdkLWLVL 100
Cdd:cd14107     4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRARAFQERDILARLS-HRRLTCLLD-QFETRKT----LILIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCSGGSVTDLVkgFLKrgERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLT--TEGGVKLVDFGVSAQLTST 178
Cdd:cd14107    78 ELCSSEELLDRL--FLK--GVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVspTREDIKICDFGFAQEITPS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  179 RHRRnTSVGTPFWMAPEVIaceQQLDTTydARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPpKLRQPEL--W 256
Cdd:cd14107   154 EHQF-SKYGSPEFVAPEIV---HQEPVS--AATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVV-SWDTPEIthL 226
                         250       260       270
                  ....*....|....*....|....*....|
gi 767960106  257 SAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd14107   227 SEDAKDFIKRVLQPDPEKRPSASECLSHEW 256
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
19-287 1.59e-23

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 101.89  E-value: 1.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEE-IEAEYNILKALSdHPNVVRFYGIYfkKDKvngDKLW 97
Cdd:cd14114     2 DHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKEtVRKEIQIMNQLH-HPKLINLHDAF--EDD---NEMV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVTDLVKGflkRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG--VKLVDFGVSAQL 175
Cdd:cd14114    76 LILEFLSGGELFERIAA---EHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSneVKLIDFGLATHL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTRHRRNTSvGTPFWMAPEVIACEQQLDTTydarcDTWSLGITAIELGDGDPPLADLHPMRALFKIPR-NPPPKLRQPE 254
Cdd:cd14114   153 DPKESVKVTT-GTAEFAAPEIVEREPVGFYT-----DMWAVGVLSYVLLSGLSPFAGENDDETLRNVKScDWNFDDSAFS 226
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767960106  255 LWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14114   227 GISEEAKDFIRKLLLADPNKRMTIHQALEHPWL 259
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
21-284 1.65e-23

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 101.54  E-value: 1.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKI-----------LDPIHDIDEEIeaeYNILKALS-DHPNVVRFYGIYfkk 88
Cdd:cd14005     2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFvpksrvtewamINGPVPVPLEI---ALLLKASKpGVPGVIRLLDWY--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   89 dkVNGDKLWLVLELCSggSVTDLVKgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG-VKLV 167
Cdd:cd14005    76 --ERPDGFLLIMERPE--PCQDLFD-FITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTGeVKLI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  168 DFGVSAQLTSTRHRrnTSVGTPFWMAPEVIACEQqldttYDARCDT-WSLGITAIELGDGDPPL-ADLHPMRALFKIPRN 245
Cdd:cd14005   151 DFGCGALLKDSVYT--DFDGTRVYSPPEWIRHGR-----YHGRPATvWSLGILLYDMLCGDIPFeNDEQILRGNVLFRPR 223
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767960106  246 pppklrqpelWSAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14005   224 ----------LSKECCDLISRCLQFDPSKRPSLEQILSH 252
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
24-286 1.79e-23

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 101.97  E-value: 1.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   24 TETIGKGTYGK-VFKvlNKKNGQKAAVK-ILDPIHDI-DEEIeaeyNILKALSDHPNVVRFYGIyfKKDKvngDKLWLVL 100
Cdd:cd13982     6 PKVLGYGSEGTiVFR--GTFDGRPVAVKrLLPEFFDFaDREV----QLLRESDEHPNVIRYFCT--EKDR---QFLYIAL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCSGgSVTDLVKGFL--KRGERmSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTT-----EGGVKLVDFGVSA 173
Cdd:cd13982    75 ELCAA-SLQDLVESPResKLFLR-PGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILISTpnahgNVRAMISDFGLCK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  174 QLTSTRH---RRNTSVGTPFWMAPEVIACEQQLDTTYDArcDTWSLG-ITAIELGDGDPPLADLHPMRALFKIPRNPPPK 249
Cdd:cd13982   153 KLDVGRSsfsRRSGVAGTSGWIAPEMLSGSTKRRQTRAV--DIFSLGcVFYYVLSGGSHPFGDKLEREANILKGKYSLDK 230
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767960106  250 LRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd13982   231 LLSLGEHGPEAQDLIERMIDFDPEKRPSAEEVLNHPF 267
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
27-299 2.23e-23

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 102.65  E-value: 2.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDE-EIE---AEYNILkALSDHPNVVRFygiyfKKDKVNGDKLWLVLEL 102
Cdd:cd05585     2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRsEVThtlAERTVL-AQVDCPFIVPL-----KFSFQSPEKLYLVLAF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRR 182
Cdd:cd05585    76 INGGELFH----HLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDKT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  183 NTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPppkLRQPELWSAEFND 262
Cdd:cd05585   152 NTFCGTPEYLAPELL-----LGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEP---LRFPDGFDRDAKD 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 767960106  263 FISKCLTKDYEKRPTV---SELLQHKFITQIEGKDVMLQK 299
Cdd:cd05585   224 LLIGLLNRDPTKRLGYngaQEIKNHPFFDQIDWKRLLMKK 263
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
22-287 3.09e-23

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 102.24  E-value: 3.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKIL---DPIHDideEIEAEYNILKALSDH-----PNVVRFY-GIYFKkdkvn 92
Cdd:cd14210    16 EVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIrnkKRFHQ---QALVEVKILKHLNDNdpddkHNIVRYKdSFIFR----- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   93 gDKLWLVLELCSggsvTDLVKgFLKRG--ERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEG--GVKLVD 168
Cdd:cd14210    88 -GHLCIVFELLS----INLYE-LLKSNnfQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSksSIKVID 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  169 FGVSAQLTSTRHrrnTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDP--PLADLH------------ 234
Cdd:cd14210   162 FGSSCFEGEKVY---TYIQSRFYRAPEVI-----LGLPYDTAIDMWSLGCILAELYTGYPlfPGENEEeqlacimevlgv 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767960106  235 -PMRALFKIPR---------------NPPPKLRQP---ELWSA------EFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14210   234 pPKSLIDKASRrkkffdsngkprpttNSKGKKRRPgskSLAQVlkcddpSFLDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
27-275 3.27e-23

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 102.46  E-value: 3.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDpiHDI---DEEIEA---EYNILKALSDHPNVVRFYGIYFKKDKvngdkLWLVL 100
Cdd:cd05592     3 LGKGSFGKVMLAELKGTNQYFAIKALK--KDVvleDDDVECtmiERRVLALASQHPFLTHLFCTFQTESH-----LFFVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCSGGsvtDLVKGFLKRGeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRH 180
Cdd:cd05592    76 EYLNGG---DLMFHIQQSG-RFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGEN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  181 RRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPLA----DlhpmrALFKIPRNPPPKLrqPELW 256
Cdd:cd05592   152 KASTFCGTPDYIAPEILKGQK-----YNQSVDWWSFGVLLYEMLIGQSPFHgedeD-----ELFWSICNDTPHY--PRWL 219
                         250
                  ....*....|....*....
gi 767960106  257 SAEFNDFISKCLTKDYEKR 275
Cdd:cd05592   220 TKEAASCLSLLLERNPEKR 238
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
27-287 4.08e-23

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 100.78  E-value: 4.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDPI---HDIDEEIEAEYNILKALSDHPNVVRFYGIYfkkdkVNGDKLWLVLELC 103
Cdd:cd14197    17 LGRGKFAVVRKCVEKDSGKEFAAKFMRKRrkgQDCRMEIIHEIAVLELAQANPWVINLHEVY-----ETASEMILVLEYA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  104 SGGSVTDlvKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTE---GGVKLVDFGVSAQLTSTRH 180
Cdd:cd14197    92 AGGEIFN--QCVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGLSRILKNSEE 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  181 RRNTsVGTPFWMAPEVIACEQQLDTTydarcDTWSLGITAIELGDGDPPLADLHPMRALFKIPR-NPPPKLRQPELWSAE 259
Cdd:cd14197   170 LREI-MGTPEYVAPEILSYEPISTAT-----DMWSIGVLAYVMLTGISPFLGDDKQETFLNISQmNVSYSEEEFEHLSES 243
                         250       260
                  ....*....|....*....|....*...
gi 767960106  260 FNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14197   244 AIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
26-287 6.02e-23

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 100.24  E-value: 6.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   26 TIGKGTYGKVFKVLNKKNGQKAAVKILD----PIHDIDEEIEAEYNILkALSDHPNVVRFYGIYfkkdKVNGDKLWLVLE 101
Cdd:cd14165     8 NLGEGSYAKVKSAYSERLKCNVAIKIIDkkkaPDDFVEKFLPRELEIL-ARLNHKSIIKTYEIF----ETSDGKVYIVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  102 LCSGGsvtDLVKgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHR 181
Cdd:cd14165    83 LGVQG---DLLE-FIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDENG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  182 R----NTSVGTPFWMAPEVIAceqqlDTTYDARC-DTWSLGITAIELGDGDPPLADLHpMRALFKIPRNPPPKLRQPELW 256
Cdd:cd14165   159 RivlsKTFCGSAAYAAPEVLQ-----GIPYDPRIyDIWSLGVILYIMVCGSMPYDDSN-VKKMLKIQKEHRVRFPRSKNL 232
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767960106  257 SAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14165   233 TSECKDLIYRLLQPDVSQRLCIDEVLSHPWL 263
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
25-283 6.33e-23

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 99.83  E-value: 6.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQKAAVKI--LDPIHDIDEEIEAEYNILKALsDHPNVVRFYGIYFKKDKVngdklWLVLEL 102
Cdd:cd05041     1 EKIGRGNFGDVYRGVLKPDNTEVAVKTcrETLPPDLKRKFLQEARILKQY-DHPNIVKLIGVCVQKQPI-----MIVMEL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGSVTDLVKgflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ-----LTS 177
Cdd:cd05041    75 VPGGSLLTFLR---KKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREeedgeYTV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  178 TRHRRNTSVGtpfWMAPEVIACEQqldttYDARCDTWSLGITAIEL-GDGDPPLADLHPMRALFKIPRNppPKLRQPELW 256
Cdd:cd05041   152 SDGLKQIPIK---WTAPEALNYGR-----YTSESDVWSFGILLWEIfSLGATPYPGMSNQQTREQIESG--YRMPAPELC 221
                         250       260
                  ....*....|....*....|....*..
gi 767960106  257 SAEFNDFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd05041   222 PEAVYRLMLQCWAYDPENRPSFSEIYN 248
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
21-230 7.05e-23

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 100.59  E-value: 7.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDpIHDIDEEIEA----EYNILKALSdHPNVVRFYgiyfkkDKVNGD-K 95
Cdd:cd07839     2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVR-LDDDDEGVPSsalrEICLLKELK-HKNIVRLY------DVLHSDkK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSggsvTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL 175
Cdd:cd07839    74 LTLVFEYCD----QDLKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAF 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  176 TSTRHRRNTSVGTPFWMAPEVIACEqqldTTYDARCDTWSLGITAIELGDGDPPL 230
Cdd:cd07839   150 GIPVRCYSAEVVTLWYRPPDVLFGA----KLYSTSIDMWSAGCIFAELANAGRPL 200
MBD_Myo3a cd21956
MORN4 binding domain (MBD) found in Myosin-IIIa and similar proteins; Myosin-IIIa, also called ...
1409-1456 7.27e-23

MORN4 binding domain (MBD) found in Myosin-IIIa and similar proteins; Myosin-IIIa, also called Myo3a, is a probable actin-based motor with ATPase and kinase activities. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Myosin-IIIa is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. It is required for normal cochlear hair bundle development and hearing, and plays an important role in the early steps of cochlear hair bundle morphogenesis. Mutations in human myosin-IIIA are responsible for progressive nonsyndromic hearing loss. This model corresponds to the MORN4 binding domain (MBD) in the tail of myosin-IIIa. MORN4 and its Drosophila ortholog retinophilin (RTP) are binding partners/cargos of class III myosins.


Pssm-ID: 439318 [Multi-domain]  Cd Length: 49  Bit Score: 92.91  E-value: 7.27e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 767960106 1409 KDNKDSKATSEREACGLAIFSKQISKLSEEYFILQKKLNEMILSQQLK 1456
Cdd:cd21956     1 KDRKDLKATSEKEACDLAIFSKQISKLSEKYLILQKKLNEMILSHQLK 48
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
27-259 7.50e-23

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 100.60  E-value: 7.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVK----ILDPIHDIDEEIEAEYNILKALsDHPNVVRFYGIYFKKDKVNGDKL-WLVLE 101
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGEYVAIKkcrqELSPSDKNRERWCLEVQIMKKL-NHPNVVSARDVPPELEKLSPNDLpLLAME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  102 LCSGGsvtDLVKgFLKRGER---MSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG---VKLVDFGVSAQL 175
Cdd:cd13989    80 YCSGG---DLRK-VLNQPENccgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGrviYKLIDLGYAKEL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 tsTRHRRNTS-VGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPP-LADLHPMRALFKIPRNPPPKLRQP 253
Cdd:cd13989   156 --DQGSLCTSfVGTLQYLAPELFESKK-----YTCTVDYWSFGTLAFECITGYRPfLPNWQPVQWHGKVKQKKPEHICAY 228

                  ....*.
gi 767960106  254 ELWSAE 259
Cdd:cd13989   229 EDLTGE 234
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
14-286 7.68e-23

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 99.79  E-value: 7.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   14 FPDpsdtweitETIGKGTYGKVFKVLNKKNGQKAAVKILDPI---HDIDEEIEAEYNILKALsDHPNVVRFYGIYFKKDK 90
Cdd:cd14082     6 FPD--------EVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLrfpTKQESQLRNEVAILQQL-SHPGVVNLECMFETPER 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   91 V-------NGDKLWLVLELCSGgsvtdlvkgflkrgeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG 163
Cdd:cd14082    77 VfvvmeklHGDMLEMILSSEKG---------------RLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEP 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  164 ---VKLVDFGVsAQLTSTRHRRNTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPL---ADLHPM- 236
Cdd:cd14082   142 fpqVKLCDFGF-ARIIGEKSFRRSVVGTPAYLAPEVL-----RNKGYNRSLDMWSVGVIIYVSLSGTFPFnedEDINDQi 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767960106  237 -RALFKIPRNPppklrqpelW---SAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd14082   216 qNAAFMYPPNP---------WkeiSPDAIDLINNLLQVKMRKRYSVDKSLSHPW 260
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
27-229 1.03e-22

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 101.03  E-value: 1.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDP---IHDIDEEIE-AEYNILKALSDHPNVVRFYGIYFKKDKvngdkLWLVLEL 102
Cdd:cd05591     3 LGKGSFGKVMLAERKGTDEVYAIKVLKKdviLQDDDVDCTmTEKRILALAAKHPFLTALHSCFQTKDR-----LFFVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGsvtDLVkgF-LKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHR 181
Cdd:cd05591    78 VNGG---DLM--FqIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKT 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 767960106  182 RNTSVGTPFWMAPEVIaceQQLDttYDARCDTWSLGITAIELGDGDPP 229
Cdd:cd05591   153 TTTFCGTPDYIAPEIL---QELE--YGPSVDWWALGVLMYEMMAGQPP 195
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
16-287 1.15e-22

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 99.69  E-value: 1.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDID-------EEIEAEYNILKALSdHPNVVRFYGIYFKK 88
Cdd:cd14195     2 MVEDHYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSsrrgvsrEEIEREVNILREIQ-HPNIITLHDIFENK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   89 DKVngdklWLVLELCSGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG----V 164
Cdd:cd14195    81 TDV-----VLILELVSGGELFD----FLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVpnprI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  165 KLVDFGVSAQLTSTRHRRNTsVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPR 244
Cdd:cd14195   152 KLIDFGIAHKIEAGNEFKNI-FGTPEFVAPEIVNYE-----PLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISA 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 767960106  245 -NPPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14195   226 vNYDFDEEYFSNTSELAKDFIRRLLVKDPKKRMTIAQSLEHSWI 269
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
27-317 1.27e-22

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 100.50  E-value: 1.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDpiHDIDEEIEAEYNILKALSDHPNVVRFYGIYFkkdkvngDKL--WLVLELCS 104
Cdd:cd14179    15 LGEGSFSICRKCLHKKTNQEYAVKIVS--KRMEANTQREIAALKLCEGHPNIVKLHEVYH-------DQLhtFLVMELLK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  105 GGSVTDLVKgflkRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG---VKLVDFGVSAQLTSTRHR 181
Cdd:cd14179    86 GGELLERIK----KKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDnseIKIIDFGFARLKPPDNQP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  182 RNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLaDLHPMRALFKIPRNPPPKLRQ------PEL 255
Cdd:cd14179   162 LKTPCFTLHYAAPELLN-----YNGYDESCDLWSLGVILYTMLSGQVPF-QCHDKSLTCTSAEEIMKKIKQgdfsfeGEA 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767960106  256 W---SAEFNDFISKCLTKDYEKRPTVSELLQHKFI---TQIEGKDVMLQKQL-TEFIGIHQCMGGTEKA 317
Cdd:cd14179   236 WknvSQEAKDLIQGLLTVDPNKRIKMSGLRYNEWLqdgSQLSSNPLMTPDILgSSGASVHTCVKATFHA 304
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
18-288 1.81e-22

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 99.70  E-value: 1.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   18 SDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPI-HDIDEEIEaeynILKALSDHPNVVRFYGIYfkkdkVNGDKL 96
Cdd:cd14177     3 TDVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSkRDPSEEIE----ILMRYGQHPNIITLKDVY-----DDGRYV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLVKgflkRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG----VKLVDFGVS 172
Cdd:cd14177    74 YLVTELMKGGELLDRIL----RQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSAnadsIRICDFGFA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLTSTRHRRNTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPLADLhpmralfkiPRNPPPKLRQ 252
Cdd:cd14177   150 KQLRGENGLLLTPCYTANFVAPEVL-----MRQGYDAACDIWSLGVLLYTMLAGYTPFANG---------PNDTPEEILL 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 767960106  253 pELWSAEFN--------------DFISKCLTKDYEKRPTVSELLQHKFIT 288
Cdd:cd14177   216 -RIGSGKFSlsggnwdtvsdaakDLLSHMLHVDPHQRYTAEQVLKHSWIA 264
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
25-284 1.88e-22

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 99.02  E-value: 1.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQKAAVK-ILDPIHDIDEEIEA--EYNILKALSDHPNVVRFYGIYfkkdkVNGDKLWLVLE 101
Cdd:cd14051     6 EKIGSGEFGSVYKCINRLDGCVYAIKkSKKPVAGSVDEQNAlnEVYAHAVLGKHPHVVRYYSAW-----AEDDHMIIQNE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  102 LCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLT-TEGGVKLVDFGVSAQLTSTRH 180
Cdd:cd14051    81 YCNGGSLADAISENEKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISrTPNPVSSEEEEEDFEGEEDNP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  181 RRN------------TSVGTPF-------WMAPEVIaceqQLDTTYDARCDTWSLGITAIELGDGDPpladlhpmralfk 241
Cdd:cd14051   161 ESNevtykigdlghvTSISNPQveegdcrFLANEIL----QENYSHLPKADIFALALTVYEAAGGGP------------- 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 767960106  242 IPRNPPP--KLRQPEL-----WSAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14051   224 LPKNGDEwhEIRQGNLpplpqCSPEFNELLRSMIHPDPEKRPSAAALLQH 273
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
21-287 2.01e-22

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 98.67  E-value: 2.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALS---------------DHPNVVRFYGIY 85
Cdd:cd14077     3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRASNAGLKKEREKRLEKEISrdirtireaalssllNHPHICRLRDFL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   86 FKKDKvngdkLWLVLELCSGGSVTDLVkgfLKRGeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVK 165
Cdd:cd14077    83 RTPNH-----YYMLFEYVDGGQLLDYI---ISHG-KLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  166 LVDFGVSaQLTSTRHRRNTSVGTPFWMAPEVIaceqqldttyDAR------CDTWSLGITAIELGDGDPPLADLHpMRAL 239
Cdd:cd14077   154 IIDFGLS-NLYDPRRLLRTFCGSLYFAAPELL----------QAQpytgpeVDVWSFGVVLYVLVCGKVPFDDEN-MPAL 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767960106  240 F-KIPRNpppKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14077   222 HaKIKKG---KVEYPSYLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
27-302 2.02e-22

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 100.04  E-value: 2.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDP--IHDIDEE--IEAEYNILKALSDHPNVVrfyGIYFKKDkvNGDKLWLVLEL 102
Cdd:cd05603     3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKktILKKKEQnhIMAERNVLLKNLKHPFLV---GLHYSFQ--TSEKLYFVLDY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGSVtdlvkgF--LKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRH 180
Cdd:cd05603    78 VNGGEL------FfhLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  181 RRNTSVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPppkLRQPELWSAEF 260
Cdd:cd05603   152 TTSTFCGTPEYLAPEVLRKE-----PYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKP---LHLPGGKTVAA 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767960106  261 NDFISKCLTKDYEKR----PTVSELLQHKFITQIEGKDvMLQKQLT 302
Cdd:cd05603   224 CDLLQGLLHKDQRRRlgakADFLEIKNHVFFSPINWDD-LYHKRIT 268
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
21-287 2.15e-22

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 98.52  E-value: 2.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEA----EYNILKALsDHPNVVRFYGIYFKKDkvngDKL 96
Cdd:cd14163     2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFIQRflprELQIVERL-DHKNIIHVYEMLESAD----GKI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLVkgflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLttEG-GVKLVDFGVSAQL 175
Cdd:cd14163    77 YLVMELAEDGDVFDCV----LHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL--QGfTLKLTDFGFAKQL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 -TSTRHRRNTSVGTPFWMAPEVIAceqqlDTTYDAR-CDTWSLGITAIELGDGDPPLADLHPMRALFKIPR--NPPPKLR 251
Cdd:cd14163   151 pKGGRELSQTFCGSTAYAAPEVLQ-----GVPHDSRkGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQQQKgvSLPGHLG 225
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767960106  252 QpelwSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14163   226 V----SRTCQDLLKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
27-302 2.16e-22

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 100.08  E-value: 2.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKIL--DPIHDIDE--EIEAEYNILKAlSDHPnvvrfYGIYFKKDKVNGDKLWLVLEL 102
Cdd:cd05595     3 LGKGTFGKVILVREKATGRYYAMKILrkEVIIAKDEvaHTVTESRVLQN-TRHP-----FLTALKYAFQTHDRLCFVMEY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGSVtdlvkgF--LKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRH 180
Cdd:cd05595    77 ANGGEL------FfhLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  181 RRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNpppKLRQPELWSAEF 260
Cdd:cd05595   151 TMKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILME---EIRFPRTLSPEA 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767960106  261 NDFISKCLTKDYEKR----PT-VSELLQHKFITQIEGKDVmLQKQLT 302
Cdd:cd05595   223 KSLLAGLLKKDPKQRlgggPSdAKEVMEHRFFLSINWQDV-VQKKLL 268
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
25-287 2.53e-22

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 98.54  E-value: 2.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLN-KKNGQKAAVKILDPIHDIDEEI--EAEYNILKALSdHPNVVRFYGIYFKKDKVngdklWLVLE 101
Cdd:cd14201    12 DLVGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSKSQIllGKEIKILKELQ-HENIVALYDVQEMPNSV-----FLVME 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  102 LCSGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEG---------GVKLVDFGVS 172
Cdd:cd14201    86 YCNGGDLAD----YLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIADFGFA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLTSTRhRRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPLADLHP--MRALFKIPRNPPPKL 250
Cdd:cd14201   162 RYLQSNM-MAATLCGSPMYMAPEVIMSQH-----YDAKADLWSIGTVIYQCLVGKPPFQANSPqdLRMFYEKNKNLQPSI 235
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767960106  251 rqPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14201   236 --PRETSPYLADLLLGLLQRNQKDRMDFEAFFSHPFL 270
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
19-291 2.55e-22

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 100.08  E-value: 2.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEE----IEAEYNILkALSDHPNVVRFYgiYFKKDKvngD 94
Cdd:cd05598     1 SMFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNqvahVKAERDIL-AEADNEWVVKLY--YSFQDK---E 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 KLWLVLELCSGGsvtDLVKGFLKRGeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:cd05598    75 NLYFVMDYIPGG---DLMSLLIKKG-IFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LTSTRHRR----NTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPLADLHPM---------RALFK 241
Cdd:cd05598   151 FRWTHDSKyylaHSLVGTPNYIAPEVL-----LRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAetqlkvinwRTTLK 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767960106  242 IPrnpppklRQPELwSAEFNDFISKcLTKDYEKR---PTVSELLQHKFITQIE 291
Cdd:cd05598   226 IP-------HEANL-SPEAKDLILR-LCCDAEDRlgrNGADEIKAHPFFAGID 269
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
22-281 2.66e-22

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 98.65  E-value: 2.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFK-VLNKKNGQKAAVKI----LDPIHDIDEEIEAEYNILKALsDHPNVVRFYGIyfkkdkVNGDKL 96
Cdd:cd05056     9 TLGRCIGEGQFGDVYQgVYMSPENEKIAVAVktckNCTSPSVREKFLQEAYIMRQF-DHPHIVKLIGV------ITENPV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLVKgflKRGERM-SEPLIAYILhEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL 175
Cdd:cd05056    82 WIVMELAPLGELRSYLQ---VNKYSLdLASLILYAY-QLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTRHRRNTSVGTPF-WMAPEVIACEQqldttYDARCDTWSLGITAIE-LGDGDPPLADLHPMRALFKIP---RNPPPKL 250
Cdd:cd05056   158 EDESYYKASKGKLPIkWMAPESINFRR-----FTSASDVWMFGVCMWEiLMLGVKPFQGVKNNDVIGRIEngeRLPMPPN 232
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767960106  251 RQPELWSaefndFISKCLTKDYEKRPTVSEL 281
Cdd:cd05056   233 CPPTLYS-----LMTKCWAYDPSKRPRFTEL 258
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
2-230 2.75e-22

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 100.84  E-value: 2.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    2 FPLIGKTIIFDNFPD--------------PSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEA--- 64
Cdd:cd05621    21 FPALRKNKNIDNFLNryekivnkirelqmKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAffw 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   65 EYNILKALSDHPNVVRFYgIYFKKDKvngdKLWLVLELCSGGSVTDLVKGFlkrgeRMSEPLIAYILHEALMGLQHLHNN 144
Cdd:cd05621   101 EERDIMAFANSPWVVQLF-CAFQDDK----YLYMVMEYMPGGDLVNLMSNY-----DVPEKWAKFYTAEVVLALDAIHSM 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  145 KTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRR-NTSVGTPFWMAPEVIAcEQQLDTTYDARCDTWSLGITAIEL 223
Cdd:cd05621   171 GLIHRDVKPDNMLLDKYGHLKLADFGTCMKMDETGMVHcDTAVGTPDYISPEVLK-SQGGDGYYGRECDWWSVGVFLFEM 249

                  ....*..
gi 767960106  224 GDGDPPL 230
Cdd:cd05621   250 LVGDTPF 256
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
21-302 2.94e-22

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 100.48  E-value: 2.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKIL--DPIHDiDEEI---EAEYNILKALSDHPNVVRFYGIYFKKDKvngdk 95
Cdd:cd05617    17 FDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVkkELVHD-DEDIdwvQTEKHVFEQASSNPFLVGLHSCFQTTSR----- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSGGsvtDLVKgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL 175
Cdd:cd05617    91 LFLVIEYVNGG---DLMF-HMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTRHRRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPL------ADLHPMRALFKIPRNPPpk 249
Cdd:cd05617   167 LGPGDTTSTFCGTPNYIAPEILRGEE-----YGFSVDWWALGVLMFEMMAGRSPFdiitdnPDMNTEDYLFQVILEKP-- 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767960106  250 LRQPELWSAEFNDFISKCLTKDYEKR------PTVSELLQHKFITQIEGkDVMLQKQLT 302
Cdd:cd05617   240 IRIPRFLSVKASHVLKGFLNKDPKERlgcqpqTGFSDIKSHTFFRSIDW-DLLEKKQVT 297
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
27-281 4.00e-22

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 97.97  E-value: 4.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAeyniLKALSDhPNVVRFYGIYFKKDKVNgdklwLVLELCSGG 106
Cdd:cd13991    14 IGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRAEELMA----CAGLTS-PRVVPLYGAVREGPWVN-----IFMDLKEGG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  107 SVTDLVKgflKRGeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG-VKLVDFGVSAQL-----TSTRH 180
Cdd:cd13991    84 SLGQLIK---EQG-CLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSdAFLCDFGHAECLdpdglGKSLF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  181 RRNTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQPELWSAEF 260
Cdd:cd13991   160 TGDYIPGTETHMAPEVV-----LGKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIANEPPPLREIPPSCAPLT 234
                         250       260
                  ....*....|....*....|.
gi 767960106  261 NDFISKCLTKDYEKRPTVSEL 281
Cdd:cd13991   235 AQAIQAGLRKEPVHRASAAEL 255
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
27-286 4.16e-22

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 98.16  E-value: 4.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEA--------EYNILKALsDHPNVVRFYGIYfkkdKVNGDKLWL 98
Cdd:cd13990     8 LGKGGFSEVYKAFDLVEQRYVACKIHQLNKDWSEEKKQnyikhalrEYEIHKSL-DHPRIVKLYDVF----EIDTDSFCT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   99 VLELCSGgsvTDLvKGFLKRGERMSEPLIAYILHEALMGLQHLHN--NKTIHRDVKGNNILL---TTEGGVKLVDFGVSA 173
Cdd:cd13990    83 VLEYCDG---NDL-DFYLKQHKSIPEREARSIIMQVVSALKYLNEikPPIIHYDLKPGNILLhsgNVSGEIKITDFGLSK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  174 QLTStRHRRN-----TS--VGTPFWMAPEviaCeqqLDTTYDAR-----CDTWSLGITAIELGDGDPPLA-DLHPMRALF 240
Cdd:cd13990   159 IMDD-ESYNSdgmelTSqgAGTYWYLPPE---C---FVVGKTPPkisskVDVWSVGVIFYQMLYGRKPFGhNQSQEAILE 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767960106  241 -KIPRNP-----PPKlrqPELwSAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd13990   232 eNTILKAtevefPSK---PVV-SSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
23-282 5.63e-22

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 97.42  E-value: 5.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   23 ITETIGKGTYGKVFKVLnkKNGQKAAVKIL--DPIHDIDEEIEA--EYNILKALSDHPNVVRFYGIYFKKDKvngdkLWL 98
Cdd:cd14145    10 LEEIIGIGGFGKVYRAI--WIGDEVAVKAArhDPDEDISQTIENvrQEAKLFAMLKHPNIIALRGVCLKEPN-----LCL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   99 VLELCSGGSVTDLVKGflkrgERMSEPLIAYILHEALMGLQHLHNNK---TIHRDVKGNNILL--TTEGG------VKLV 167
Cdd:cd14145    83 VMEFARGGPLNRVLSG-----KRIPPDILVNWAVQIARGMNYLHCEAivpVIHRDLKSSNILIleKVENGdlsnkiLKIT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  168 DFGVSAQLTSTRhrRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNpP 247
Cdd:cd14145   158 DFGLAREWHRTT--KMSAAGTYAWMAPEVIR-----SSMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMN-K 229
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767960106  248 PKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELL 282
Cdd:cd14145   230 LSLPIPSTCPEPFARLMEDCWNPDPHSRPPFTNIL 264
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
18-230 7.35e-22

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 100.08  E-value: 7.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   18 SDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEA---EYNILKALSDHPNVVR-FYGiyFKKDKVng 93
Cdd:cd05622    72 AEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAffwEERDIMAFANSPWVVQlFYA--FQDDRY-- 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   94 dkLWLVLELCSGGSVTDLVKGFlkrgeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSA 173
Cdd:cd05622   148 --LYMVMEYMPGGDLVNLMSNY-----DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCM 220
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767960106  174 QLTSTRHRR-NTSVGTPFWMAPEVIAcEQQLDTTYDARCDTWSLGITAIELGDGDPPL 230
Cdd:cd05622   221 KMNKEGMVRcDTAVGTPDYISPEVLK-SQGGDGYYGRECDWWSVGVFLYEMLVGDTPF 277
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
27-286 1.11e-21

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 96.61  E-value: 1.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAA-----VKILDPI--HDIDEEIEaeynILKALSdHPNVVRFYGIYfkKDKVNGDK-LWL 98
Cdd:cd14033     9 IGRGSFKTVYRGLDTETTVEVAwcelqTRKLSKGerQRFSEEVE----MLKGLQ-HPNIVRFYDSW--KSTVRGHKcIIL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   99 VLELCSGGSvtdlVKGFLKRGERMSEPLIAYILHEALMGLQHLHNN--KTIHRDVKGNNILLT-TEGGVKLVDFGVsAQL 175
Cdd:cd14033    82 VTELMTSGT----LKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRcpPILHRDLKCDNIFITgPTGSVKIGDLGL-ATL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTRHRRNTsVGTPFWMAPEViaceqqLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALF-KIPRNPPP----KL 250
Cdd:cd14033   157 KRASFAKSV-IGTPEFMAPEM------YEEKYDEAVDVYAFGMCILEMATSEYPYSECQNAAQIYrKVTSGIKPdsfyKV 229
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767960106  251 RQPELwsaefNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd14033   230 KVPEL-----KEIIEGCIRTDKDERFTIQDLLEHRF 260
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
25-286 1.22e-21

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 96.80  E-value: 1.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQKAAVKILDpihdIDEEIEA-------EYNILKALsDHPNVVRFYGIYFkkdkvNGDKLW 97
Cdd:cd07860     6 EKIGEGTYGVVYKARNKLTGEVVALKKIR----LDTETEGvpstairEISLLKEL-NHPNIVKLLDVIH-----TENKLY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSggsvTDLvKGFLK--RGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL 175
Cdd:cd07860    76 LVFEFLH----QDL-KKFMDasALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTRHRRNTSVGTPFWMAPEV-IACEqqldtTYDARCDTWSLGITAIEL--------GDGD------------------- 227
Cdd:cd07860   151 GVPVRTYTHEVVTLWYRAPEIlLGCK-----YYSTAVDIWSLGCIFAEMvtrralfpGDSEidqlfrifrtlgtpdevvw 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767960106  228 PPLADLHPMRALFkiPRNPPPKLRQ--PELwSAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd07860   226 PGVTSMPDYKPSF--PKWARQDFSKvvPPL-DEDGRDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
25-286 1.26e-21

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 96.98  E-value: 1.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDiDEEIEA----EYNILKALSdHPNVVRFYGIYFKkdkvnGDKLWLVL 100
Cdd:cd07835     5 EKIGEGTYGVVYKARDKLTGEIVALKKIRLETE-DEGVPStairEISLLKELN-HPNIVRLLDVVHS-----ENKLYLVF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCSggsvTDLVKGFLKRGERMSEP-LIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVsAQLTSTR 179
Cdd:cd07835    78 EFLD----LDLKKYMDSSPLTGLDPpLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGL-ARAFGVP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  180 HRRNT-SVGTPFWMAPEVIACEQQldttYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKI---------------- 242
Cdd:cd07835   153 VRTYThEVVTLWYRAPEILLGSKH----YSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIfrtlgtpdedvwpgvt 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  243 ---------PRNPPPKLRQ--PELwSAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd07835   229 slpdykptfPKWARQDLSKvvPSL-DEDGLDLLSQMLVYDPAKRISAKAALQHPY 282
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
21-286 1.31e-21

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 96.21  E-value: 1.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSdHPNVVRfygiyFKKDKVNGDKLWLVL 100
Cdd:cd14665     2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDENVQREIINHRSLR-HPNIVR-----FKEVILTPTHLAIVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCSGGsvtDLVKGFLKRGeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILL--TTEGGVKLVDFGVSAqlTST 178
Cdd:cd14665    76 EYAAGG---ELFERICNAG-RFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLdgSPAPRLKICDFGYSK--SSV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  179 RHRR-NTSVGTPFWMAPEVIaceqqLDTTYDAR-CDTWSLGITAIELGDGDPPLADLHPMRALFK-IPRNPPPKLRQPEL 255
Cdd:cd14665   150 LHSQpKSTVGTPAYIAPEVL-----LKKEYDGKiADVWSCGVTLYVMLVGAYPFEDPEEPRNFRKtIQRILSVQYSIPDY 224
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767960106  256 --WSAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd14665   225 vhISPECRHLISRIFVADPATRITIPEIRNHEW 257
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
27-279 1.67e-21

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 95.80  E-value: 1.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFK-VLNKKNGQK-AAVKIL-----DPihDIDEEIEAEYNILKALsDHPNVVRFYGIyfkkdkVNGDKLWLV 99
Cdd:cd05116     3 LGSGNFGTVKKgYYQMKKVVKtVAVKILkneanDP--ALKDELLREANVMQQL-DNPYIVRMIGI------CEAESWMLV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  100 LELCSGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTR 179
Cdd:cd05116    74 MEMAELGPLNK----FLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  180 --HRRNTSVGTPF-WMAPEVIACEQqldttYDARCDTWSLGITAIE-LGDGDPPLADLHPMRALFKIPRNppPKLRQPEL 255
Cdd:cd05116   150 nyYKAQTHGKWPVkWYAPECMNYYK-----FSSKSDVWSFGVLMWEaFSYGQKPYKGMKGNEVTQMIEKG--ERMECPAG 222
                         250       260
                  ....*....|....*....|....
gi 767960106  256 WSAEFNDFISKCLTKDYEKRPTVS 279
Cdd:cd05116   223 CPPEMYDLMKLCWTYDVDERPGFA 246
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
19-289 2.04e-21

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 97.44  E-value: 2.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILdpIHDIDEEIEA-----EYNILKALSdHPNVVRFYGIYFKKDKVN- 92
Cdd:cd07855     5 DRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKI--PNAFDVVTTAkrtlrELKILRHFK-HDNIIAIRDILRPKVPYAd 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   93 GDKLWLVLELCSGgsvtDLVKgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS 172
Cdd:cd07855    82 FKDVYVVLDLMES----DLHH-IIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLTS--TRHRRNTS--VGTPFWMAPEVIACEQQldttYDARCDTWSLG-ITAIELGD--------------------GD 227
Cdd:cd07855   157 RGLCTspEEHKYFMTeyVATRWYRAPELMLSLPE----YTQAIDMWSVGcIFAEMLGRrqlfpgknyvhqlqliltvlGT 232
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  228 PPLADLHPMRA------LFKIPRNPP-------PKLRQPELwsaefnDFISKCLTKDYEKRPTVSELLQHKFITQ 289
Cdd:cd07855   233 PSQAVINAIGAdrvrryIQNLPNKQPvpwetlyPKADQQAL------DLLSQMLRFDPSERITVAEALQHPFLAK 301
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
27-283 2.13e-21

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 96.14  E-value: 2.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKknGQKAAVKILDPI---------------HDIDE-------EIEAEYNILKALSdHPNVVRFYGI 84
Cdd:cd14000     2 LGDGGFGSVYRASYK--GEPVAVKIFNKHtssnfanvpadtmlrHLRATdamknfrLLRQELTVLSHLH-HPSIVYLLGI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   85 YFKKdkvngdkLWLVLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTT---- 160
Cdd:cd14000    79 GIHP-------LMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVWTlypn 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  161 -EGGVKLVDFGVSAQltSTRHRRNTSVGTPFWMAPEVIACEQQldttYDARCDTWSLGITAIELGDGDPPLADLHPMRAL 239
Cdd:cd14000   152 sAIIIKIADYGISRQ--CCRMGAKGSEGTPGFRAPEIARGNVI----YNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNE 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767960106  240 FKIPRNPPPKLRQPE--LWSaEFNDFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd14000   226 FDIHGGLRPPLKQYEcaPWP-EVEVLMKKCWKENPQQRPTAVTVVS 270
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
27-284 2.16e-21

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 95.41  E-value: 2.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSdHPNVVRFYGIYfkkdkVNGDKLWLVLELCSGG 106
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQ-HPQYITLHDTY-----ESPTSYILVLELMDDG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  107 SVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTE---GGVKLVDFGVSAQLTSTRHRRN 183
Cdd:cd14115    75 RLLD----YLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHRHVHH 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  184 TsVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPR---NPPPKLRQPELWSAEf 260
Cdd:cd14115   151 L-LGNPEFAAPEVIQ-----GTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRvdfSFPDEYFGDVSQAAR- 223
                         250       260
                  ....*....|....*....|....
gi 767960106  261 nDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14115   224 -DFINVILQEDPRRRPTAATCLQH 246
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
21-287 2.19e-21

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 96.18  E-value: 2.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILD--------PIHDIdeeieAEYNILKALS--DHPNVVRFYGIYFKKDK 90
Cdd:cd07863     2 YEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRvqtnedglPLSTV-----REVALLKRLEafDHPNIVRLMDVCATSRT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   91 VNGDKLWLVLElcsggSVTDLVKGFLKRGERMSEPL--IAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVD 168
Cdd:cd07863    77 DRETKVTLVFE-----HVDQDLRTYLDKVPPPGLPAetIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLAD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  169 FGVsAQLTSTRHRRNTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIEL--------GDGDP------------ 228
Cdd:cd07863   152 FGL-ARIYSCQMALTPVVVTLWYRAPEVL-----LQSTYATPVDMWSVGCIFAEMfrrkplfcGNSEAdqlgkifdligl 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  229 PLADLHPM-----RALFKiPRNPPPKLR-QPELwSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd07863   226 PPEDDWPRdvtlpRGAFS-PRGPRPVQSvVPEI-EESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
22-289 2.24e-21

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 95.81  E-value: 2.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVK--ILDPIHDIdEEIEAEYNILKALSDHPNVVRFYGIYFKKDKVNGDKLWLV 99
Cdd:cd14037     6 TIEKYLAEGGFAHVYLVKTSNGGNRAALKrvYVNDEHDL-NVCKREIEIMKRLSGHKNIVGYIDSSANRSGNGVYEVLLL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  100 LELCSGGSVTDLVKGFLKrgERMSEPLIAYILHEALMGLQHLHNNKT--IHRDVKGNNILLTTEGGVKLVDFG-VSAQLT 176
Cdd:cd14037    85 MEYCKGGGVIDLMNQRLQ--TGLTESEILKIFCDVCEAVAAMHYLKPplIHRDLKVENVLISDSGNYKLCDFGsATTKIL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRHR-----------RNTsvgTPFWMAPEVIACEQQLDTTYDArcDTWSLGITAIEL-------GDGDpPLADLHpmrA 238
Cdd:cd14037   163 PPQTKqgvtyveedikKYT---TLQYRAPEMIDLYRGKPITEKS--DIWALGCLLYKLcfyttpfEESG-QLAILN---G 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767960106  239 LFKIPRNPPpklrqpelWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQ 289
Cdd:cd14037   234 NFTFPDNSR--------YSKRLHKLIRYMLEEDPEKRPNIYQVSYEAFELA 276
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
25-287 2.70e-21

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 96.25  E-value: 2.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQKAAVKILD--PIHdIDEEIEAEYNILKALSDHPNVVRFYGiYFKKDkvngDKLWLVLEL 102
Cdd:cd14173     8 EVLGEGAYARVQTCINLITNKEYAVKIIEkrPGH-SRSRVFREVEMLYQCQGHRNVLELIE-FFEEE----DKFYLVFEK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTE---GGVKLVDF--GVSAQLTS 177
Cdd:cd14173    82 MRGGSILS----HIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPnqvSPVKICDFdlGSGIKLNS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  178 -----TRHRRNTSVGTPFWMAPEVIACEQQLDTTYDARCDTWSLGITAIELGDGDPPLADL----------HPMRA---- 238
Cdd:cd14173   158 dcspiSTPELLTPCGSAEYMAPEVVEAFNEEASIYDKRCDLWSLGVILYIMLSGYPPFVGRcgsdcgwdrgEACPAcqnm 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767960106  239 LFKIPRNppPKLRQPEL-W---SAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14173   238 LFESIQE--GKYEFPEKdWahiSCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
18-304 3.11e-21

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 96.05  E-value: 3.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   18 SDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIhdIDEEI-EAEYNILKALSdHPNVVRFYGIYfkKDKVNgdkL 96
Cdd:cd14085     2 EDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKT--VDKKIvRTEIGVLLRLS-HPNIIKLKEIF--ETPTE---I 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLV--KGFlkrgerMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG---VKLVDFGV 171
Cdd:cd14085    74 SLVLELVTGGELFDRIveKGY------YSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  172 SaQLTSTRHRRNTSVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLR 251
Cdd:cd14085   148 S-KIVDQQVTMKTVCGTPGYCAPEILRGC-----AYGPEVDMWSVGVITYILLCGFEPFYDERGDQYMFKRILNCDYDFV 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  252 QPelW----SAEFNDFISKCLTKDYEKRPTVSELLQHKFITQIEGKDVML---QKQLTEF 304
Cdd:cd14085   222 SP--WwddvSLNAKDLVKKLIVLDPKKRLTTQQALQHPWVTGKAANFAHMdtaQKKLQEF 279
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
27-286 4.10e-21

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 95.90  E-value: 4.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDpihdIDEEIEA-------EYNILKALSdHPNVVRFygiyfkKDKVNGDKL--- 96
Cdd:cd07845    15 IGEGTYGIVYRARDTTSGEIVALKKVR----MDNERDGipisslrEITLLLNLR-HPNIVEL------KEVVVGKHLdsi 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSG--GSVTDLVKgflkrgERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:cd07845    84 FLVMEYCEQdlASLLDNMP------TPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLART 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LTSTRHRRNTSVGTPFWMAPEVIACeqqlDTTYDARCDTWSLGITAIELGDGDPPL------------------------ 230
Cdd:cd07845   158 YGLPAKPMTPKVVTLWYRAPELLLG----CTTYTTAIDMWAVGCILAELLAHKPLLpgkseieqldliiqllgtpnesiw 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  231 ---ADLhPMRALFKIPRNPPPKLRQPELWSAEFN-DFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd07845   234 pgfSDL-PLVGKFTLPKQPYNNLKHKFPWLSEAGlRLLNFLLMYDPKKRATAEEALESSY 292
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
19-287 4.53e-21

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 95.48  E-value: 4.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEIT-ETIGKGTYGKVFKVLNKKNGQKAAVKILDPI--HD---IDEEIEAEY------NILKALSDHPNVVRFYgiyf 86
Cdd:cd14174     1 DLYRLTdELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNagHSrsrVFREVETLYqcqgnkNILELIEFFEDDTRFY---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   87 kkdkvngdklwLVLELCSGGSVTdlvkGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTE---GG 163
Cdd:cd14174    77 -----------LVFEKLRGGSIL----AHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPdkvSP 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  164 VKLVDF--GVSAQLTS-----TRHRRNTSVGTPFWMAPEVIACEQQLDTTYDARCDTWSLGITAIELGDGDPPL-----A 231
Cdd:cd14174   142 VKICDFdlGSGVKLNSactpiTTPELTTPCGSAEYMAPEVVEVFTDEATFYDKRCDLWSLGVILYIMLSGYPPFvghcgT 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767960106  232 DLHPMRA---------LFKipRNPPPKLRQPE-LW---SAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14174   222 DCGWDRGevcrvcqnkLFE--SIQEGKYEFPDkDWshiSSEAKDLISKLLVRDAKERLSAAQVLQHPWV 288
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
27-229 4.64e-21

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 96.22  E-value: 4.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKIL---DPIH-DIDEEIEAEYNILKALSD--HPNVVRFYGIYFKKDKVngdklWLVL 100
Cdd:cd05589     7 LGRGHFGKVLLAEYKPTGELFAIKALkkgDIIArDEVESLMCEKRIFETVNSarHPFLVNLFACFQTPEHV-----CFVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCSGGsvtDLVKGFlkRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRH 180
Cdd:cd05589    82 EYAAGG---DLMMHI--HEDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGD 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 767960106  181 RRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPP 229
Cdd:cd05589   157 RTSTFCGTPEFLAPEVLT-----DTSYTRAVDWWGLGVLIYEMLVGESP 200
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
27-218 4.65e-21

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 94.70  E-value: 4.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVRFYGIYFKKDkvngDKLWLVLELCSGG 106
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFLREYNISLELSVHPHIIKTYDVAFETE----DYYVFAQEYAPYG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  107 SVTDLVKGflKRGerMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEG--GVKLVDFGVSAQLTSTRHRRNT 184
Cdd:cd13987    77 DLFSIIPP--QVG--LPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDcrRVKLCDFGLTRRVGSTVKRVSG 152
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 767960106  185 SvgTPFwMAPEViaCEQQLDTTY--DARCDTWSLGI 218
Cdd:cd13987   153 T--IPY-TAPEV--CEAKKNEGFvvDPSIDVWAFGV 183
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
27-223 4.75e-21

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 95.01  E-value: 4.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQkaaVKILDPIHDIDEEIE----AEYNILKALsDHPNVVRFYGIYFKKDKVNgdklwLVLEL 102
Cdd:cd14222     1 LGKGFFGQAIKVTHKATGK---VMVMKELIRCDEETQktflTEVKVMRSL-DHPNVLKFIGVLYKDKRLN-----LLTEF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT------ 176
Cdd:cd14222    72 IEGGTLKD----FLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVeekkkp 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767960106  177 --------------STRHRRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIEL 223
Cdd:cd14222   148 ppdkpttkkrtlrkNDRKKRYTVVGNPYWMAPEMLNGKS-----YDEKVDIFSFGIVLCEI 203
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
27-283 6.16e-21

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 94.38  E-value: 6.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKknGQKAAVKI--LDPIHDIDEEIEA---EYNILKALSdHPNVVRFYGIYfkkdkVNGDKLWLVLE 101
Cdd:cd14061     2 IGVGGFGKVYRGIWR--GEEVAVKAarQDPDEDISVTLENvrqEARLFWMLR-HPNIIALRGVC-----LQPPNLCLVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  102 LCSGGSVTDLVKGFLKRGERmsepLIAYILHEAlMGLQHLHNNK---TIHRDVKGNNILL--------TTEGGVKLVDFG 170
Cdd:cd14061    74 YARGGALNRVLAGRKIPPHV----LVDWAIQIA-RGMNYLHNEApvpIIHRDLKSSNILIleaienedLENKTLKITDFG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  171 VSAQLTSTRhrRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRN----P 246
Cdd:cd14061   149 LAREWHKTT--RMSAAGTYAWMAPEVIK-----SSTFSKASDVWSYGVLLWELLTGEVPYKGIDGLAVAYGVAVNkltlP 221
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767960106  247 PPKlRQPElwsaEFNDFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd14061   222 IPS-TCPE----PFAQLMKDCWQPDPHDRPSFADILK 253
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
24-284 7.07e-21

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 94.84  E-value: 7.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   24 TETIGKGTYGKVFKVLNKKNGQKAAVKILdpihdIDE-EIEAEYNILKALSDHPNVVRFYGIY-----FKKDKVNGDKLW 97
Cdd:cd14171    11 TQKLGTGISGPVRVCVKKSTGERFALKIL-----LDRpKARTEVRLHMMCSGHPNIVQIYDVYansvqFPGESSPRARLL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVTDLV---KGFLKRGERMsepliaYILHEALmGLQHLHNNKTIHRDVKGNNILL---TTEGGVKLVDFGV 171
Cdd:cd14171    86 IVMELMEGGELFDRIsqhRHFTEKQAAQ------YTKQIAL-AVQHCHSLNIAHRDLKPENLLLkdnSEDAPIKLCDFGF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  172 sAQLTSTRHRrnTSVGTPFWMAPEVIACEQQLDT------------TYDARCDTWSLGITAIELGDGDPPLADLHPMRAl 239
Cdd:cd14171   159 -AKVDQGDLM--TPQFTPYYVAPQVLEAQRRHRKersgiptsptpyTYDKSCDMWSLGVIIYIMLCGYPPFYSEHPSRT- 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767960106  240 fkIPRNPPPKL-----RQPEL-WSA---EFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14171   235 --ITKDMKRKImtgsyEFPEEeWSQiseMAKDIVRKLLCVDPEERMTIEEVLHH 286
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
23-283 7.08e-21

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 94.50  E-value: 7.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   23 ITETIGKGTYGKVFKVLNKKNGQKAAVK-ILDPIHDIDEEIEAEYNILKALSDHPNVVRFYG---IYFKKDKVNGDKLWL 98
Cdd:cd14036     4 IKRVIAEGGFAFVYEAQDVGTGKEYALKrLLSNEEEKNKAIIQEINFMKKLSGHPNIVQFCSaasIGKEESDQGQAEYLL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   99 VLELCSGGSVtDLVKGfLKRGERMSEPLIAYILHEALMGLQHLHNNK--TIHRDVKGNNILLTTEGGVKLVDFGvSAQLT 176
Cdd:cd14036    84 LTELCKGQLV-DFVKK-VEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFG-SATTE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 S-------TRHRRN------TSVGTPFWMAPEVIACEQQLDTTydARCDTWSLGITAIELGDGDPPLAD---LHPMRALF 240
Cdd:cd14036   161 AhypdyswSAQKRSlvedeiTRNTTPMYRTPEMIDLYSNYPIG--EKQDIWALGCILYLLCFRKHPFEDgakLRIINAKY 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 767960106  241 KIPRNPppklRQPELwsaeFNDFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd14036   239 TIPPND----TQYTV----FHDLIRSTLKVNPEERLSITEIVE 273
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
19-291 7.96e-21

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 96.28  E-value: 7.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEE----IEAEYNILkALSDHPNVVRFYgiYFKKDKVNgd 94
Cdd:cd05627     2 DDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEqvahIRAERDIL-VEADGAWVVKMF--YSFQDKRN-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 kLWLVLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:cd05627    77 -LYLIMEFLPGGDMMTL----LMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 L--------------------------------TSTRHRRN---TSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGIT 219
Cdd:cd05627   152 LkkahrtefyrnlthnppsdfsfqnmnskrkaeTWKKNRRQlaySTVGTPDYIAPEVF-----MQTGYNKLCDWWSLGVI 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767960106  220 AIELGDGDPPLADLHPMRALFKIPRNPPPKLRQPEL-WSAEFNDFISKCLTkDYEKR---PTVSELLQHKFITQIE 291
Cdd:cd05627   227 MYEMLIGYPPFCSETPQETYRKVMNWKETLVFPPEVpISEKAKDLILRFCT-DAENRigsNGVEEIKSHPFFEGVD 301
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
27-283 8.62e-21

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 93.74  E-value: 8.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDpiHDIDEE-IEAEYNILKALSdHPNVVRFYGIYFKKDKvngdkLWLVLELCSG 105
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKIYK--NDVDQHkIVREISLLQKLS-HPNIVRYLGICVKDEK-----LHPILEYVSG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  106 GSVTDLvkgfLKRGE-----RMSEPLIAYILHealmGLQHLHNNKTIHRDVKGNNILLTTEGGVK---LVDFGVSAQL-- 175
Cdd:cd14156    73 GCLEEL----LAREElplswREKVELACDISR----GMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREVge 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 --TSTRHRRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPLADLHPMR-------ALFK--IPR 244
Cdd:cd14156   145 mpANDPERKLSLVGSAFWMAPEMLRGEP-----YDRKVDVFSFGIVLCEILARIPADPEVLPRTgdfgldvQAFKemVPG 219
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767960106  245 NPPPKLrqpelwsaefnDFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd14156   220 CPEPFL-----------DLAASCCRMDAFKRPSFAELLD 247
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
27-279 8.95e-21

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 95.16  E-value: 8.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVF---KVLNKKNGQKAAVKILDP----IHDiDEEIEAEYNILKALSdHPNVVRFYgiY-FKKDkvngDKLWL 98
Cdd:cd05582     3 LGQGSFGKVFlvrKITGPDAGTLYAMKVLKKatlkVRD-RVRTKMERDILADVN-HPFIVKLH--YaFQTE----GKLYL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   99 VLELCSGGSV-TDLVKGFLkrgerMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 177
Cdd:cd05582    75 ILDFLRGGDLfTRLSKEVM-----FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESID 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  178 TRHRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLAD--------------------LHP-- 235
Cdd:cd05582   150 HEKKAYSFCGTVEYMAPEVVN-----RRGHTQSADWWSFGVLMFEMLTGSLPFQGkdrketmtmilkaklgmpqfLSPea 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767960106  236 ---MRALFKipRNPPPKL-----------RQPELWSAEFNDFISKCLTKDYekRPTVS 279
Cdd:cd05582   225 qslLRALFK--RNPANRLgagpdgveeikRHPFFATIDWNKLYRKEIKPPF--KPAVS 278
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
19-284 9.18e-21

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 93.94  E-value: 9.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEE--IEAEYNILKALSdHPNVvrfygIYFKKDKVNGDKL 96
Cdd:cd14184     1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEhlIENEVSILRRVK-HPNI-----IMLIEEMDTPAEL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLVKGFLKRGERMSEPLIaYILHEALmglQHLHNNKTIHRDVKGNNILLTT----EGGVKLVDFGVS 172
Cdd:cd14184    75 YLVMELVKGGDLFDAITSSTKYTERDASAMV-YNLASAL---KYLHGLCIVHRDIKPENLLVCEypdgTKSLKLGDFGLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLTSTRHrrnTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPL-------ADLHPMRALFKIpRN 245
Cdd:cd14184   151 TVVEGPLY---TVCGTPTYVAPEIIA-----ETGYGLKVDIWAAGVITYILLCGFPPFrsennlqEDLFDQILLGKL-EF 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767960106  246 PPPklrqpeLW---SAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14184   222 PSP------YWdniTDSAKELISHMLQVNVEARYTAEQILSH 257
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
23-287 1.06e-20

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 93.70  E-value: 1.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   23 ITETIGKGTYGKV-----FKVLNKKNGQKAAVKIL--DPIHDIDEE--IEAEYNILKALSdHPNVVRFYGIyFKKDKVNG 93
Cdd:cd14076     5 LGRTLGEGEFGKVklgwpLPKANHRSGVQVAIKLIrrDTQQENCQTskIMREINILKGLT-HPNIVRLLDV-LKTKKYIG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   94 dklwLVLELCSGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSA 173
Cdd:cd14076    83 ----IVLEFVSGGELFD----YILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFAN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  174 QL-TSTRHRRNTSVGTPFWMAPEVIACeqqlDTTYDAR-CDTWSLGIT--AIELG----DGDPPLADLHPMRALFKIPRN 245
Cdd:cd14076   155 TFdHFNGDLMSTSCGSPCYAAPELVVS----DSMYAGRkADIWSCGVIlyAMLAGylpfDDDPHNPNGDNVPRLYRYICN 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767960106  246 PPpkLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14076   231 TP--LIFPEYVTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
27-299 1.23e-20

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 94.73  E-value: 1.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKIL--DPIHDIDE--EIEAEYNILKAlSDHPnvvrfYGIYFKKDKVNGDKLWLVLEL 102
Cdd:cd05571     3 LGKGTFGKVILCREKATGELYAIKILkkEVIIAKDEvaHTLTENRVLQN-TRHP-----FLTSLKYSFQTNDRLCFVMEY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGSVtdlvkgF--LKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRH 180
Cdd:cd05571    77 VNGGEL------FfhLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  181 RRNTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPLADlHPMRALFKIPRNPPpkLRQPELWSAEF 260
Cdd:cd05571   151 TTKTFCGTPEYLAPEVL-----EDNDYGRAVDWWGLGVVMYEMMCGRLPFYN-RDHEVLFELILMEE--VRFPSTLSPEA 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 767960106  261 NDFISKCLTKDYEKR-----PTVSELLQHKFITQIEGKDVMLQK 299
Cdd:cd05571   223 KSLLAGLLKKDPKKRlgggpRDAKEIMEHPFFASINWDDLYQKK 266
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
27-287 1.29e-20

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 93.38  E-value: 1.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKIldpihdIDEE---------IEAEYNILKALsDHPNVvrfygIYFKKDKVNGDKLW 97
Cdd:cd14097     9 LGQGSFGVVIEATHKETQTKWAIKK------INREkagssavklLEREVDILKHV-NHAHI-----IHLEEVFETPKRMY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEG-------GVKLVDFG 170
Cdd:cd14097    77 LVMELCEDGELKEL----LLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIidnndklNIKVTDFG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  171 VSAQL--TSTRHRRNTsVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPLADlHPMRALFKIPRNPPP 248
Cdd:cd14097   153 LSVQKygLGEDMLQET-CGTPIYMAPEVISAHG-----YSQQCDIWSIGVIMYMLLCGEPPFVA-KSEEKLFEEIRKGDL 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767960106  249 KLRQpELW---SAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14097   226 TFTQ-SVWqsvSDAAKNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
22-286 1.48e-20

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 93.06  E-value: 1.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFK-------VLNKKNGQKAAVKIL----DPIHdideeIEAEYNILKALSDHPNVvrfygIYFKKDK 90
Cdd:cd14019     4 RIIEKIGEGTFSSVYKaedklhdLYDRNKGRLVALKHIyptsSPSR-----ILNELECLERLGGSNNV-----SGLITAF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   91 VNGDKLWLVLELCSGGSVTDLVKgflkrgeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILL--TTEGGVkLVD 168
Cdd:cd14019    74 RNEDQVVAVLPYIEHDDFRDFYR-------KMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYnrETGKGV-LVD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  169 FGVsAQLTSTRHRRNTS-VGTPFWMAPEVI-ACEQQldTTydaRCDTWSLGITAIELGDGD-PPLADLHPMRALFKIprn 245
Cdd:cd14019   146 FGL-AQREEDRPEQRAPrAGTRGFRAPEVLfKCPHQ--TT---AIDIWSAGVILLSILSGRfPFFFSSDDIDALAEI--- 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767960106  246 ppPKLRQpelwSAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd14019   217 --ATIFG----SDEAYDLLDKLLELDPSKRITAEEALKHPF 251
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
19-229 1.55e-20

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 94.72  E-value: 1.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDpihdideeieaEYNILKalsdhpnvvRFYGIYFKKDK---VNGDK 95
Cdd:cd05597     1 DDFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILN-----------KWEMLK---------RAETACFREERdvlVNGDR 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LW---------------LVLELCSGGsvtDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTT 160
Cdd:cd05597    61 RWitklhyafqdenylyLVMDYYCGG---DLLTLLSKFEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDR 137
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  161 EGGVKLVDFGVSAQLTSTRH-RRNTSVGTPFWMAPEVIACEQQLDTTYDARCDTWSLGITAIELGDGDPP 229
Cdd:cd05597   138 NGHIRLADFGSCLKLREDGTvQSSVAVGTPDYISPEILQAMEDGKGRYGPECDWWSLGVCMYEMLYGETP 207
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
23-284 1.55e-20

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 93.17  E-value: 1.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   23 ITETIGKGTYGKVFKvlNKKNGQKAAVKIL--DPIHDID---EEIEAEYNILKALSdHPNVVRFYGIYFKKDKvngdkLW 97
Cdd:cd14147     7 LEEVIGIGGFGKVYR--GSWRGELVAVKAArqDPDEDISvtaESVRQEARLFAMLA-HPNIIALKAVCLEEPN-----LC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVTDLVKGflkrgERMSEPLIAYILHEALMGLQHLHNNK---TIHRDVKGNNILLTTEG--------GVKL 166
Cdd:cd14147    79 LVMEYAAGGPLSRALAG-----RRVPPHVLVNWAVQIARGMHYLHCEAlvpVIHRDLKSNNILLLQPIenddmehkTLKI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  167 VDFGVSAQLTSTrhRRNTSVGTPFWMAPEVIACeqqldTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNp 246
Cdd:cd14147   154 TDFGLAREWHKT--TQMSAAGTYAWMAPEVIKA-----STFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVN- 225
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767960106  247 PPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14147   226 KLTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQ 263
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
19-242 1.69e-20

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 95.49  E-value: 1.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEE----IEAEYNILkALSDHPNVVRFYgiYFKKDKVNgd 94
Cdd:cd05628     1 EDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEqvghIRAERDIL-VEADSLWVVKMF--YSFQDKLN-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 kLWLVLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:cd05628    76 -LYLIMEFLPGGDMMTL----LMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 L--------------------------------TSTRHRRN---TSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGIT 219
Cdd:cd05628   151 LkkahrtefyrnlnhslpsdftfqnmnskrkaeTWKRNRRQlafSTVGTPDYIAPEVF-----MQTGYNKLCDWWSLGVI 225
                         250       260
                  ....*....|....*....|...
gi 767960106  220 AIELGDGDPPLADLHPMRALFKI 242
Cdd:cd05628   226 MYEMLIGYPPFCSETPQETYKKV 248
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
27-302 1.77e-20

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 94.56  E-value: 1.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEA----EYNIL--KALSDHPNVVrfyGIYFKKDkvNGDKLWLVL 100
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAhtigERNILvrTALDESPFIV---GLKFSFQ--TPTDLYLVT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCSGGsvtDLVKGFLKRGeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRH 180
Cdd:cd05586    76 DYMSGG---ELFWHLQKEG-RFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  181 RRNTSVGTPFWMAPEVIACEqqldTTYDARCDTWSLGITAIELGDGDPPL--ADLHPMRALFKIPRNPPPKlrqpELWSA 258
Cdd:cd05586   152 TTNTFCGTTEYLAPEVLLDE----KGYTKMVDFWSLGVLVFEMCCGWSPFyaEDTQQMYRNIAFGKVRFPK----DVLSD 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 767960106  259 EFNDFISKCLTKDYEKR----PTVSELLQHKFITQIEGkDVMLQKQLT 302
Cdd:cd05586   224 EGRSFVKGLLNRNPKHRlgahDDAVELKEHPFFADIDW-DLLSKKKIT 270
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
17-302 1.80e-20

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 94.70  E-value: 1.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   17 PSDtWEITETIGKGTYGKVFKVLNKKNGQKAAVKILD--PIHDIDEE--IEAEYNILKALSDHPNVVrfyGIYFKKDKVn 92
Cdd:cd05602     6 PSD-FHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQkkAILKKKEEkhIMSERNVLLKNVKHPFLV---GLHFSFQTT- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   93 gDKLWLVLELCSGGSVTdlvkGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS 172
Cdd:cd05602    81 -DKLYFVLDYINGGELF----YHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLTSTRHRRNTSVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIpRNPPPKLRq 252
Cdd:cd05602   156 KENIEPNGTTSTFCGTPEYLAPEVLHKQ-----PYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNI-LNKPLQLK- 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767960106  253 PELWSAEFNdFISKCLTKDYEKR----PTVSELLQHKFITQIEGKDvMLQKQLT 302
Cdd:cd05602   229 PNITNSARH-LLEGLLQKDRTKRlgakDDFTEIKNHIFFSPINWDD-LINKKIT 280
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
25-287 1.87e-20

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 92.62  E-value: 1.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQKAAVKILD----PIHDIDEEIEAEYNILKALsDHPNVVRFYGIYfkkdKVNGDKLWLVL 100
Cdd:cd14164     6 TTIGEGSFSKVKLATSQKYCCKVAIKIVDrrraSPDFVQKFLPRELSILRRV-NHPNIVQMFECI----EVANGRLYIVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ElcsgGSVTDLVKgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEG-GVKLVDFGVSAQLTSTR 179
Cdd:cd14164    81 E----AAATDLLQ-KIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVEDYP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  180 HRRNTSVGTPFWMAPEVIaceqqLDTTYDA-RCDTWSLGITAIELGDGDPPL-ADLHPMRALFKIPRNPPPKLRQPELWS 257
Cdd:cd14164   156 ELSTTFCGSRAYTPPEVI-----LGTPYDPkKYDVWSLGVVLYVMVTGTMPFdETNVRRLRLQQRGVLYPSGVALEEPCR 230
                         250       260       270
                  ....*....|....*....|....*....|
gi 767960106  258 AefndFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14164   231 A----LIRTLLQFNPSTRPSIQQVAGNSWL 256
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
20-287 2.28e-20

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 92.57  E-value: 2.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   20 TWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHD-----IDEEIEAEYNILKALSdHPNVVRFYGIYFKKDKvngd 94
Cdd:cd14070     3 SYLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAkkdsyVTKNLRREGRIQQMIR-HPNITQLLDILETENS---- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 kLWLVLELCSGGsvtDLVKGFLKRgERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS-- 172
Cdd:cd14070    78 -YYLVMELCPGG---NLMHRIYDK-KRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSnc 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLTSTRHRRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPLA-DLHPMRALFKI----PRNP- 246
Cdd:cd14070   153 AGILGYSDPFSTQCGSPAYAAPELLARKK-----YGPKVDVWSIGVNMYAMLTGTLPFTvEPFSLRALHQKmvdkEMNPl 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767960106  247 PPKLrqpelwSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14070   228 PTDL------SPGAISFLRSLLEPDPLKRPNIKQALANRWL 262
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
17-283 2.32e-20

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 93.70  E-value: 2.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   17 PSDTWEITETIGKGTYGKV-----FKVLNKKNGQKAAVKILDPIHDIDEE--IEAEYNILKALSDHPNVVRFYGIYFKkd 89
Cdd:cd05055    33 PRNNLSFGKTLGAGAFGKVveataYGLSKSDAVMKVAVKMLKPTAHSSEReaLMSELKIMSHLGNHENIVNLLGACTI-- 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   90 kvnGDKLWLVLELCSGGsvtDLVKgFLKRGERM---SEPLIAYILHEAlMGLQHLHNNKTIHRDVKGNNILLTTEGGVKL 166
Cdd:cd05055   111 ---GGPILVITEYCCYG---DLLN-FLRRKRESfltLEDLLSFSYQVA-KGMAFLASKNCIHRDLAARNVLLTHGKIVKI 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  167 VDFGVSAQLtstRHRRNTSV-GTPF----WMAPEVIaceqqLDTTYDARCDTWSLGITAIELGD-GDPPLADLhPMRALF 240
Cdd:cd05055   183 CDFGLARDI---MNDSNYVVkGNARlpvkWMAPESI-----FNCVYTFESDVWSYGILLWEIFSlGSNPYPGM-PVDSKF 253
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 767960106  241 KIPRNPPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd05055   254 YKLIKEGYRMAQPEHAPAEIYDIMKTCWDADPLKRPTFKQIVQ 296
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
21-286 2.60e-20

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 93.17  E-value: 2.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQK----AAVKILDPIHDIDEEIEAEYNILKALS--DHPNVVRFYGIYFKKDKVNGD 94
Cdd:cd07862     3 YECVAEIGEGAYGKVFKARDLKNGGRfvalKRVRVQTGEEGMPLSTIREVAVLRHLEtfEHPNVVRLFDVCTVSRTDRET 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 KLWLVLELCSGGSVTDLvkgflkrgERMSEP-----LIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDF 169
Cdd:cd07862    83 KLTLVFEHVDQDLTTYL--------DKVPEPgvpteTIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  170 GVsAQLTSTRHRRNTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPL---ADLHPMRALFKI---- 242
Cdd:cd07862   155 GL-ARIYSFQMALTSVVVTLWYRAPEVL-----LQSSYATPVDLWSVGCIFAEMFRRKPLFrgsSDVDQLGKILDViglp 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767960106  243 -----------PRNP-PPKLRQP-ELWSAEFND----FISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd07862   229 geedwprdvalPRQAfHSKSAQPiEKFVTDIDElgkdLLLKCLTFNPAKRISAYSALSHPY 289
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
19-287 3.05e-20

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 93.33  E-value: 3.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDpihdIDEEIEA-------EYNILKALsDHPNVVRFYGIY------ 85
Cdd:cd07864     7 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVR----LDNEKEGfpitairEIKILRQL-NHRSVVNLKEIVtdkqda 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   86 --FKKDKVNgdkLWLVLELCSggsvTDLVkGFLKRG-ERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEG 162
Cdd:cd07864    82 ldFKKDKGA---FYLVFEYMD----HDLM-GLLESGlVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  163 GVKLVDFGVsAQLTSTRHRR--NTSVGTPFWMAPEVIACEQQldttYDARCDTWSLGITAIEL------GDGDPPLADLH 234
Cdd:cd07864   154 QIKLADFGL-ARLYNSEESRpyTNKVITLWYRPPELLLGEER----YGPAIDVWSCGCILGELftkkpiFQANQELAQLE 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767960106  235 --------------------PMRALFKIPRNPPPKLRQP-ELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd07864   229 lisrlcgspcpavwpdviklPYFNTMKPKKQYRRRLREEfSFIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
21-287 3.23e-20

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 94.00  E-value: 3.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKAL--SDHP---NVVRFYG-IYFKKdkvngd 94
Cdd:cd14225    45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKKRFHHQALVEVKILDALrrKDRDnshNVIHMKEyFYFRN------ 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 KLWLVLELCsGGSVTDLVKGFLKRGERMSepLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEG--GVKLVDFGVS 172
Cdd:cd14225   119 HLCITFELL-GMNLYELIKKNNFQGFSLS--LIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGqsSIKVIDFGSS 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AqltsTRHRR-NTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDP---------PLA------DLHPM 236
Cdd:cd14225   196 C----YEHQRvYTYIQSRFYRSPEVI-----LGLPYSMAIDMWSLGCILAELYTGYPlfpgeneveQLAcimevlGLPPP 266
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  237 --------RALF----KIPR---NPPPKLRQP---ELWSA------EFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14225   267 elienaqrRRLFfdskGNPRcitNSKGKKRRPnskDLASAlktsdpLFLDFIRRCLEWDPSKRMTPDEALQHEWI 341
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
19-287 4.10e-20

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 91.80  E-value: 4.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITE-TIGKGTYGKVFKVLNKKNGQKAAVKILDpihdIDEEIEAEYNILKALsDHPNVVRFYGIYfkkdKVNGDKLW 97
Cdd:cd14109     3 ELYEIGEeDEKRAAQGAPFHVTERSTGRNFLAQLRY----GDPFLMREVDIHNSL-DHPNIVQMHDAY----DDEKLAVT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGsvtDLVKGFLKRG-ERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGgVKLVDFGVSAQLT 176
Cdd:cd14109    74 VIDNLASTI---ELVRDNLLPGkDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDDK-LKLADFGQSRRLL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 stRHRRNTSV-GTPFWMAPEVIACEQQLDTTydarcDTWSLG-ITAIELGDGDPPLADlHPMRALFKIpRNPPPKLRQPE 254
Cdd:cd14109   150 --RGKLTTLIyGSPEFVSPEIVNSYPVTLAT-----DMWSVGvLTYVLLGGISPFLGD-NDRETLTNV-RSGKWSFDSSP 220
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767960106  255 L--WSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14109   221 LgnISDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
27-304 4.67e-20

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 93.61  E-value: 4.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKIL--DPIHDIDE--EIEAEYNILKAlSDHPNVVRFYGIYFKKDKvngdkLWLVLEL 102
Cdd:cd05593    23 LGKGTFGKVILVREKASGKYYAMKILkkEVIIAKDEvaHTLTESRVLKN-TRHPFLTSLKYSFQTKDR-----LCFVMEY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGSVTdlvkGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRR 182
Cdd:cd05593    97 VNGGELF----FHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATM 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  183 NTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADlHPMRALFKIPRNPPPKLrqPELWSAEFND 262
Cdd:cd05593   173 KTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPFYN-QDHEKLFELILMEDIKF--PRTLSADAKS 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767960106  263 FISKCLTKDYEKR-----PTVSELLQHKFITQIEGKDVMLQKQLTEF 304
Cdd:cd05593   245 LLSGLLIKDPNKRlgggpDDAKEIMRHSFFTGVNWQDVYDKKLVPPF 291
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
27-299 5.38e-20

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 92.12  E-value: 5.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDP--IHDIDEEIEA--EYNILKALS---DHPNVVRFYGIYfkkdkVNGDKLWLV 99
Cdd:cd05606     2 IGRGGFGEVYGCRKADTGKMYAMKCLDKkrIKMKQGETLAlnERIMLSLVStggDCPFIVCMTYAF-----QTPDKLCFI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  100 LELCSGGsvtDLVKGFLKRGErMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLtsTR 179
Cdd:cd05606    77 LDLMNGG---DLHYHLSQHGV-FSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDF--SK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  180 HRRNTSVGTPFWMAPEVIaceqQLDTTYDARCDTWSLGITAIELGDGDPPLADlHPMRALFKIPRNPPPK-LRQPELWSA 258
Cdd:cd05606   151 KKPHASVGTHGYMAPEVL----QKGVAYDSSADWFSLGCMLYKLLKGHSPFRQ-HKTKDKHEIDRMTLTMnVELPDSFSP 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767960106  259 EFNDFISKCLTKDYEKR-----PTVSELLQHKFITQIEGKDVMLQK 299
Cdd:cd05606   226 ELKSLLEGLLQRDVSKRlgclgRGATEVKEHPFFKGVDWQQVYLQK 271
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
15-283 6.09e-20

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 92.10  E-value: 6.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   15 PDPSdtWEIT-------ETIGKGTYGKVFK------VLNKKNGQKAAVKIL-DPIHDID-EEIEAEYNILKALSDHPNVV 79
Cdd:cd05053     3 LDPE--WELPrdrltlgKPLGEGAFGQVVKaeavglDNKPNEVVTVAVKMLkDDATEKDlSDLVSEMEMMKMIGKHKNII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   80 RFYGIYFKKDKvngdkLWLVLELCSGGSVTDLVKGFLKRGERMS----EPLIAYILHEALM--------GLQHLHNNKTI 147
Cdd:cd05053    81 NLLGACTQDGP-----LYVVVEYASKGNLREFLRARRPPGEEASpddpRVPEEQLTQKDLVsfayqvarGMEYLASKKCI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  148 HRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRRNTSVG-TPF-WMAPEVIaceqqLDTTYDARCDTWSLGITAIELGD 225
Cdd:cd05053   156 HRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYRKTTNGrLPVkWMAPEAL-----FDRVYTHQSDVWSFGVLLWEIFT 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767960106  226 -GDPPLADLhPMRALFKIPRNpPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd05053   231 lGGSPYPGI-PVEELFKLLKE-GHRMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQLVE 287
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
25-283 6.29e-20

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 91.15  E-value: 6.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQKAAVK----ILDPihDIDEEIEAEYNILKALsDHPNVVRFYGIYFKKDKVngdklWLVL 100
Cdd:cd05084     2 ERIGRGNFGEVFSGRLRADNTPVAVKscreTLPP--DLKAKFLQEARILKQY-SHPNIVRLIGVCTQKQPI-----YIVM 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCSGGsvtDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ-----L 175
Cdd:cd05084    74 ELVQGG---DFLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREeedgvY 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTRHRRNTSVGtpfWMAPEVIACEQqldttYDARCDTWSLGITAIE-LGDGDPPLADL---HPMRALFKIPRNPPPKLR 251
Cdd:cd05084   151 AATGGMKQIPVK---WTAPEALNYGR-----YSSESDVWSFGILLWEtFSLGAVPYANLsnqQTREAVEQGVRLPCPENC 222
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767960106  252 QPELWSaefndFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd05084   223 PDEVYR-----LMEQCWEYDPRKRPSFSTVHQ 249
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
27-284 6.75e-20

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 91.64  E-value: 6.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKknGQKAAVKIL--DPIHDID---EEIEAEYNILKALSdHPNVVRFYGIYFKKDKvngdkLWLVLE 101
Cdd:cd14146     2 IGVGGFGKVYRATWK--GQEVAVKAArqDPDEDIKataESVRQEAKLFSMLR-HPNIIKLEGVCLEEPN-----LCLVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  102 LCSGGSVTDLVKGF-----LKRGERMSEPLIAYILHEALMGLQHLHNNK---TIHRDVKGNNILLTTE--------GGVK 165
Cdd:cd14146    74 FARGGTLNRALAAAnaapgPRRARRIPPHILVNWAVQIARGMLYLHEEAvvpILHRDLKSSNILLLEKiehddicnKTLK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  166 LVDFGVSAQLTSTRhrRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRN 245
Cdd:cd14146   154 ITDFGLAREWHRTT--KMSAAGTYAWMAPEVIK-----SSLFSKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVAVN 226
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767960106  246 pPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14146   227 -KLTLPIPSTCPEPFAKLMKECWEQDPHIRPSFALILEQ 264
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
16-282 8.07e-20

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 90.78  E-value: 8.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITEtIGKGTYGKVFK--VLNKKngqKAAVKILDPIHDIDEEIEAEYNILKALSdHPNVVRFYGIYFKKDKVng 93
Cdd:cd05112     2 DPSELTFVQE-IGSGQFGLVHLgyWLNKD---KVAIKTIREGAMSEEDFIEEAEVMMKLS-HPKLVQLYGVCLEQAPI-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   94 dklWLVLELCSGGSVTDLVKGflKRGERMSEPLIAYILhEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSA 173
Cdd:cd05112    75 ---CLVFEFMEHGCLSDYLRT--QRGLFSAETLLGMCL-DVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  174 QLTSTRHrrNTSVGTPF---WMAPEVIACEQqldttYDARCDTWSLGITAIEL-GDGDPPLADLHPMRALFKIprNPPPK 249
Cdd:cd05112   149 FVLDDQY--TSSTGTKFpvkWSSPEVFSFSR-----YSSKSDVWSFGVLMWEVfSEGKIPYENRSNSEVVEDI--NAGFR 219
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767960106  250 LRQPELWSAEFNDFISKCLTKDYEKRPTVSELL 282
Cdd:cd05112   220 LYKPRLASTHVYEIMNHCWKERPEDRPSFSLLL 252
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
25-295 8.46e-20

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 92.31  E-value: 8.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQKAAVKILDP-IHDIDEEIE---AEYNILKALSDHPNVVRFYGIYFKKDKvngdkLWLVL 100
Cdd:cd05620     1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKdVVLIDDDVEctmVEKRVLALAWENPFLTHLYCTFQTKEH-----LFFVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCSGGsvtDLVKGFLKRGeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRH 180
Cdd:cd05620    76 EFLNGG---DLMFHIQDKG-RFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGDN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  181 RRNTSVGTPFWMAPEVIaceQQLDTTYDArcDTWSLGITAIELGDGDPPLADlHPMRALFKIPRNPPPklRQPELWSAEF 260
Cdd:cd05620   152 RASTFCGTPDYIAPEIL---QGLKYTFSV--DWWSFGVLLYEMLIGQSPFHG-DDEDELFESIRVDTP--HYPRWITKES 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767960106  261 NDFISKCLTKDYEKR-PTVSELLQHKFI-----TQIEGKDV 295
Cdd:cd05620   224 KDILEKLFERDPTRRlGVVGNIRGHPFFktinwTALEKREL 264
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
21-284 8.82e-20

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 90.98  E-value: 8.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSdHPNVVRfygiyFKKDKVNGDKLWLVL 100
Cdd:cd14662     2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKIDENVQREIINHRSLR-HPNIIR-----FKEVVLTPTHLAIVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCSGGsvtDLVKGFLKRGeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILL--TTEGGVKLVDFGVSAqlTST 178
Cdd:cd14662    76 EYAAGG---ELFERICNAG-RFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLdgSPAPRLKICDFGYSK--SSV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  179 RHRR-NTSVGTPFWMAPEVIACEQqldttYDAR-CDTWSLGITAIELGDGDPPLADLHPMRALFK-IPRNPPPKLRQPEL 255
Cdd:cd14662   150 LHSQpKSTVGTPAYIAPEVLSRKE-----YDGKvADVWSCGVTLYVMLVGAYPFEDPDDPKNFRKtIQRIMSVQYKIPDY 224
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767960106  256 --WSAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14662   225 vrVSQDCRHLLSRIFVANPAKRITIPEIKNH 255
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
27-290 8.93e-20

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 91.48  E-value: 8.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDPIHDID----EEIEAEYNILKALSDHPNVVRFYGIYFKKDkvngdkLWLVLEL 102
Cdd:cd05608     9 LGKGGFGEVSACQMRATGKLYACKKLNKKRLKKrkgyEGAMVEKRILAKVHSRFIVSLAYAFQTKTD------LCLVMTI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRR 182
Cdd:cd05608    83 MNGGDLRYHIYNVDEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQTKT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  183 NTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELgdgdppLADLHPMRALFKIPRNPPPKLR-------QPEL 255
Cdd:cd05608   163 KGYAGTPGFMAPELLLGEE-----YDYSVDYFTLGVTLYEM------IAARGPFRARGEKVENKELKQRilndsvtYSEK 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 767960106  256 WSAEFNDFISKCLTKDYEKR-----PTVSELLQHKFITQI 290
Cdd:cd05608   232 FSPASKSICEALLAKDPEKRlgfrdGNCDGLRTHPFFRDI 271
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
16-305 9.05e-20

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 92.03  E-value: 9.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKIL--DPIHDIDEEIEAEYNILKALSdHPNVVRFYGIYfkkdkVNG 93
Cdd:cd14168     7 DIKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIpkKALKGKESSIENEIAVLRKIK-HENIVALEDIY-----ESP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   94 DKLWLVLELCSGGSVTDLV--KGFlkrgerMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTT---EGGVKLVD 168
Cdd:cd14168    81 NHLYLVMQLVSGGELFDRIveKGF------YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSqdeESKIMISD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  169 FGVSaQLTSTRHRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRaLFKIPRNPPP 248
Cdd:cd14168   155 FGLS-KMEGKGDVMSTACGTPGYVAPEVLA-----QKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSK-LFEQILKADY 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  249 KLRQPeLW---SAEFNDFISKCLTKDYEKRPTVSELLQHKFItqieGKDVMLQKQLTEFI 305
Cdd:cd14168   228 EFDSP-YWddiSDSAKDFIRNLMEKDPNKRYTCEQALRHPWI----AGDTALCKNIHESV 282
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
27-283 9.18e-20

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 90.82  E-value: 9.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKknGQKAAVKI--LDPIHDID---EEIEAEYNILKALSdHPNVVRFYGIYfkkdkVNGDKLWLVLE 101
Cdd:cd14148     2 IGVGGFGKVYKGLWR--GEEVAVKAarQDPDEDIAvtaENVRQEARLFWMLQ-HPNIIALRGVC-----LNPPHLCLVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  102 LCSGGSVTDLVKGflkrgeRMSEP--LIAYILHEAlMGLQHLHNNK---TIHRDVKGNNILLT--------TEGGVKLVD 168
Cdd:cd14148    74 YARGGALNRALAG------KKVPPhvLVNWAVQIA-RGMNYLHNEAivpIIHRDLKSSNILILepienddlSGKTLKITD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  169 FGVSAQLTSTRhrRNTSVGTPFWMAPEVIACeqqldTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNpPP 248
Cdd:cd14148   147 FGLAREWHKTT--KMSAAGTYAWMAPEVIRL-----SLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMN-KL 218
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767960106  249 KLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd14148   219 TLPIPSTCPEPFARLLEECWDPDPHGRPDFGSILK 253
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
27-283 9.64e-20

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 90.53  E-value: 9.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKvlNKKNGQkAAVKIL---DPIHDIDEEIEAEYNILKALSdHPNVVRFYGIyfkkdkVNGDKLWLVLELC 103
Cdd:cd14062     1 IGSGSFGTVYK--GRWHGD-VAVKKLnvtDPTPSQLQAFKNEVAVLRKTR-HVNILLFMGY------MTKPQLAIVTQWC 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  104 SGGSvtdLVKgFLKRGERMSEPL-IAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT--STRH 180
Cdd:cd14062    71 EGSS---LYK-HLHVLETKFEMLqLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATVKTrwSGSQ 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  181 RRNTSVGTPFWMAPEVIacEQQLDTTYDARCDTWSLGITAIELGDGDPPLADLHPM-RALF------------KIPRNPP 247
Cdd:cd14062   147 QFEQPTGSILWMAPEVI--RMQDENPYSFQSDVYAFGIVLYELLTGQLPYSHINNRdQILFmvgrgylrpdlsKVRSDTP 224
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767960106  248 PKLRQpelwsaefndFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd14062   225 KALRR----------LMEDCIKFQRDERPLFPQILA 250
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
27-305 1.11e-19

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 91.05  E-value: 1.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEA----EYNILKALSDHPNVVRFYGIYFKkdkvngDKLWLVLEL 102
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETmalnEKIILEKVSSPFIVSLAYAFETK------DKLCLVLTL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGsvtDLVKGFLKRGER-MSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLtSTRHR 181
Cdd:cd05577    75 MNGG---DLKYHIYNVGTRgFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEF-KGGKK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  182 RNTSVGTPFWMAPEVIaceqQLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPR---NPPPKLrqPELWSA 258
Cdd:cd05577   151 IKGRVGTHGYMAPEVL----QKEVAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRrtlEMAVEY--PDSFSP 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767960106  259 EFNDFISKCLTKDYEKR-----PTVSELLQHKFITQIEGKDVMLQKQLTEFI 305
Cdd:cd05577   225 EARSLCEGLLQKDPERRlgcrgGSADEVKEHPFFRSLNWQRLEAGMLEPPFV 276
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
22-290 1.21e-19

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 93.17  E-value: 1.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKIL--DPIHDIDE--EIEAEYNILkALSDHPNVVRFYgiYFKKDKvngDKLW 97
Cdd:cd05600    14 QILTQVGQGGYGSVFLARKKDTGEICALKIMkkKVLFKLNEvnHVLTERDIL-TTTNSPWLVKLL--YAFQDP---ENVY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVTDLV--KGFLKRGErmseplIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS--- 172
Cdd:cd05600    88 LAMEYVPGGDFRTLLnnSGILSEEH------ARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLAsgt 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 ----------------------------------AQLTSTRHRRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGI 218
Cdd:cd05600   162 lspkkiesmkirleevkntafleltakerrniyrAMRKEDQNYANSVVGSPDYMAPEVLRGEG-----YDLTVDYWSLGC 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  219 TAIELGDGDPPLA---------DLHPMRALFKIPRNPPPKLRQPelWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQ 289
Cdd:cd05600   237 ILFECLVGFPPFSgstpnetwaNLYHWKKTLQRPVYTDPDLEFN--LSDEAWDLITKLITDPQDRLQSPEQIKNHPFFKN 314

                  .
gi 767960106  290 I 290
Cdd:cd05600   315 I 315
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
13-286 1.33e-19

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 91.45  E-value: 1.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   13 NFPDPSDtWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPI--HDIDEEIEaeynILKALSDHPNVVRFYGIYFkkdk 90
Cdd:cd14132    13 EWGSQDD-YEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKPVkkKKIKREIK----ILQNLRGGPNIVKLLDVVK---- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   91 vNGDKLWLVLelcsggsVTDLVKG--FLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLT-TEGGVKLV 167
Cdd:cd14132    84 -DPQSKTPSL-------IFEYVNNtdFKTLYPTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDhEKRKLRLI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  168 DFGVsAQLTSTRHRRNTSVGTPFWMAPEVIACEQQldttYDARCDTWSLGIT------------------------AIEL 223
Cdd:cd14132   156 DWGL-AEFYHPGQEYNVRVASRYYKGPELLVDYQY----YDYSLDMWSLGCMlasmifrkepffhghdnydqlvkiAKVL 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  224 GdGDPPLA---------DLHPMRALFKIPRNPPPKLRQPE---LWSAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd14132   231 G-TDDLYAyldkygielPPRLNDILGRHSKKPWERFVNSEnqhLVTPEALDLLDKLLRYDHQERITAKEAMQHPY 304
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
21-304 1.34e-19

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 92.40  E-value: 1.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDpihdiDEEIEAEYNILKALSDH---PNVVRFYGIYFKKDKVNGDKLW 97
Cdd:cd05594    27 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILK-----KEVIVAKDEVAHTLTENrvlQNSRHPFLTALKYSFQTHDRLC 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVTdlvkGFLKRGERMSEPLIAYILHEALMGLQHLHNNK-TIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:cd05594   102 FVMEYANGGELF----FHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGI 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRHRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPLADlHPMRALFKIPRNppPKLRQPELW 256
Cdd:cd05594   178 KDGATMKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPFYN-QDHEKLFELILM--EEIRFPRTL 249
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767960106  257 SAEFNDFISKCLTKDYEKR-----PTVSELLQHKFITQIEGKDVMLQKQLTEF 304
Cdd:cd05594   250 SPEAKSLLSGLLKKDPKQRlgggpDDAKEIMQHKFFAGIVWQDVYEKKLVPPF 302
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
27-284 1.42e-19

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 90.23  E-value: 1.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKiLDPIHDIDEEIEAEYNILKALSdHPNVVRFYGIYfkkdkVNGDKLWLVLELCSGG 106
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALK-MNTLSSNRANMLREVQLMNRLS-HPNILRFMGVC-----VHQGQLHALTEYINGG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  107 SVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILL-TTEGGVKLV--DFGVSAQL--TSTRHR 181
Cdd:cd14155    74 NLEQL----LDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIkRDENGYTAVvgDFGLAEKIpdYSDGKE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  182 RNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIEL---GDGDPplaDLHPMRALFK---------IPRNPPPK 249
Cdd:cd14155   150 KLAVVGSPYWMAPEVLR-----GEPYNEKADVFSYGIILCEIiarIQADP---DYLPRTEDFGldydafqhmVGDCPPDF 221
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767960106  250 LRqpelwsAEFNdfiskCLTKDYEKRPTVSELLQH 284
Cdd:cd14155   222 LQ------LAFN-----CCNMDPKSRPSFHDIVKT 245
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
18-229 1.48e-19

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 92.05  E-value: 1.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   18 SDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEA----EYNILkALSDHPNVVRFYgIYFKKDKvng 93
Cdd:cd05596    25 AEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAffweERDIM-AHANSEWIVQLH-YAFQDDK--- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   94 dKLWLVLELCSGGSVTDLVKGFlkrgeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSA 173
Cdd:cd05596   100 -YLYMVMDYMPGGDLVNLMSNY-----DVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCM 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767960106  174 QLTSTRH-RRNTSVGTPFWMAPEVIAcEQQLDTTYDARCDTWSLGITAIELGDGDPP 229
Cdd:cd05596   174 KMDKDGLvRSDTAVGTPDYISPEVLK-SQGGDGVYGRECDWWSVGVFLYEMLVGDTP 229
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
27-218 1.57e-19

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 90.09  E-value: 1.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDPIHdIDEE----IEAEYNILKALSdHPNVVRFYGIyfkkdkVNG-DKLWLVLE 101
Cdd:cd14075    10 LGSGNFSQVKLGIHQLTKEKVAIKILDKTK-LDQKtqrlLSREISSMEKLH-HPNIIRLYEV------VETlSKLHLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  102 LCSGGsvtDLVKGFLKRGeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRhR 181
Cdd:cd14075    82 YASGG---ELYTKISTEG-KLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKRGE-T 156
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767960106  182 RNTSVGTPFWMAPEVIAceqqlDTTYDAR-CDTWSLGI 218
Cdd:cd14075   157 LNTFCGSPPYAAPELFK-----DEHYIGIyVDIWALGV 189
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
27-281 1.73e-19

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 90.52  E-value: 1.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFK----VLNKKNGQKAAVKILDP------IHDIDEEIEaeynILKALsDHPNVVRFYGIyfkKDKVNGDKL 96
Cdd:cd05038    12 LGEGHFGSVELcrydPLGDNTGEQVAVKSLQPsgeeqhMSDFKREIE----ILRTL-DHEYIVKYKGV---CESPGRRSL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVtdlvKGFLKR-GERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL 175
Cdd:cd05038    84 RLIMEYLPSGSL----RDYLQRhRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTR--HRRNTSVGTP-FWMAPEVIAceqqlDTTYDARCDTWSLGITAIEL-GDGDPplaDLHPMRALFKIPRN------ 245
Cdd:cd05038   160 PEDKeyYYVKEPGESPiFWYAPECLR-----ESRFSSASDVWSFGVTLYELfTYGDP---SQSPPALFLRMIGIaqgqmi 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 767960106  246 ---------PPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSEL 281
Cdd:cd05038   232 vtrllellkSGERLPRPPSCPDEVYDLMKECWEYEPQDRPSFSDL 276
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
18-288 1.77e-19

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 90.33  E-value: 1.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   18 SDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKIL--DPIHDIDEEIEAEYNILKALSdHPNVVRFYGIYfkkdkVNGDK 95
Cdd:cd14169     2 NSVYELKEKLGEGAFSEVVLAQERGSQRLVALKCIpkKALRGKEAMVENEIAVLRRIN-HENIVSLEDIY-----ESPTH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSGGSVTDLVkgfLKRGErMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTT---EGGVKLVDFGVS 172
Cdd:cd14169    76 LYLAMELVTGGELFDRI---IERGS-YTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATpfeDSKIMISDFGLS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AqlTSTRHRRNTSVGTPFWMAPEVIacEQQldtTYDARCDTWSLGITAIELGDGDPPLADLHPMRaLFKIPRNPPPKLRQ 252
Cdd:cd14169   152 K--IEAQGMLSTACGTPGYVAPELL--EQK---PYGKAVDVWAIGVISYILLCGYPPFYDENDSE-LFNQILKAEYEFDS 223
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767960106  253 PeLW---SAEFNDFISKCLTKDYEKRPTVSELLQHKFIT 288
Cdd:cd14169   224 P-YWddiSESAKDFIRHLLERDPEKRFTCEQALQHPWIS 261
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
22-286 1.82e-19

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 91.47  E-value: 1.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKIldpIHDIDEEIEA---EYNILKALSDHPNVVRFYGI----YFkkdkvngd 94
Cdd:cd14134    15 KILRLLGEGTFGKVLECWDRKRKRYVAVKI---IRNVEKYREAakiEIDVLETLAEKDPNGKSHCVqlrdWF-------- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 kLW-----LVLELCsGGSVTDLVKGFLKRGERMSepLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEG------- 162
Cdd:cd14134    84 -DYrghmcIVFELL-GPSLYDFLKKNNYGPFPLE--HVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDyvkvynp 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  163 ------------GVKLVDFGvSA--------QLTSTRHRRntsvgtpfwmAPEVIaceqqLDTTYDARCDTWSLGITAIE 222
Cdd:cd14134   160 kkkrqirvpkstDIKLIDFG-SAtfddeyhsSIVSTRHYR----------APEVI-----LGLGWSYPCDVWSIGCILVE 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  223 LGDGDP------PLADLHPM-RALFKIP----------------------------------RNPPPKLRQPELWSAE-- 259
Cdd:cd14134   224 LYTGELlfqthdNLEHLAMMeRILGPLPkrmirrakkgakyfyfyhgrldwpegsssgrsikRVCKPLKRLMLLVDPEhr 303
                         330       340
                  ....*....|....*....|....*...
gi 767960106  260 -FNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd14134   304 lLFDLIRKMLEYDPSKRITAKEALKHPF 331
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
25-286 1.93e-19

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 90.62  E-value: 1.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQKAAVKIldpIH-DIDEEIEA----EYNILKALSdHPNVVRFYgiyfkkDKVNG-DKLWL 98
Cdd:cd07836     6 EKLGEGTYATVYKGRNRTTGEIVALKE---IHlDAEEGTPStairEISLMKELK-HENIVRLH------DVIHTeNKLML 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   99 VLELCSGgsvtDLVKGFLKRGERMSEP--LIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:cd07836    76 VFEYMDK----DLKKYMDTHGVRGALDpnTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRHRRNTSVGTPFWMAPEVIACEQqldtTYDARCDTWSLGITAIELGDGDPPLA---DLHPMRALFKI----------- 242
Cdd:cd07836   152 IPVNTFSNEVVTLWYRAPDVLLGSR----TYSTSIDIWSVGCIMAEMITGRPLFPgtnNEDQLLKIFRImgtptestwpg 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767960106  243 -----------PRNPPPKLRQ--PELwSAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd07836   228 isqlpeykptfPRYPPQDLQQlfPHA-DPLGIDLLHRLLQLNPELRISAHDALQHPW 283
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
22-283 2.04e-19

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 90.10  E-value: 2.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKvlNKKNGQkAAVKILDPIHDIDEEIEAEYNILKAL--SDHPNVVRFYGIYFKKDKvngdkLWLV 99
Cdd:cd14063     3 EIKEVIGKGRFGRVHR--GRWHGD-VAIKLLNIDYLNEEQLEAFKEEVAAYknTRHDNLVLFMGACMDPPH-----LAIV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  100 LELCSGGSVTDLVKgflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLttEGG-VKLVDFGVS--AQLT 176
Cdd:cd14063    75 TSLCKGRTLYSLIH---ERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFL--ENGrVVITDFGLFslSGLL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRHRRNTSVGTPFW---MAPEVIA-----CEQQLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPP 248
Cdd:cd14063   150 QPGRREDTLVIPNGWlcyLAPEIIRalspdLDFEESLPFTKASDVYAFGTVWYELLAGRWPFKEQPAESIIWQVGCGKKQ 229
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767960106  249 KLRQPELwSAEFNDFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd14063   230 SLSQLDI-GREVKDILMQCWAYDPEKRPTFSDLLR 263
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
18-287 2.15e-19

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 89.68  E-value: 2.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   18 SDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEE-IEAEYNILKALSdHPNVVRFYGIYFKKDKVngdkl 96
Cdd:cd14191     1 SDFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKEnIRQEISIMNCLH-HPKLVQCVDAFEEKANI----- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLV--KGFlkrgERMSEPLIAYILhEALMGLQHLHNNKTIHRDVKGNNILLTTEGG--VKLVDFGVS 172
Cdd:cd14191    75 VMVLEMVSGGELFERIidEDF----ELTERECIKYMR-QISEGVEYIHKQGIVHLDLKPENIMCVNKTGtkIKLIDFGLA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLTSTRHRRnTSVGTPFWMAPEVIACEQqldTTYDArcDTWSLGITAIELGDGDPPLADLHPMRALFKIprnpppklrQ 252
Cdd:cd14191   150 RRLENAGSLK-VLFGTPEFVAPEVINYEP---IGYAT--DMWSIGVICYILVSGLSPFMGDNDNETLANV---------T 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 767960106  253 PELW----------SAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14191   215 SATWdfddeafdeiSDDAKDFISNLLKKDMKARLTCTQCLQHPWL 259
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
27-230 2.27e-19

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 91.21  E-value: 2.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDP---IHDIDEEIEAEYNILKALSDHPNVVRFYGIYFKkdkvNGDKLWLVLELC 103
Cdd:cd05616     8 LGKGSFGKVMLAERKGTDELYAVKILKKdvvIQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQ----TMDRLYFVMEYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  104 SGGsvtDLVKGFLKRGeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRRN 183
Cdd:cd05616    84 NGG---DLMYHIQQVG-RFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTK 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 767960106  184 TSVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPL 230
Cdd:cd05616   160 TFCGTPDYIAPEIIAYQ-----PYGKSVDWWAFGVLLYEMLAGQAPF 201
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
27-230 2.46e-19

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 91.12  E-value: 2.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKIL--DPIHDiDEEIEA---EYNILKALSDHPNVVRFYGIYfkkdkVNGDKLWLVLE 101
Cdd:cd05590     3 LGKGSFGKVMLARLKESGRLYAVKVLkkDVILQ-DDDVECtmtEKRILSLARNHPFLTQLYCCF-----QTPDRLFFVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  102 LCSGGsvtDLVKgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHR 181
Cdd:cd05590    77 FVNGG---DLMF-HIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKT 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 767960106  182 RNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPL 230
Cdd:cd05590   153 TSTFCGTPDYIAPEILQEML-----YGPSVDWWAMGVLLYEMLCGHAPF 196
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
21-284 2.89e-19

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 89.28  E-value: 2.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDE--------EIEAeYNILKalsdHPNVVRFYGIYFKKDKVn 92
Cdd:cd14162     2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDylqkflprEIEV-IKGLK----HPNLICFYEAIETTSRV- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   93 gdklWLVLELCSGGSVTDLVK--GFLkrgermSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFG 170
Cdd:cd14162    76 ----YIIMELAENGDLLDYIRknGAL------PEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  171 VSAQLTST----RHRRNTSVGTPFWMAPEVIAceqqlDTTYDAR-CDTWSLGITAIELGDGDPPLADLHpMRALFKIPRN 245
Cdd:cd14162   146 FARGVMKTkdgkPKLSETYCGSYAYASPEILR-----GIPYDPFlSDIWSMGVVLYTMVYGRLPFDDSN-LKVLLKQVQR 219
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767960106  246 PPPKLRQPELwSAEFNDFISKCLTKdYEKRPTVSELLQH 284
Cdd:cd14162   220 RVVFPKNPTV-SEECKDLILRMLSP-VKKRITIEEIKRD 256
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
21-286 3.67e-19

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 90.07  E-value: 3.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVK-ILdpIHDIDE--EIEA--EYNILKALSdHPNVVRFYGIYFKKDKVNGDK 95
Cdd:cd07866    10 YEILGKLGEGTFGEVYKARQIKTGRVVALKkIL--MHNEKDgfPITAlrEIKILKKLK-HPNVVPLIDMAVERPDKSKRK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LwLVLELCSGGSVTDLVkGFLKRGE-RMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS-- 172
Cdd:cd07866    87 R-GSVYMVTPYMDHDLS-GLLENPSvKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLArp 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 ---------AQLTSTRHRRNTSVGTPFWMAPEVIACEQQldttYDARCDTWSLGITAIELGDGDPPLA---DLHPMRALF 240
Cdd:cd07866   165 ydgpppnpkGGGGGGTRKYTNLVVTRWYRPPELLLGERR----YTTAVDIWGIGCVFAEMFTRRPILQgksDIDQLHLIF 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  241 KIPRNP-----------------------PPKLRQP-ELWSAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd07866   241 KLCGTPteetwpgwrslpgcegvhsftnyPRTLEERfGKLGPEGLDLLSKLLSLDPYKRLTASDALEHPY 310
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
19-230 4.11e-19

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 91.99  E-value: 4.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDpihdideeieaEYNILKalsdhpnvvRFYGIYFKKDK---VNGDK 95
Cdd:cd05624    72 DDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILN-----------KWEMLK---------RAETACFREERnvlVNGDC 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LW---------------LVLELCSGGSVTDLVKGFlkrGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTT 160
Cdd:cd05624   132 QWittlhyafqdenylyLVMDYYVGGDLLTLLSKF---EDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDM 208
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767960106  161 EGGVKLVDFGVSAQLTSTRH-RRNTSVGTPFWMAPEVIACEQQLDTTYDARCDTWSLGITAIELGDGDPPL 230
Cdd:cd05624   209 NGHIRLADFGSCLKMNDDGTvQSSVAVGTPDYISPEILQAMEDGMGKYGPECDWWSLGVCMYEMLYGETPF 279
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
27-289 6.74e-19

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 89.82  E-value: 6.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDpIHDIDEEIEA----------------EYNILKALSdHPNVVRFYGIYFKKDK 90
Cdd:PTZ00024   17 LGEGTYGKVEKAYDTLTGKIVAIKKVK-IIEISNDVTKdrqlvgmcgihfttlrELKIMNEIK-HENIMGLVDVYVEGDF 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   91 VNgdklwLVLELCSGgsvtDLVKgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFG 170
Cdd:PTZ00024   95 IN-----LVMDIMAS----DLKK-VVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  171 V-------------SAQLTSTRHRRNTS-VGTPFWMAPEVIACEqqldTTYDARCDTWSLGITAIELGDGDPPLADLHPM 236
Cdd:PTZ00024  165 LarrygyppysdtlSKDETMQRREEMTSkVVTLWYRAPELLMGA----EKYHFAVDMWSVGCIFAELLTGKPLFPGENEI 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767960106  237 RALFKI--------PRNPPPKL----------RQPELWSAEFN-------DFISKCLTKDYEKRPTVSELLQHKFITQ 289
Cdd:PTZ00024  241 DQLGRIfellgtpnEDNWPQAKklplyteftpRKPKDLKTIFPnasddaiDLLQSLLKLNPLERISAKEALKHEYFKS 318
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
18-287 8.03e-19

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 88.05  E-value: 8.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   18 SDTWEIT--ETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEA-EYNILKALSdHPNVVRFYGIYFKKDKVngd 94
Cdd:cd14190     1 SSTFSIHskEVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMVLlEIQVMNQLN-HRNLIQLYEAIETPNEI--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 klWLVLELCSGGsvtDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG--VKLVDFGVs 172
Cdd:cd14190    77 --VLFMEYVEGG---ELFERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGhqVKIIDFGL- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLTSTRHRRNTSVGTPFWMAPEVIACEQQLDTTydarcDTWSLGITAIELGDGDPPLADLHPMRALFKI-PRNPPPKLR 251
Cdd:cd14190   151 ARRYNPREKLKVNFGTPEFLSPEVVNYDQVSFPT-----DMWSMGVITYMLLSGLSPFLGDDDTETLNNVlMGNWYFDEE 225
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767960106  252 QPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14190   226 TFEHVSDEAKDFVSNLIIKERSARMSATQCLKHPWL 261
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
27-288 8.45e-19

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 89.74  E-value: 8.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKildPIHDI-DEEIEA-----EYNILKALsDHPNVVRFYGIYFKKDKVNGDKLWLVL 100
Cdd:cd07858    13 IGRGAYGIVCSAKNSETNEKVAIK---KIANAfDNRIDAkrtlrEIKLLRHL-DHENVIAIKDIMPPPHREAFNDVYIVY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCSggsvTDLVKgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVsAQLTSTRH 180
Cdd:cd07858    89 ELMD----TDLHQ-IIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGL-ARTTSEKG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  181 RRNTS-VGTPFWMAPEVIACEqqldTTYDARCDTWSLGITAIELGDGDP--PLAD-LHPMRALFKI---P---------- 243
Cdd:cd07858   163 DFMTEyVVTRWYRAPELLLNC----SEYTTAIDVWSVGCIFAELLGRKPlfPGKDyVHQLKLITELlgsPseedlgfirn 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767960106  244 -------RNPPPKLRQP--ELW---SAEFNDFISKCLTKDYEKRPTVSELLQHKFIT 288
Cdd:cd07858   239 ekarryiRSLPYTPRQSfaRLFphaNPLAIDLLEKMLVFDPSKRITVEEALAHPYLA 295
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
19-299 8.68e-19

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 89.74  E-value: 8.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIH---DIDEEIEAEYNILKAL---SDHPNVVRFYGIYFKKDKvn 92
Cdd:cd05633     5 NDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRikmKQGETLALNERIMLSLvstGDCPFIVCMTYAFHTPDK-- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   93 gdkLWLVLELCSGGsvtDLVKGFLKRGErMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS 172
Cdd:cd05633    83 ---LCFILDLMNGG---DLHYHLSQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLtsTRHRRNTSVGTPFWMAPEVIaceqQLDTTYDARCDTWSLGITAIELGDGDPPLADlHPMRALFKIPR-NPPPKLR 251
Cdd:cd05633   156 CDF--SKKKPHASVGTHGYMAPEVL----QKGTAYDSSADWFSLGCMLFKLLRGHSPFRQ-HKTKDKHEIDRmTLTVNVE 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767960106  252 QPELWSAEFNDFISKCLTKDYEKRPTV-----SELLQHKFITQIEGKDVMLQK 299
Cdd:cd05633   229 LPDSFSPELKSLLEGLLQRDVSKRLGChgrgaQEVKEHSFFKGIDWQQVYLQK 281
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
16-289 8.72e-19

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 89.67  E-value: 8.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPI--HDIDEEIEAEYNILKALsDHPNVVRFYGIYFKKDKVNG 93
Cdd:cd07849     2 DVGPRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISPFehQTYCLRTLREIKILLRF-KHENIIGILDIQRPPTFESF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   94 DKLWLVLELCSggsvTDLVKgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVsA 173
Cdd:cd07849    81 KDVYIVQELME----TDLYK--LIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGL-A 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  174 QLTSTRHrRNTS-----VGTPFWMAPEVIACEQQldttYDARCDTWSLGITAIELGDGDP--PLAD-LHPMRALFKIPRN 245
Cdd:cd07849   154 RIADPEH-DHTGflteyVATRWYRAPEIMLNSKG----YTKAIDIWSVGCILAEMLSNRPlfPGKDyLHQLNLILGILGT 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767960106  246 P--------------------PPKLRQPelWSAEFN-------DFISKCLTKDYEKRPTVSELLQHKFITQ 289
Cdd:cd07849   229 PsqedlnciislkarnyikslPFKPKVP--WNKLFPnadpkalDLLDKMLTFNPHKRITVEEALAHPYLEQ 297
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
27-229 8.85e-19

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 89.37  E-value: 8.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVfkVLNKKNGQKA--AVKILDP---IHDIDEE-IEAEYNILkALSDHPN-VVRFYGIYFKKDKvngdkLWLV 99
Cdd:cd05587     4 LGKGSFGKV--MLAERKGTDElyAIKILKKdviIQDDDVEcTMVEKRVL-ALSGKPPfLTQLHSCFQTMDR-----LYFV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  100 LELCSGGsvtDLVKGFLKRGeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTR 179
Cdd:cd05587    76 MEYVNGG---DLMYHIQQVG-KFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGG 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 767960106  180 HRRNTSVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPP 229
Cdd:cd05587   152 KTTRTFCGTPDYIAPEIIAYQ-----PYGKSVDWWAYGVLLYEMLAGQPP 196
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
21-229 9.62e-19

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 88.23  E-value: 9.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDP----IHDIDEEIEAEYNILkALSDHPNVVRFYGIYFKKDKvngdkL 96
Cdd:cd05609     2 FETIKLISNGAYGAVYLVRHRETRQRFAMKKINKqnliLRNQIQQVFVERDIL-TFAENPFVVSMYCSFETKRH-----L 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLVKGFLKRGERMSEPLIAyilhEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSA--- 173
Cdd:cd05609    76 CMVMEYVEGGDCATLLKNIGPLPVDMARMYFA----ETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKigl 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767960106  174 -QLTS----------TRHRRNTSV-GTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPP 229
Cdd:cd05609   152 mSLTTnlyeghiekdTREFLDKQVcGTPEYIAPEVI-----LRQGYGKPVDWWAMGIILYEFLVGCVP 214
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
21-290 1.05e-18

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 89.63  E-value: 1.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITE------TIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALS--DHPNVVRFYGIyFKKDkVN 92
Cdd:cd07880    11 WEVPDryrdlkQVGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKhmKHENVIGLLDV-FTPD-LS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   93 GDKL---WLVLELCSggsvTDLvkGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDF 169
Cdd:cd07880    89 LDRFhdfYLVMPFMG----TDL--GKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  170 GVSAQLTStrhRRNTSVGTPFWMAPEVIACEQQldttYDARCDTWSLGITAIELGDGDPPLA---DLHPMRALFKIPRNP 246
Cdd:cd07880   163 GLARQTDS---EMTGYVVTRWYRAPEVILNWMH----YTQTVDIWSVGCIMAEMLTGKPLFKghdHLDQLMEIMKVTGTP 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767960106  247 P-------------------PKLRQPELWSAEFN------DFISKCLTKDYEKRPTVSELLQHKFITQI 290
Cdd:cd07880   236 SkefvqklqsedaknyvkklPRFRKKDFRSLLPNanplavNVLEKMLVLDAESRITAAEALAHPYFEEF 304
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
25-284 1.14e-18

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 88.06  E-value: 1.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQKAAVK-ILDPIHDIDEEIEA--EYNILKALSDHPNVVRFYGIYfkkdkVNGDKLWLVLE 101
Cdd:cd14139     6 EKIGVGEFGSVYKCIKRLDGCVYAIKrSMRPFAGSSNEQLAlhEVYAHAVLGHHPHVVRYYSAW-----AEDDHMIIQNE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  102 LCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNIL----LTTEGGV------------- 164
Cdd:cd14139    81 YCNGGSLQDAISENTKSGNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFichkMQSSSGVgeevsneedefls 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  165 -----KLVDFGVSAQLTSTRhrrnTSVGTPFWMAPEVIaceqQLDTTYDARCDTWSLGITaIELGDGDPPL----ADLHP 235
Cdd:cd14139   161 anvvyKIGDLGHVTSINKPQ----VEEGDSRFLANEIL----QEDYRHLPKADIFALGLT-VALAAGAEPLptngAAWHH 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767960106  236 MRAlfkipRNPPPklrQPELWSAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14139   232 IRK-----GNFPD---VPQELPESFSSLLKNMIQPDPEQRPSATALARH 272
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
27-292 1.26e-18

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 87.85  E-value: 1.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAA-VKILDPIHDIDEE--IEAEYNILKALSdHPNVVRFYGIYfkKDKVNGDK-LWLVLEL 102
Cdd:cd14031    18 LGRGAFKTVYKGLDTETWVEVAwCELQDRKLTKAEQqrFKEEAEMLKGLQ-HPNIVRFYDSW--ESVLKGKKcIVLVTEL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGSVtdlvKGFLKRGERMSEPLIAYILHEALMGLQHLHNNK--TIHRDVKGNNILLT-TEGGVKLVDFGVSAQLTSTR 179
Cdd:cd14031    95 MTSGTL----KTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATLMRTSF 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  180 HRrnTSVGTPFWMAPEViaceqqLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALF-KIPRNPPP----KLRQPE 254
Cdd:cd14031   171 AK--SVIGTPEFMAPEM------YEEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYrKVTSGIKPasfnKVTDPE 242
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767960106  255 LwsaefNDFISKCLTKDYEKRPTVSELLQHKFITQIEG 292
Cdd:cd14031   243 V-----KEIIEGCIRQNKSERLSIKDLLNHAFFAEDTG 275
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
71-287 1.26e-18

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 91.23  E-value: 1.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   71 ALSDHPNVVRFYGiYFKKDkvngDKLWLVLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRD 150
Cdd:PTZ00267  120 AACDHFGIVKHFD-DFKSD----DKLLLIMEYGSGGDLNKQIKQRLKEHLPFQEYEVGLLFYQIVLALDEVHSRKMMHRD 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  151 VKGNNILLTTEGGVKLVDFGVSAQLTSTRHRRNTS--VGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIElgdgdp 228
Cdd:PTZ00267  195 LKSANIFLMPTGIIKLGDFGFSKQYSDSVSLDVASsfCGTPYYLAPELWERKR-----YSKKADMWSLGVILYE------ 263
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  229 pLADLH-PmralFKIPRNppPKLRQPELW----------SAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:PTZ00267  264 -LLTLHrP----FKGPSQ--REIMQQVLYgkydpfpcpvSSGMKALLDPLLSKNPALRPTTQQLLHTEFL 326
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
25-286 1.33e-18

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 87.86  E-value: 1.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQKAAVKILDpIHDIDEEIEA----EYNILKALSdHPNVVRFYGIYFKKDKvngdkLWLVL 100
Cdd:cd07861     6 EKIGEGTYGVVYKGRNKKTGQIVAMKKIR-LESEEEGVPStairEISLLKELQ-HPNIVCLEDVLMQENR-----LYLVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCSggsvTDLVKGF--LKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST 178
Cdd:cd07861    79 EFLS----MDLKKYLdsLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFGIP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  179 RHRRNTSVGTPFWMAPEVIACEQQldttYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPR-------------- 244
Cdd:cd07861   155 VRVYTHEVVTLWYRAPEVLLGSPR----YSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRilgtptediwpgvt 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767960106  245 ------NPPPKLRQPELWSAEFN------DFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd07861   231 slpdykNTFPKWKKGSLRTAVKNldedglDLLEKMLIYDPAKRISAKKALVHPY 284
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
25-284 1.75e-18

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 87.39  E-value: 1.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQKAAVK-ILDPIH-DIDEEieaeyNILK------ALSDHPNVVRFYGIYfkkdkVNGDKL 96
Cdd:cd14138    11 EKIGSGEFGSVFKCVKRLDGCIYAIKrSKKPLAgSVDEQ-----NALRevyahaVLGQHSHVVRYYSAW-----AEDDHM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLT---------------TE 161
Cdd:cd14138    81 LIQNEYCNGGSLADAISENYRIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISrtsipnaaseegdedEW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  162 GGVKLV----DFGVSAQLTSTRhrrnTSVGTPFWMAPEVIaceqQLDTTYDARCDTWSLGITAIELGDGDPpladlhpmr 237
Cdd:cd14138   161 ASNKVIfkigDLGHVTRVSSPQ----VEEGDSRFLANEVL----QENYTHLPKADIFALALTVVCAAGAEP--------- 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  238 alfkIPRNPPP--KLRQ------PELWSAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14138   224 ----LPTNGDQwhEIRQgklpriPQVLSQEFLDLLKVMIHPDPERRPSAVALVKH 274
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
21-301 2.02e-18

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 88.94  E-value: 2.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKIL--DPIHDiDEEI---EAEYNILKALSDHPNVVRFYGIYFKKDKvngdk 95
Cdd:cd05618    22 FDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVkkELVND-DEDIdwvQTEKHVFEQASNHPFLVGLHSCFQTESR----- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSGGsvtDLVKgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL 175
Cdd:cd05618    96 LFFVIEYVNGG---DLMF-HMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEG 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTRHRRNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPL--------ADLHPMRALFKIPRNpp 247
Cdd:cd05618   172 LRPGDTTSTFCGTPNYIAPEILRGED-----YGFSVDWWALGVLMFEMMAGRSPFdivgssdnPDQNTEDYLFQVILE-- 244
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  248 PKLRQPELWSAEFNDFISKCLTKDYEKR------PTVSELLQHKFITQIEGkDVMLQKQL 301
Cdd:cd05618   245 KQIRIPRSLSVKAASVLKSFLNKDPKERlgchpqTGFADIQGHPFFRNVDW-DLMEQKQV 303
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
19-230 2.53e-18

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 89.30  E-value: 2.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVfKVLNKKNGQKA-AVKILDpihdideeieaEYNILKalsdhpnvvRFYGIYFKKDK---VNGD 94
Cdd:cd05623    72 EDFEILKVIGRGAFGEV-AVVKLKNADKVfAMKILN-----------KWEMLK---------RAETACFREERdvlVNGD 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 KLW---------------LVLELCSGGSVTDLVKGFlkrGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLT 159
Cdd:cd05623   131 SQWittlhyafqddnnlyLVMDYYVGGDLLTLLSKF---EDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMD 207
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767960106  160 TEGGVKLVDFGVSAQLTSTRH-RRNTSVGTPFWMAPEVIACEQQLDTTYDARCDTWSLGITAIELGDGDPPL 230
Cdd:cd05623   208 MNGHIRLADFGSCLKLMEDGTvQSSVAVGTPDYISPEILQAMEDGKGKYGPECDWWSLGVCMYEMLYGETPF 279
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
21-294 2.93e-18

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 88.17  E-value: 2.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITET------IGKGTYGKVFKVLNKKNGQKAAVKILD-PIHDI--DEEIEAEYNILKALSdHPNVVRFYGIYFKKDKV 91
Cdd:cd07877    13 WEVPERyqnlspVGSGAYGSVCAAFDTKTGLRVAVKKLSrPFQSIihAKRTYRELRLLKHMK-HENVIGLLDVFTPARSL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   92 NG-DKLWLVLELCsGGSVTDLVKGflkrgERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFG 170
Cdd:cd07877    92 EEfNDVYLVTHLM-GADLNNIVKC-----QKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  171 VSAQltsTRHRRNTSVGTPFWMAPEVIACEQQldttYDARCDTWSLGITAIELGDGD---PPLADLHPMRALFKIPRNPP 247
Cdd:cd07877   166 LARH---TDDEMTGYVATRWYRAPEIMLNWMH----YNQTVDIWSVGCIMAELLTGRtlfPGTDHIDQLKLILRLVGTPG 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767960106  248 PKLRQ--------------PELWSAEFN-----------DFISKCLTKDYEKRPTVSELLQHKFITQIEGKD 294
Cdd:cd07877   239 AELLKkissesarnyiqslTQMPKMNFAnvfiganplavDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPD 310
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
17-293 3.25e-18

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 86.63  E-value: 3.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   17 PSDTWEITETIGKGTYGKVFKVLnKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSdHPNVVRFYGIYFKKDKVngdkl 96
Cdd:cd05072     5 PRESIKLVKKLGAGQFGEVWMGY-YNNSTKVAVKTLKPGTMSVQAFLEEANLMKTLQ-HDKLVRLYAVVTKEEPI----- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDLVKGflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:cd05072    78 YIITEYMAKGSLLDFLKS--DEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRHRRNTSVGTPF-WMAPEVIACeqqldTTYDARCDTWSLGITAIELGDGD----PPLADLHPMRAL---FKIPRnppp 248
Cdd:cd05072   156 DNEYTAREGAKFPIkWTAPEAINF-----GSFTIKSDVWSFGILLYEIVTYGkipyPGMSNSDVMSALqrgYRMPR---- 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767960106  249 klrqPELWSAEFNDFISKCLTKDYEKRPTVSEL--LQHKFITQIEGK 293
Cdd:cd05072   227 ----MENCPDELYDIMKTCWKEKAEERPTFDYLqsVLDDFYTATEGQ 269
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
25-283 3.50e-18

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 86.25  E-value: 3.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKknGQKAAVKILDPIHDIDEEIEAEYNILKALSdHPNVVRFYGIYFKkdkvnGDKLWLVLELCS 104
Cdd:cd05039    12 ELIGKGEFGDVMLGDYR--GQKVAVKCLKDDSTAAQAFLAEASVMTTLR-HPNLVQLLGVVLE-----GNGLYIVTEYMA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  105 GGSVTDLVKgflKRGERM--SEPLIAYILHEAlMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTStrhrr 182
Cdd:cd05039    84 KGSLVDYLR---SRGRAVitRKDQLGFALDVC-EGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEASS----- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  183 NTSVGT-PF-WMAPEVIACEQqldttYDARCDTWSLGITAIElgdgdppladlhpmraLFKIPRNPPPKLRQ-------- 252
Cdd:cd05039   155 NQDGGKlPIkWTAPEALREKK-----FSTKSDVWSFGILLWE----------------IYSFGRVPYPRIPLkdvvphve 213
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767960106  253 -------PELWSAEFNDFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd05039   214 kgyrmeaPEGCPPEVYKVMKNCWELDPAKRPTFKQLRE 251
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
11-290 3.53e-18

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 91.34  E-value: 3.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   11 FDNFPDPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDpIHDIDE----EIEAEYNILKALSdHPNVVRFYGIYF 86
Cdd:PTZ00266    5 YDDGESRLNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAIS-YRGLKEreksQLVIEVNVMRELK-HKNIVRYIDRFL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   87 KKDKvngDKLWLVLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHN-------NKTIHRDVKGNNILLT 159
Cdd:PTZ00266   83 NKAN---QKLYILMEFCDAGDLSRNIQKCYKMFGKIEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  160 TegGV-------------------KLVDFGVSAQLtSTRHRRNTSVGTPFWMAPEVIACEQQldtTYDARCDTWSLGITA 220
Cdd:PTZ00266  160 T--GIrhigkitaqannlngrpiaKIGDFGLSKNI-GIESMAHSCVGTPYYWSPELLLHETK---SYDDKSDMWALGCII 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767960106  221 IELGDGDPPLADLHPMRALF-KIPRNPPPKLRQPelwSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQI 290
Cdd:PTZ00266  234 YELCSGKTPFHKANNFSQLIsELKRGPDLPIKGK---SKELNILIKNLLNLSAKERPSALQCLGYQIIKNV 301
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
25-281 3.74e-18

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 85.83  E-value: 3.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKkngQKAAVKILDPIHDIDEEIE----AEYNILKALsDHPNVVRFYGIYFKKDKVngdklWLVL 100
Cdd:cd05085     2 ELLGKGNFGEVYKGTLK---DKTPVAVKTCKEDLPQELKikflSEARILKQY-DHPNIVKLIGVCTQRQPI-----YIVM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCSGGSVTDLVKGflKRGERMSEPLIAYILhEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRH 180
Cdd:cd05085    73 ELVPGGDFLSFLRK--KKDELKTKQLVKFSL-DAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDDGVY 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  181 RRNTSVGTPF-WMAPEVIACEQqldttYDARCDTWSLGITAIE-LGDGDPPLADLHPMRALFKIPRNppPKLRQPELWSA 258
Cdd:cd05085   150 SSSGLKQIPIkWTAPEALNYGR-----YSSESDVWSFGILLWEtFSLGVCPYPGMTNQQAREQVEKG--YRMSAPQRCPE 222
                         250       260
                  ....*....|....*....|...
gi 767960106  259 EFNDFISKCLTKDYEKRPTVSEL 281
Cdd:cd05085   223 DIYKIMQRCWDYNPENRPKFSEL 245
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
27-282 4.22e-18

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 85.97  E-value: 4.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVK---ILDPIHDIDEEIEAEYNILKALSdHPNVVRFYGIYFKKDKVNgdklwLVLELC 103
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKclhSSPNCIEERKALLKEAEKMERAR-HSYVLPLLGVCVERRSLG-----LVMEYM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  104 SGGSVTDLVKgflKRGERMSEPLIAYILHEALMGLQHLHNNK--TIHRDVKGNNILLTTEGGVKLVDFGVSA--QLTSTR 179
Cdd:cd13978    75 ENGSLKSLLE---REIQDVPWSLRFRIIHEIALGMNFLHNMDppLLHHDLKPENILLDNHFHVKISDFGLSKlgMKSISA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  180 HRRNTS---VGTPFWMAPEviaceqQLDTTY---DARCDTWSLGITAIELGDGDPPLAD-LHPMRALFKI-----PRNPP 247
Cdd:cd13978   152 NRRRGTenlGGTPIYMAPE------AFDDFNkkpTSKSDVYSFAIVIWAVLTRKEPFENaINPLLIMQIVskgdrPSLDD 225
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767960106  248 PKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELL 282
Cdd:cd13978   226 IGRLKQIENVQELISLMIRCWDGNPDARPTFLECL 260
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
27-230 4.80e-18

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 87.36  E-value: 4.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDP---IHDIDEEIE-AEYNILKALSDHPNVVRFYGIYfkkdkVNGDKLWLVLEL 102
Cdd:cd05615    18 LGKGSFGKVMLAERKGSDELYAIKILKKdvvIQDDDVECTmVEKRVLALQDKPPFLTQLHSCF-----QTVDRLYFVMEY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGsvtDLVKGFLKRGeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRR 182
Cdd:cd05615    93 VNGG---DLMYHIQQVG-KFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVEGVTT 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 767960106  183 NTSVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPL 230
Cdd:cd05615   169 RTFCGTPDYIAPEIIAYQ-----PYGRSVDWWAYGVLLYEMLAGQPPF 211
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
17-284 5.30e-18

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 86.39  E-value: 5.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   17 PSDTWEITETIGKGTYGKV-----FKVLNKKNGQKAAVKIL--DPIHDIDEEIEAEYNILKALSDHPNVVRFYGIYFKKd 89
Cdd:cd05054     5 PRDRLKLGKPLGRGAFGKViqasaFGIDKSATCRTVAVKMLkeGATASEHKALMTELKILIHIGHHLNVVNLLGACTKP- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   90 kvnGDKLWLVLELCSGGSVTDLVKGflKR--------------------GERMSEP-----LIAYILHEAlMGLQHLHNN 144
Cdd:cd05054    84 ---GGPLMVIVEFCKFGNLSNYLRS--KReefvpyrdkgardveeeeddDELYKEPltledLICYSFQVA-RGMEFLASR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  145 KTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST-RHRRNTSVGTPF-WMAPEVIaceqqLDTTYDARCDTWSLGITAIE 222
Cdd:cd05054   158 KCIHRDLAARNILLSENNVVKICDFGLARDIYKDpDYVRKGDARLPLkWMAPESI-----FDKVYTTQSDVWSFGVLLWE 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767960106  223 LGD-GDPPLADLHpMRALFKIPRNPPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd05054   233 IFSlGASPYPGVQ-MDEEFCRRLKEGTRMRAPEYTTPEIYQIMLDCWHGEPKERPTFSELVEK 294
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
27-281 6.23e-18

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 86.46  E-value: 6.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDpiHDIDEEIEAEYNILKALSDHPNVVRFYGIYfkKDKVNGdklWLVLELCSGG 106
Cdd:cd14180    14 LGEGSFSVCRKCRHRQSGQEYAVKIIS--RRMEANTQREVAALRLCQSHPNIVALHEVL--HDQYHT---YLVMELLRGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  107 SVTDLVKgflkRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG---VKLVDFGVSAQLTSTRHRRN 183
Cdd:cd14180    87 ELLDRIK----KKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFARLRPQGSRPLQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  184 TSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPL-------ADLHPMRALFKIPRNPPPklRQPELW 256
Cdd:cd14180   163 TPCFTLQYAAPELFS-----NQGYDESCDLWSLGVILYTMLSGQVPFqskrgkmFHNHAADIMHKIKEGDFS--LEGEAW 235
                         250       260
                  ....*....|....*....|....*...
gi 767960106  257 ---SAEFNDFISKCLTKDYEKRPTVSEL 281
Cdd:cd14180   236 kgvSEEAKDLVRGLLTVDPAKRLKLSEL 263
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
27-280 6.27e-18

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 85.79  E-value: 6.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFK-VLNkkNGQKAAVKILDP--IHDIDEEIEAEYNILKALSdHPNVVRFYGIYFKKDkvngDKLwLVLELC 103
Cdd:cd14066     1 IGSGGFGTVYKgVLE--NGTVVAVKRLNEmnCAASKKEFLTELEMLGRLR-HPNLVRLLGYCLESD----EKL-LVYEYM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  104 SGGSVTDLVKGFLKRG-----ERMSepliayILHEALMGLQHLHN---NKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL 175
Cdd:cd14066    73 PNGSLEDRLHCHKGSPplpwpQRLK------IAKGIARGLEYLHEecpPPIIHGDIKSSNILLDEDFEPKLTDFGLARLI 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTR--HRRNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPlADLHPMRALFKiprnpppKLRQ- 252
Cdd:cd14066   147 PPSEsvSKTSAVKGTIGYLAPEYIR-----TGRVSTKSDVYSFGVVLLELLTGKPA-VDENRENASRK-------DLVEw 213
                         250       260
                  ....*....|....*....|....*....
gi 767960106  253 -PELWSAEFNDFISKCLTKDYEKRPTVSE 280
Cdd:cd14066   214 vESKGKEELEDILDKRLVDDDGVEEEEVE 242
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
25-287 7.16e-18

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 85.40  E-value: 7.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDID-EEIEAEYNILKALSdHPNVVRFYGIYFKKDKVNgdklwLVLELC 103
Cdd:cd14192    10 EVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKErEEVKNEINIMNQLN-HVNLIQLYDAFESKTNLT-----LIMEYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  104 SGGSVTDLVkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG--VKLVDFGVsAQLTSTRHR 181
Cdd:cd14192    84 DGGELFDRI---TDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTGnqIKIIDFGL-ARRYKPREK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  182 RNTSVGTPFWMAPEVIaceqqldtTYD---ARCDTWSLG-ITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQPELWS 257
Cdd:cd14192   160 LKVNFGTPEFLAPEVV--------NYDfvsFPTDMWSVGvITYMLLSGLSPFLGETDAETMNNIVNCKWDFDAEAFENLS 231
                         250       260       270
                  ....*....|....*....|....*....|
gi 767960106  258 AEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14192   232 EEAKDFISRLLVKEKSCRMSATQCLKHEWL 261
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
27-289 7.19e-18

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 87.08  E-value: 7.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILD-PIHDIDEEIEA--EYNILKaLSDHPNVVRFYGIyFKKDKVNGD--KLWLVLE 101
Cdd:cd07850     8 IGSGAQGIVCAAYDTVTGQNVAIKKLSrPFQNVTHAKRAyrELVLMK-LVNHKNIIGLLNV-FTPQKSLEEfqDVYLVME 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  102 LCSGgSVTDLVKGFLKRgERMSepliaYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVsAQLTSTRHR 181
Cdd:cd07850    86 LMDA-NLCQVIQMDLDH-ERMS-----YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGL-ARTAGTSFM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  182 RNTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIEL--------GD-------------GDPP---LADLHPMR 237
Cdd:cd07850   158 MTPYVVTRYYRAPEVI-----LGMGYKENVDIWSVGCIMGEMirgtvlfpGTdhidqwnkiieqlGTPSdefMSRLQPTV 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767960106  238 A----------------LFKIPRNPPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQ 289
Cdd:cd07850   233 RnyvenrpkyagysfeeLFPDVLFPPDSEEHNKLKASQARDLLSKMLVIDPEKRISVDDALQHPYINV 300
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
19-289 7.87e-18

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 86.96  E-value: 7.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILD-PIHDideEIEA-----EYNILKALsDHPNVVRFYGIYFKKDKVN 92
Cdd:cd07851    15 DRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSrPFQS---AIHAkrtyrELRLLKHM-KHENVIGLLDVFTPASSLE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   93 G-DKLWLVLELCSggsvTDLVKgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGV 171
Cdd:cd07851    91 DfQDVYLVTHLMG----ADLNN--IVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  172 SAQltsTRHRRNTSVGTPFWMAPEVIACEQQldttYDARCDTWSLGITAIELGDGDP--PLAD-LHPMRALFKIPRNPPP 248
Cdd:cd07851   165 ARH---TDDEMTGYVATRWYRAPEIMLNWMH----YNQTVDIWSVGCIMAELLTGKTlfPGSDhIDQLKRIMNLVGTPDE 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767960106  249 KLRQ--------------PELWSAEFN-----------DFISKCLTKDYEKRPTVSELLQHKFITQ 289
Cdd:cd07851   238 ELLKkissesarnyiqslPQMPKKDFKevfsganplaiDLLEKMLVLDPDKRITAAEALAHPYLAE 303
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
20-287 8.37e-18

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 84.97  E-value: 8.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   20 TWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPI-HDIDEEIEAEYNILKALsDHPNVVRFYGIYFKKDKVngdklWL 98
Cdd:cd14193     5 NVNKEEILGGGRFGQVHKCEEKSSGLKLAAKIIKARsQKEKEEVKNEIEVMNQL-NHANLIQLYDAFESRNDI-----VL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   99 VLELCSGGSVTDLVkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG--VKLVDFGVsAQLT 176
Cdd:cd14193    79 VMEYVDGGELFDRI---IDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREAnqVKIIDFGL-ARRY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRHRRNTSVGTPFWMAPEVIACEQQLDTTydarcDTWSLGITAIELGDGDPPLADLHPMRALFKI-PRNPPPKLRQPEL 255
Cdd:cd14193   155 KPREKLRVNFGTPEFLAPEVVNYEFVSFPT-----DMWSLGVIAYMLLSGLSPFLGEDDNETLNNIlACQWDFEDEEFAD 229
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767960106  256 WSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14193   230 ISEEAKDFISKLLIKEKSWRMSASEALKHPWL 261
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
27-291 8.60e-18

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 87.21  E-value: 8.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKIL--DPIHDIDE--EIEAEYNILkALSDHPNVVRFYgiYFKKDkvnGDKLWLVLEL 102
Cdd:cd05629     9 IGKGAFGEVRLVQKKDTGKIYAMKTLlkSEMFKKDQlaHVKAERDVL-AESDSPWVVSLY--YSFQD---AQYLYLIMEF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGsvtDLVKgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL------- 175
Cdd:cd05629    83 LPGG---DLMT-MLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLSTGFhkqhdsa 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 -----------TSTRHRRNT-----------------------------SVGTPFWMAPEVIaceqqLDTTYDARCDTWS 215
Cdd:cd05629   159 yyqkllqgksnKNRIDNRNSvavdsinltmsskdqiatwkknrrlmaysTVGTPDYIAPEIF-----LQQGYGQECDWWS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  216 LGITAIELGDGDPPLADLHPMRALFKIpRNPPPKLRQPE--LWSAEFNDFISKCLTKDYEK--RPTVSELLQHKFITQIE 291
Cdd:cd05629   234 LGAIMFECLIGWPPFCSENSHETYRKI-INWRETLYFPDdiHLSVEAEDLIRRLITNAENRlgRGGAHEIKSHPFFRGVD 312
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
21-223 8.74e-18

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 85.70  E-value: 8.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVK-ILDPIHDID-EEIEAEYNILKALsDHPNVVRFYGIYFK------KDKVN 92
Cdd:cd14048     8 FEPIQCLGRGGFGVVFEAKNKVDDCNYAVKrIRLPNNELArEKVLREVRALAKL-DHPGIVRYFNAWLErppegwQEKMD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   93 GDKLWLVLELCSGGSVTDlvkgFLKRGERMSEPLIAYILH---EALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDF 169
Cdd:cd14048    87 EVYLYIQMQLCRKENLKD----WMNRRCTMESRELFVCLNifkQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDF 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767960106  170 GVSAQL--------------TSTRHRRNtsVGTPFWMAPeviacEQQLDTTYDARCDTWSLGITAIEL 223
Cdd:cd14048   163 GLVTAMdqgepeqtvltpmpAYAKHTGQ--VGTRLYMSP-----EQIHGNQYSEKVDIFALGLILFEL 223
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
17-287 8.91e-18

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 84.87  E-value: 8.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   17 PSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSdHPNVVRFYGIYfkkdkVNGDKL 96
Cdd:cd14111     1 PQKPYTFLDEKARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQGVLQEYEILKSLH-HERIMALHEAY-----ITPRYL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGgsvTDLVKGFLKRGeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGvSAQ-- 174
Cdd:cd14111    75 VLIAEFCSG---KELLHSLIDRF-RYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFG-SAQsf 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 ----LTSTRHRrntsVGTPFWMAPEVIACEqqldtTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKI--PRNPPP 248
Cdd:cd14111   150 nplsLRQLGRR----TGTLEYMAPEMVKGE-----PVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKIlvAKFDAF 220
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767960106  249 KLRQPELWSAEFndFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14111   221 KLYPNVSQSASL--FLKKVLSSYPWSRPTTKDCFAHAWL 257
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
27-292 9.02e-18

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 85.13  E-value: 9.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAA-VKILD-PIHDIDEE-IEAEYNILKALSdHPNVVRFYGiyFKKDKVNGDK-LWLVLEL 102
Cdd:cd14032     9 LGRGSFKTVYKGLDTETWVEVAwCELQDrKLTKVERQrFKEEAEMLKGLQ-HPNIVRFYD--FWESCAKGKRcIVLVTEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGSVtdlvKGFLKRGERMSEPLIAYILHEALMGLQHLHNNK--TIHRDVKGNNILLT-TEGGVKLVDFGVSAQLTSTR 179
Cdd:cd14032    86 MTSGTL----KTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATLKRASF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  180 HRrnTSVGTPFWMAPEViaceqqLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFK-----IPRNPPPKLRQPE 254
Cdd:cd14032   162 AK--SVIGTPEFMAPEM------YEEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRkvtcgIKPASFEKVTDPE 233
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767960106  255 LwsaefNDFISKCLTKDYEKRPTVSELLQHKFITQIEG 292
Cdd:cd14032   234 I-----KEIIGECICKNKEERYEIKDLLSHAFFAEDTG 266
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
22-281 1.47e-17

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 84.77  E-value: 1.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFK-----------------VLNKKNGQKAAVKILDpihdideeiEAeynILKALSDHPNVVRFYGI 84
Cdd:cd05057    10 EKGKVLGSGAFGTVYKgvwipegekvkipvaikVLREETGPKANEEILD---------EA---YVMASVDHPHLVRLLGI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   85 YFkkdkvnGDKLWLVLELCSGGSVTDLVKGflKRGERMSEPLIAYILHEAlMGLQHLHNNKTIHRDVKGNNILLTTEGGV 164
Cdd:cd05057    78 CL------SSQVQLITQLMPLGCLLDYVRN--HRDNIGSQLLLNWCVQIA-KGMSYLEEKRLVHRDLAARNVLVKTPNHV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  165 KLVDFGVSAQLTSTRHRRNTSVG-TPF-WMAPEVIaceqqLDTTYDARCDTWSLGITAIELGD-GDPPLADLhPMRALFK 241
Cdd:cd05057   149 KITDFGLAKLLDVDEKEYHAEGGkVPIkWMALESI-----QYRIYTHKSDVWSYGVTVWELMTfGAKPYEGI-PAVEIPD 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 767960106  242 IPRNpPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSEL 281
Cdd:cd05057   223 LLEK-GERLPQPPICTIDVYMVLVKCWMIDAESRPTFKEL 261
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
19-282 1.49e-17

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 84.73  E-value: 1.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITE-------TIGKGTYGKVFKvlNKKNGQkAAVKILDPIHDIDEEIEAEYNILKAL--SDHPNVVRFYGIYFKKd 89
Cdd:cd14151     1 DDWEIPDgqitvgqRIGSGSFGTVYK--GKWHGD-VAVKMLNVTAPTPQQLQAFKNEVGVLrkTRHVNILLFMGYSTKP- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   90 kvngdKLWLVLELCSGGSVTDLVKGFLKRGERMSeplIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDF 169
Cdd:cd14151    77 -----QLAIVTQWCEGSSLYHHLHIIETKFEMIK---LIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  170 GVSAQLT--STRHRRNTSVGTPFWMAPEVIacEQQLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRA--------- 238
Cdd:cd14151   149 GLATVKSrwSGSHQFEQLSGSILWMAPEVI--RMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQiifmvgrgy 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 767960106  239 ----LFKIPRNPPPKLRQpelwsaefndFISKCLTKDYEKRPTVSELL 282
Cdd:cd14151   227 lspdLSKVRSNCPKAMKR----------LMAECLKKKRDERPLFPQIL 264
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
25-217 1.60e-17

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 85.02  E-value: 1.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFkvLNKKNGQKAAVKILdpiHDIDEEI---EAE-YNILkaLSDHPNVVRFYGiyfkKDKVNGD---KLW 97
Cdd:cd14056     1 KTIGKGRYGEVW--LGKYRGEKVAVKIF---SSRDEDSwfrETEiYQTV--MLRHENILGFIA----ADIKSTGswtQLW 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVTDlvkgFLKRGErMSEPLIAYILHEALMGLQHLHN------NK--TIHRDVKGNNILLTTEGGVKLVDF 169
Cdd:cd14056    70 LITEYHEHGSLYD----YLQRNT-LDTEEALRLAYSAASGLAHLHTeivgtqGKpaIAHRDLKSKNILVKRDGTCCIADL 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  170 GV----SAQLTSTRHRRNTSVGTPFWMAPEVIacEQQLDTT-YDA--RCDTWSLG 217
Cdd:cd14056   145 GLavryDSDTNTIDIPPNPRVGTKRYMAPEVL--DDSINPKsFESfkMADIYSFG 197
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
25-291 1.63e-17

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 86.60  E-value: 1.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDE----EIEAEYNILkALSDHPNVVRFYgiYFKKDKvngDKLWLVL 100
Cdd:cd05626     7 KTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRnqvaHVKAERDIL-AEADNEWVVKLY--YSFQDK---DNLYFVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSA------- 173
Cdd:cd05626    81 DYIPGGDMMSL----LIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTgfrwthn 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  174 -------------------------------------QLTSTRHRR---NTSVGTPFWMAPEVIaceqqLDTTYDARCDT 213
Cdd:cd05626   157 skyyqkgshirqdsmepsdlwddvsncrcgdrlktleQRATKQHQRclaHSLVGTPNYIAPEVL-----LRKGYTQLCDW 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  214 WSLGITAIELGDGDPPLADLHPMRALFKI-----PRNPPPKLRqpelWSAEFNDFISK--CLTKDYEKRPTVSELLQHKF 286
Cdd:cd05626   232 WSVGVILFEMLVGQPPFLAPTPTETQLKVinwenTLHIPPQVK----LSPEAVDLITKlcCSAEERLGRNGADDIKAHPF 307

                  ....*
gi 767960106  287 ITQIE 291
Cdd:cd05626   308 FSEVD 312
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
17-283 1.73e-17

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 85.40  E-value: 1.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   17 PSDTWEITETIGKGTYGKVFKV----LNKKNGQKA---AVKIL-DPIHDID-EEIEAEYNILKALSDHPNVVRFYGIYFK 87
Cdd:cd05099    10 PRDRLVLGKPLGEGCFGQVVRAeaygIDKSRPDQTvtvAVKMLkDNATDKDlADLISEMELMKLIGKHKNIINLLGVCTQ 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   88 KDKvngdkLWLVLELCSGGSVTDLVKG-------FLKRGERMSEPLIAY-----ILHEALMGLQHLHNNKTIHRDVKGNN 155
Cdd:cd05099    90 EGP-----LYVIVEYAAKGNLREFLRArrppgpdYTFDITKVPEEQLSFkdlvsCAYQVARGMEYLESRRCIHRDLAARN 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  156 ILLTTEGGVKLVDFGVSAQLTSTRHRRNTSVG-TPF-WMAPEVIaceqqLDTTYDARCDTWSLGITAIELGD-GDPPLAD 232
Cdd:cd05099   165 VLVTEDNVMKIADFGLARGVHDIDYYKKTSNGrLPVkWMAPEAL-----FDRVYTHQSDVWSFGILMWEIFTlGGSPYPG 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767960106  233 LhPMRALFKIPRNpPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd05099   240 I-PVEELFKLLRE-GHRMDKPSNCTHELYMLMRECWHAVPTQRPTFKQLVE 288
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
25-281 1.98e-17

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 84.68  E-value: 1.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKV----FKVLNKKNGQKAAVKILDpiHDIDE---EIEAEYNILKALSdHPNVVRFYGIYFKKDKVNgdkLW 97
Cdd:cd14205    10 QQLGKGNFGSVemcrYDPLQDNTGEVVAVKKLQ--HSTEEhlrDFEREIEILKSLQ-HDNIVKYKGVCYSAGRRN---LR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVTDLVKgflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLts 177
Cdd:cd14205    84 LIMEYLPYGSLRDYLQ---KHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVL-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  178 TRHRRNTSVGTP-----FWMAPEVIAceqqlDTTYDARCDTWSLGITAIEL-----GDGDPPLADLHPMRA--------- 238
Cdd:cd14205   159 PQDKEYYKVKEPgespiFWYAPESLT-----ESKFSVASDVWSFGVVLYELftyieKSKSPPAEFMRMIGNdkqgqmivf 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 767960106  239 -LFKIPRNpPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSEL 281
Cdd:cd14205   234 hLIELLKN-NGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDL 276
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
27-259 2.00e-17

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 84.58  E-value: 2.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKI--LDPIHDIDEEIEAEYNILKALsDHPNVVRFYGIYFKKDKVNGDKLWLVLELCS 104
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGEKIAIKScrLELSVKNKDRWCHEIQIMKKL-NHPNVVKACDVPEEMNFLVNDVPLLAMEYCS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  105 GGsvtDLVKgFLKRGER---MSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGV---KLVDFGVSAQLtsT 178
Cdd:cd14039    80 GG---DLRK-LLNKPENccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKivhKIIDLGYAKDL--D 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  179 RHRRNTS-VGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDG-DPPLADLHPMRALFKIPRNPPPKLRQPELW 256
Cdd:cd14039   154 QGSLCTSfVGTLQYLAPELFE-----NKSYTVTVDYWSFGTMVFECIAGfRPFLHNLQPFTWHEKIKKKDPKHIFAVEEM 228

                  ...
gi 767960106  257 SAE 259
Cdd:cd14039   229 NGE 231
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
27-229 2.62e-17

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 84.85  E-value: 2.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDPI---HDIDEEIEaEYNILKALsDHPNVVRFYGIyfkKDKVNGDKLWLVLELC 103
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKVFNNLsfmRPLDVQMR-EFEVLKKL-NHKNIVKLFAI---EEELTTRHKVLVMELC 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  104 SGGSVTDLvkgflkrgerMSEPLIAY---------ILHEALMGLQHLHNNKTIHRDVKGNNIL-LTTEGG---VKLVDFG 170
Cdd:cd13988    76 PCGSLYTV----------LEEPSNAYglpesefliVLRDVVAGMNHLRENGIVHRDIKPGNIMrVIGEDGqsvYKLTDFG 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767960106  171 VSAQLTSTRHRRNTsVGTPFWMAP---EVIACEQQLDTTYDARCDTWSLGITAIELGDGDPP 229
Cdd:cd13988   146 AARELEDDEQFVSL-YGTEEYLHPdmyERAVLRKDHQKKYGATVDLWSIGVTFYHAATGSLP 206
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
17-283 2.67e-17

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 83.78  E-value: 2.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   17 PSDTWEITETIGKGTYGKVFKVLnKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSdHPNVVRFYGIyfkkdkVNGDKL 96
Cdd:cd05067     5 PRETLKLVERLGAGQFGEVWMGY-YNGHTKVAIKSLKQGSMSPDAFLAEANLMKQLQ-HQRLVRLYAV------VTQEPI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDlvkgFLKRGERMSEPLIAYILHEALM--GLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:cd05067    77 YIITEYMENGSLVD----FLKTPSGIKLTINKLLDMAAQIaeGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LTSTRHRRNTSVGTPF-WMAPEVIACeqqldTTYDARCDTWSLGITAIELGD-GDPPLADLHPMRALFKIPRNppPKLRQ 252
Cdd:cd05067   153 IEDNEYTAREGAKFPIkWTAPEAINY-----GTFTIKSDVWSFGILLTEIVThGRIPYPGMTNPEVIQNLERG--YRMPR 225
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767960106  253 PELWSAEFNDFISKCLTKDYEKRPTVsELLQ 283
Cdd:cd05067   226 PDNCPEELYQLMRLCWKERPEDRPTF-EYLR 255
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
4-282 2.68e-17

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 87.23  E-value: 2.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106    4 LIGKtiIFDNFPD-----------PSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDpihdIDEEIEAEYNILKA- 71
Cdd:PTZ00283    8 MIGR--VCRTFPDtfakdeatakeQAKKYWISRVLGSGATGTVLCAKRVSDGEPFAVKVVD----MEGMSEADKNRAQAe 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   72 ----LS-DHPNVVRFYGIYFKKDKVNGDK---LWLVLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHN 143
Cdd:PTZ00283   82 vcclLNcDFFSIVKCHEDFAKKDPRNPENvlmIALVLDYANAGDLRQEIKSRAKTNRTFREHEAGLLFIQVLLAVHHVHS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  144 NKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRR--NTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAI 221
Cdd:PTZ00283  162 KHMIHRDIKSANILLCSNGLVKLGDFGFSKMYAATVSDDvgRTFCGTPYYVAPEIWR-----RKPYSKKADMFSLGVLLY 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767960106  222 ELGDGDPPL--ADLHP-MRALFKIPRNPPPklrqPELwSAEFNDFISKCLTKDYEKRPTVSELL 282
Cdd:PTZ00283  237 ELLTLKRPFdgENMEEvMHKTLAGRYDPLP----PSI-SPEMQEIVTALLSSDPKRRPSSSKLL 295
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
21-299 3.02e-17

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 84.71  E-value: 3.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIH---DIDEEIEAEYNILKAL---SDHPNVVRFYGIYFKKDKVNgd 94
Cdd:cd14223     2 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRikmKQGETLALNERIMLSLvstGDCPFIVCMSYAFHTPDKLS-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 klwLVLELCSGGsvtDLVKGFLKRGErMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:cd14223    80 ---FILDLMNGG---DLHYHLSQHGV-FSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LtsTRHRRNTSVGTPFWMAPEVIaceqQLDTTYDARCDTWSLGITAIELGDGDPPLADlHPMRALFKIPR-NPPPKLRQP 253
Cdd:cd14223   153 F--SKKKPHASVGTHGYMAPEVL----QKGVAYDSSADWFSLGCMLFKLLRGHSPFRQ-HKTKDKHEIDRmTLTMAVELP 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767960106  254 ELWSAEFNDFISKCLTKDYEKR-----PTVSELLQHKFITQIEGKDVMLQK 299
Cdd:cd14223   226 DSFSPELRSLLEGLLQRDVNRRlgcmgRGAQEVKEEPFFRGLDWQMVFLQK 276
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
12-287 3.18e-17

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 83.49  E-value: 3.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   12 DNFPdpSDTWEITEtIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSdHPNVVRFYGIYfkkdkV 91
Cdd:cd14113     3 DNFD--SFYSEVAE-LGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQVTHELGVLQSLQ-HPQLVGLLDTF-----E 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   92 NGDKLWLVLELCSGGSVTDlvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILL---TTEGGVKLVD 168
Cdd:cd14113    74 TPTSYILVLEMADQGRLLD----YVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVdqsLSKPTIKLAD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  169 FGVSAQLTSTRHRRNTsVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDPPLAD-------LHPMRALFK 241
Cdd:cd14113   150 FGDAVQLNTTYYIHQL-LGSPEFAAPEII-----LGNPVSLTSDLWSIGVLTYVLLSGVSPFLDesveetcLNICRLDFS 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767960106  242 IPRNPPPKLRQpelwsaEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14113   224 FPDDYFKGVSQ------KAKDFVCFLLQMDPAKRPSAALCLQEQWL 263
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
27-276 3.78e-17

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 83.46  E-value: 3.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQK--AAVKILDPIHD--IDEEIEAEYNILKALsDHPNVVRFYGIyfkkdkVNGDKLWLVLEL 102
Cdd:cd05115    12 LGSGNFGCVKKGVYKMRKKQidVAIKVLKQGNEkaVRDEMMREAQIMHQL-DNPYIVRMIGV------CEAEALMLVMEM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGSVTDLVKGflkRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS--TRH 180
Cdd:cd05115    85 ASGGPLNKFLSG---KKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALGAddSYY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  181 RRNTSVGTPF-WMAPEVIACEQqldttYDARCDTWSLGITAIE-LGDGDPPLADLHPMRALFKIPRNppPKLRQPELWSA 258
Cdd:cd05115   162 KARSAGKWPLkWYAPECINFRK-----FSSRSDVWSYGVTMWEaFSYGQKPYKKMKGPEVMSFIEQG--KRMDCPAECPP 234
                         250
                  ....*....|....*...
gi 767960106  259 EFNDFISKCLTKDYEKRP 276
Cdd:cd05115   235 EMYALMSDCWIYKWEDRP 252
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
17-218 4.26e-17

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 83.21  E-value: 4.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   17 PSDTWEITETIGKGTYGKVFK-VLNKKNGQKA----AVKIL--DPIHDIDEEIEAEYNILKALsDHPNVVRFYGIYFKKD 89
Cdd:cd05036     4 PRKNLTLIRALGQGAFGEVYEgTVSGMPGDPSplqvAVKTLpeLCSEQDEMDFLMEALIMSKF-NHPNIVRCIGVCFQRL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   90 KvngdkLWLVLELCSGGsvtDLvKGFLK----RGERMSEPLIAYILHEAL---MGLQHLHNNKTIHRDVKGNNILLTTEG 162
Cdd:cd05036    83 P-----RFILLELMAGG---DL-KSFLRenrpRPEQPSSLTMLDLLQLAQdvaKGCRYLEENHFIHRDIAARNCLLTCKG 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767960106  163 G---VKLVDFGVSAQL-TSTRHRRNTSVGTPF-WMAPEVIaceqqLDTTYDARCDTWSLGI 218
Cdd:cd05036   154 PgrvAKIGDFGMARDIyRADYYRKGGKAMLPVkWMPPEAF-----LDGIFTSKTDVWSFGV 209
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
20-233 4.34e-17

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 83.08  E-value: 4.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   20 TWEITETIGKGTYGKVFKVLNKKNGQKAAVKiLDPIHDIDEEIEAEYNILKALSDHPNVVRFYGiYFKKDKVNgdklWLV 99
Cdd:cd14017     1 RWKVVKKIGGGGFGEIYKVRDVVDGEEVAMK-VESKSQPKQVLKMEVAVLKKLQGKPHFCRLIG-CGRTERYN----YIV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  100 LELCsGGSVTDLVKGFLKRgeRMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG----VKLVDFGVSAQL 175
Cdd:cd14017    75 MTLL-GPNLAELRRSQPRG--KFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGPSdertVYILDFGLARQY 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  176 TST-----RHRRNTS--VGTPFWMApevIACEQQLDTTYdaRCDTWSLGITAIELGDGDPPLADL 233
Cdd:cd14017   152 TNKdgeveRPPRNAAgfRGTVRYAS---VNAHRNKEQGR--RDDLWSWFYMLIEFVTGQLPWRKL 211
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
25-281 4.34e-17

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 82.91  E-value: 4.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFK---VLNKKNGQKAAVKILDPIHDIdEEIEA---EYNILKALSdHPNVVRFYGIYFKKDkvnGDKLWL 98
Cdd:cd05058     1 EVIGKGHFGCVYHgtlIDSDGQKIHCAVKSLNRITDI-EEVEQflkEGIIMKDFS-HPNVLSLLGICLPSE---GSPLVV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   99 VLELCSGgsvtDLvKGFLKRGER--MSEPLIAYILHEAlMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:cd05058    76 LPYMKHG----DL-RNFIRSETHnpTVKDLIGFGLQVA-KGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIY 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  177 STRH---RRNTSVGTPF-WMAPEVIacEQQLDTTydaRCDTWSLGITAIEL-GDGDPPLADLHPM---RALFKIPRnppp 248
Cdd:cd05058   150 DKEYysvHNHTGAKLPVkWMALESL--QTQKFTT---KSDVWSFGVLLWELmTRGAPPYPDVDSFditVYLLQGRR---- 220
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767960106  249 kLRQPELWSAEFNDFISKCLTKDYEKRPTVSEL 281
Cdd:cd05058   221 -LLQPEYCPDPLYEVMLSCWHPKPEMRPTFSEL 252
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
19-286 4.71e-17

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 83.73  E-value: 4.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDiDEEIEA----EYNILKALSDHPNVVRFYGIYFKKDKvNGD 94
Cdd:cd07837     1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLEME-EEGVPStalrEVSLLQMLSQSIYIVRLLDVEHVEEN-GKP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 KLWLVLELCSggsvTDLvKGFLKRGER-----MSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGV-KLVD 168
Cdd:cd07837    79 LLYLVFEYLD----TDL-KKFIDSYGRgphnpLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLlKIAD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  169 FGVSAQLTSTRHRRNTSVGTPFWMAPEVIACEqqldTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKI------ 242
Cdd:cd07837   154 LGLGRAFTIPIKSYTHEIVTLWYRAPEVLLGS----THYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIfrllgt 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767960106  243 ------------------PRNPPPKLRQ--PELwSAEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd07837   230 pneevwpgvsklrdwheyPQWKPQDLSRavPDL-EPEGVDLLTKMLAYDPAKRISAKAALQHPY 292
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
21-294 6.58e-17

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 84.18  E-value: 6.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITET------IGKGTYGKVFKVLNKKNGQKAAVKILDpiHDIDEEIEA-----EYNILKALSdHPNVVRFYGIYFKKD 89
Cdd:cd07879    11 WELPERytslkqVGSGAYGSVCSAIDKRTGEKVAIKKLS--RPFQSEIFAkrayrELTLLKHMQ-HENVIGLLDVFTSAV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   90 KVNG-DKLWLVLELCSggsvTDLVKgflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVD 168
Cdd:cd07879    88 SGDEfQDFYLVMPYMQ----TDLQK---IMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  169 FGVSaqltstRHRRNTSVG---TPFWMAPEVIACEQQldttYDARCDTWSLGITAIELGDGDPPLAD---LHPMRALFKI 242
Cdd:cd07879   161 FGLA------RHADAEMTGyvvTRWYRAPEVILNWMH----YNQTVDIWSVGCIMAEMLTGKTLFKGkdyLDQLTQILKV 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767960106  243 PRNPPPKLRQ--------------PELWSAEFN-----------DFISKCLTKDYEKRPTVSELLQHKFITQIEGKD 294
Cdd:cd07879   231 TGVPGPEFVQkledkaaksyikslPKYPRKDFStlfpkaspqavDLLEKMLELDVDKRLTATEALEHPYFDSFRDAD 307
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
27-302 6.65e-17

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 84.01  E-value: 6.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKIL--DPIHDiDEEI---EAEYNILKALSDHPNVVRFYGIYFKKDKvngdkLWLVLE 101
Cdd:cd05588     3 IGRGSYAKVLMVELKKTKRIYAMKVIkkELVND-DEDIdwvQTEKHVFETASNHPFLVGLHSCFQTESR-----LFFVIE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  102 LCSGGsvtDLVKgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHR 181
Cdd:cd05588    77 FVNGG---DLMF-HMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  182 RNTSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPL--------ADLHPMRALFKIPRNPPpkLRQP 253
Cdd:cd05588   153 TSTFCGTPNYIAPEILRGED-----YGFSVDWWALGVLMFEMLAGRSPFdivgssdnPDQNTEDYLFQVILEKP--IRIP 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  254 ELWSAEFNDFISKCLTKDYEKR------PTVSELLQHKFITQIEGkDVMLQKQLT 302
Cdd:cd05588   226 RSLSVKAASVLKGFLNKNPAERlgchpqTGFADIQSHPFFRTIDW-EQLEQKQVT 279
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
22-282 1.20e-16

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 81.99  E-value: 1.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKvlNKKNGQkAAVKILDPIHDIDEEIEAEYNILKAL--SDHPNVVRFYGIYFKKDkvngdkLWLV 99
Cdd:cd14150     3 SMLKRIGTGSFGTVFR--GKWHGD-VAVKILKVTEPTPEQLQAFKNEMQVLrkTRHVNILLFMGFMTRPN------FAII 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  100 LELCSGGSVTDLVKGFLKRGERMSEPLIAyilHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT--S 177
Cdd:cd14150    74 TQWCEGSSLYRHLHVTETRFDTMQLIDVA---RQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTrwS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  178 TRHRRNTSVGTPFWMAPEVIacEQQLDTTYDARCDTWSLGITAIELGDGDPPLAD---------------LHPmrALFKI 242
Cdd:cd14150   151 GSQQVEQPSGSILWMAPEVI--RMQDTNPYSFQSDVYAYGVVLYELMSGTLPYSNinnrdqiifmvgrgyLSP--DLSKL 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 767960106  243 PRNPPPKLRQpelwsaefndFISKCLTKDYEKRPTVSELL 282
Cdd:cd14150   227 SSNCPKAMKR----------LLIDCLKFKREERPLFPQIL 256
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
25-282 1.58e-16

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 82.38  E-value: 1.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQK----AAVKILDPIHD--IDEEIEAEYNILKALsDHPNVVRFYGIYFKKdkvngdKLWL 98
Cdd:cd05108    13 KVLGSGAFGTVYKGLWIPEGEKvkipVAIKELREATSpkANKEILDEAYVMASV-DNPHVCRLLGICLTS------TVQL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   99 VLELCSGGSVTDLVKgflKRGERM-SEPLIAYILHEAlMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 177
Cdd:cd05108    86 ITQLMPFGCLLDYVR---EHKDNIgSQYLLNWCVQIA-KGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  178 TRHRRNTSVG-TPF-WMAPEVIaceqqLDTTYDARCDTWSLGITAIELGD-GDPPLaDLHPMRALFKIPRNpPPKLRQPE 254
Cdd:cd05108   162 EEKEYHAEGGkVPIkWMALESI-----LHRIYTHQSDVWSYGVTVWELMTfGSKPY-DGIPASEISSILEK-GERLPQPP 234
                         250       260
                  ....*....|....*....|....*...
gi 767960106  255 LWSAEFNDFISKCLTKDYEKRPTVSELL 282
Cdd:cd05108   235 ICTIDVYMIMVKCWMIDADSRPKFRELI 262
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
21-172 1.66e-16

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 81.35  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKIlDPIHDIDEEIEAEYNILKALSDHPNVVRFYgiYFKKDkvnGDKLWLVL 100
Cdd:cd14016     2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKI-EKKDSKHPQLEYEAKVYKLLQGGPGIPRLY--WFGQE---GDYNVMVM 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  101 ELCsGGSVTDLvkgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVK---LVDFGVS 172
Cdd:cd14016    76 DLL-GPSLEDL---FNKCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNkvyLIDFGLA 146
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
19-285 1.93e-16

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 81.30  E-value: 1.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITET-------IGKGTYGKVFKVL-NkkNGQKAAVKILDPIHDIDEEIEAEYNILKALSdHPNVVRFYGIYFKKDK 90
Cdd:cd05068     1 DQWEIDRKslkllrkLGSGQFGEVWEGLwN--NTTPVAVKTLKPGTMDPEDFLREAQIMKKLR-HPKLIQLYAVCTLEEP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   91 VngdklWLVLELCSGGSVTDLVKGflkRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFG 170
Cdd:cd05068    78 I-----YIITELMKHGSLLEYLQG---KGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  171 VsAQLTSTRHRRNTSVGTPF---WMAPEVIACEQqldttYDARCDTWSLGITAIEL-GDGDPPLADLHPMRALFKIPRN- 245
Cdd:cd05068   150 L-ARVIKVEDEYEAREGAKFpikWTAPEAANYNR-----FSIKSDVWSFGILLTEIvTYGRIPYPGMTNAEVLQQVERGy 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767960106  246 --PPPKLRQPELWsaefnDFISKCLTKDYEKRPTVsELLQHK 285
Cdd:cd05068   224 rmPCPPNCPPQLY-----DIMLECWKADPMERPTF-ETLQWK 259
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
16-286 2.11e-16

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 81.62  E-value: 2.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITET-------IGKGTYGKVFKvlNKKNGQkAAVKILDPIHDIDEEIEAEYNILKAL--SDHPNVVRFYGiYF 86
Cdd:cd14149     2 DSSYYWEIEASevmlstrIGSGSFGTVYK--GKWHGD-VAVKILKVVDPTPEQFQAFRNEVAVLrkTRHVNILLFMG-YM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   87 KKDKvngdkLWLVLELCSGGSvtdLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKL 166
Cdd:cd14149    78 TKDN-----LAIVTQWCEGSS---LYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  167 VDFGVSAQLT--STRHRRNTSVGTPFWMAPEVIacEQQLDTTYDARCDTWSLGITAIELGDGDPPLADL----------- 233
Cdd:cd14149   150 GDFGLATVKSrwSGSQQVEQPTGSILWMAPEVI--RMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHInnrdqiifmvg 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767960106  234 --HPMRALFKIPRNPPPKLRQpelwsaefndFISKCLTKDYEKRP------TVSELLQHKF 286
Cdd:cd14149   228 rgYASPDLSKLYKNCPKAMKR----------LVADCIKKVKEERPlfpqilSSIELLQHSL 278
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
27-283 2.35e-16

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 81.40  E-value: 2.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVK-ILDPIHDIDE--EIEAEYNILKALsDHPNVVRFYGIYFKKDKVngdKLWLVLELC 103
Cdd:cd14049    14 LGKGGYGKVYKVRNKLDGQYYAIKkILIKKVTKRDcmKVLREVKVLAGL-QHPNIVGYHTAWMEHVQL---MLYIQMQLC 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  104 SGgSVTDLVKGFLKRGERMSEPLIAY----------ILHEALMGLQHLHNNKTIHRDVKGNNILLT-TEGGVKLVDFGVS 172
Cdd:cd14049    90 EL-SLWDWIVERNKRPCEEEFKSAPYtpvdvdvttkILQQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHVRIGDFGLA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQL-------TSTRHRRNTS-----VGTPFWMAPEviaceqQLD-TTYDARCDTWSLGITAIELgdGDPPLADLHPMRAL 239
Cdd:cd14049   169 CPDilqdgndSTTMSRLNGLthtsgVGTCLYAAPE------QLEgSHYDFKSDMYSIGVILLEL--FQPFGTEMERAEVL 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767960106  240 FKIPRNPPPK---LRQPELwsaefNDFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd14049   241 TQLRNGQIPKslcKRWPVQ-----AKYIKLLTSTEPSERPSASQLLE 282
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
27-286 2.47e-16

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 80.40  E-value: 2.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKvlNKKNGQ-KAAVKILDPIHDIDEEIEAEYNILKALsDHPNVVRFYGIYFKkdkvnGDKLWLVLELCSG 105
Cdd:cd05034     3 LGAGQFGEVWM--GVWNGTtKVAVKTLKPGTMSPEAFLQEAQIMKKL-RHDKLVQLYAVCSD-----EEPIYIVTELMSK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  106 GSVTDlvkgFLK--RGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHrrN 183
Cdd:cd05034    75 GSLLD----YLRtgEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLIEDDEY--T 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  184 TSVGTPF---WMAPEVIaceqqLDTTYDARCDTWSLGITAIEL-GDGDPPLADLHPMRALFKIPRNppPKLRQPELWSAE 259
Cdd:cd05034   149 AREGAKFpikWTAPEAA-----LYGRFTIKSDVWSFGILLYEIvTYGRVPYPGMTNREVLEQVERG--YRMPKPPGCPDE 221
                         250       260
                  ....*....|....*....|....*..
gi 767960106  260 FNDFISKCLTKDYEKRPTVsELLQHKF 286
Cdd:cd05034   222 LYDIMLQCWKKEPEERPTF-EYLQSFL 247
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
17-282 2.55e-16

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 81.24  E-value: 2.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   17 PSDTWEITETIGKGTYGKVFK--VLNKKNGQ---KAAVKILDPIHDIDEEIE--AEYNILKALsDHPNVVRFYGIYFKkd 89
Cdd:cd05032     4 PREKITLIRELGQGSFGMVYEglAKGVVKGEpetRVAIKTVNENASMRERIEflNEASVMKEF-NCHHVVRLLGVVST-- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   90 kvnGDKLWLVLELCSGGsvtDLvKGFLK--RGERMSEPLIAYILHEALM--------GLQHLHNNKTIHRDVKGNNILLT 159
Cdd:cd05032    81 ---GQPTLVVMELMAKG---DL-KSYLRsrRPEAENNPGLGPPTLQKFIqmaaeiadGMAYLAAKKFVHRDLAARNCMVA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  160 TEGGVKLVDFGVSAQLTSTRHRRNTSVGT-PF-WMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDgdppLADLhPMR 237
Cdd:cd05032   154 EDLTVKIGDFGMTRDIYETDYYRKGGKGLlPVrWMAPESLK-----DGVFTTKSDVWSFGVVLWEMAT----LAEQ-PYQ 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767960106  238 AL--------------FKIPRNPPPKLRqpelwsaefnDFISKCLTKDYEKRPTVSELL 282
Cdd:cd05032   224 GLsneevlkfvidgghLDLPENCPDKLL----------ELMRMCWQYNPKMRPTFLEIV 272
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
20-287 3.42e-16

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 80.35  E-value: 3.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   20 TWEITETIGKGTYGKVFKVLNKKNGQKAAVKILdPIHDIDEE-IEAEYNILKALSdHPNVVRFYGIYfkkdkVNGDKLWL 98
Cdd:cd14110     4 TYAFQTEINRGRFSVVRQCEEKRSGQMLAAKII-PYKPEDKQlVLREYQVLRRLS-HPRIAQLHSAY-----LSPRHLVL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   99 VLELCSGgsvTDLVKGFLKRGErMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST 178
Cdd:cd14110    77 IEELCSG---PELLYNLAERNS-YSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  179 R----HRRNTSVGTpfwMAPEVIACEQQLDTTydarcDTWSLGITA-IELGDGDPPLADLHpmRALFKIPRNPPPKLRQ- 252
Cdd:cd14110   153 KvlmtDKKGDYVET---MAPELLEGQGAGPQT-----DIWAIGVTAfIMLSADYPVSSDLN--WERDRNIRKGKVQLSRc 222
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767960106  253 -PELWSAEFNdFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14110   223 yAGLSGGAVN-FLKSTLCAKPWGRPTASECLQNPWL 257
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
21-218 3.67e-16

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 81.45  E-value: 3.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPihDIDEEIE---AEYNILKAL-SDHPNVVRFYGIYFKKDKV----- 91
Cdd:cd13977     2 YSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRC--NAPENVElalREFWALSSIqRQHPNVIQLEECVLQRDGLaqrms 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   92 NGDK--------------------------LWLVLELCSGGsvtDLVKGFLKRgeRMSEPLIAYILHEALMGLQHLHNNK 145
Cdd:cd13977    80 HGSSksdlylllvetslkgercfdprsacyLWFVMEFCDGG---DMNEYLLSR--RPDRQTNTSFMLQLSSALAFLHRNQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  146 TIHRDVKGNNILLTTEGG---VKLVDFGVSAQLTST-----------RHRRNTSVGTPFWMAPEViaceqqLDTTYDARC 211
Cdd:cd13977   155 IVHRDLKPDNILISHKRGepiLKVADFGLSKVCSGSglnpeepanvnKHFLSSACGSDFYMAPEV------WEGHYTAKA 228

                  ....*..
gi 767960106  212 DTWSLGI 218
Cdd:cd13977   229 DIFALGI 235
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
27-283 5.07e-16

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 80.62  E-value: 5.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFK-VLNKKNgqkAAVKILDPIHDIDEE-----IEAEYNILKALSdHPNVVRFYGiyFKKDkvnGDKLWLVL 100
Cdd:cd14158    23 LGEGGFGVVFKgYINDKN---VAVKKLAAMVDISTEdltkqFEQEIQVMAKCQ-HENLVELLG--YSCD---GPQLCLVY 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCSGGSVTDLVkGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGV---SAQLTS 177
Cdd:cd14158    94 TYMPNGSLLDRL-ACLNDTPPLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLaraSEKFSQ 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  178 TRHRRNTsVGTPFWMAPEVIACEqqldttYDARCDTWSLGITAIELGDGDPPLaDLHPMRALFKIPRNpppKLRQPELWS 257
Cdd:cd14158   173 TIMTERI-VGTTAYMAPEALRGE------ITPKSDIFSFGVVLLEIITGLPPV-DENRDPQLLLDIKE---EIEDEEKTI 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767960106  258 AEFND----------------FISKCLTKDYEKRPTVSELLQ 283
Cdd:cd14158   242 EDYVDkkmgdwdstsieamysVASQCLNDKKNRRPDIAKVQQ 283
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
18-288 5.42e-16

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 80.04  E-value: 5.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   18 SDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEE--IEAEYNILKALSdHPNVVRFYgiyfkKDKVNGDK 95
Cdd:cd14183     5 SERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEhmIQNEVSILRRVK-HPNIVLLI-----EEMDMPTE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSGGSVTDLVKGFLKRGERMSEPLIaYILHEALmglQHLHNNKTIHRDVKGNNILLTTE----GGVKLVDFGV 171
Cdd:cd14183    79 LYLVMELVKGGDLFDAITSTNKYTERDASGML-YNLASAI---KYLHSLNIVHRDIKPENLLVYEHqdgsKSLKLGDFGL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  172 SAQLTSTRHrrnTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIELGDGDPPL-ADLHPMRALFKIPRNPPPKL 250
Cdd:cd14183   155 ATVVDGPLY---TVCGTPTYVAPEIIA-----ETGYGLKVDIWAAGVITYILLCGFPPFrGSGDDQEVLFDQILMGQVDF 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767960106  251 RQPeLW---SAEFNDFISKCLTKDYEKRPTVSELLQHKFIT 288
Cdd:cd14183   227 PSP-YWdnvSDSAKELITMMLQVDVDQRYSALQVLEHPWVN 266
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
17-283 6.54e-16

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 80.84  E-value: 6.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   17 PSD-TWEITET-------IGKGTYGKVFKV----LNKKNGQKA---AVKIL-DPIHDID-EEIEAEYNILKALSDHPNVV 79
Cdd:cd05100     2 PADpKWELSRTrltlgkpLGEGCFGQVVMAeaigIDKDKPNKPvtvAVKMLkDDATDKDlSDLVSEMEMMKMIGKHKNII 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   80 RFYGIYfkkdkVNGDKLWLVLELCSGGSVTDLVKGFLKRG------------ERMSEPLIAYILHEALMGLQHLHNNKTI 147
Cdd:cd05100    82 NLLGAC-----TQDGPLYVLVEYASKGNLREYLRARRPPGmdysfdtcklpeEQLTFKDLVSCAYQVARGMEYLASQKCI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  148 HRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRRNTSVGT-PF-WMAPEVIaceqqLDTTYDARCDTWSLGITAIELGD 225
Cdd:cd05100   157 HRDLAARNVLVTEDNVMKIADFGLARDVHNIDYYKKTTNGRlPVkWMAPEAL-----FDRVYTHQSDVWSFGVLLWEIFT 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767960106  226 -GDPPLADLhPMRALFKIPRNpPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd05100   232 lGGSPYPGI-PVEELFKLLKE-GHRMDKPANCTHELYMIMRECWHAVPSQRPTFKQLVE 288
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
22-283 7.08e-16

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 82.92  E-value: 7.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNGQKAAVKILDPihDI--DEEIEA----EynilkALS----DHPNVVRFY------GIY 85
Cdd:NF033483   10 EIGERIGRGGMAEVYLAKDTRLDRDVAVKVLRP--DLarDPEFVArfrrE-----AQSaaslSHPNIVSVYdvgedgGIP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   86 FkkdkvngdklwLVLELCSGgsvTDLvKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVK 165
Cdd:NF033483   83 Y-----------IVMEYVDG---RTL-KDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  166 LVDFG----VSAQ-LTSTrhrrNTSVGTPFWMAPeviacEQQLDTTYDARCDTWSLGITAIEL--G----DGDPPLADLH 234
Cdd:NF033483  148 VTDFGiaraLSSTtMTQT----NSVLGTVHYLSP-----EQARGGTVDARSDIYSLGIVLYEMltGrppfDGDSPVSVAY 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  235 -----PMralfkiprnPPPKLRQPELwSAEFNDFISKCLTKDYEKRP-TVSELLQ 283
Cdd:NF033483  219 khvqeDP---------PPPSELNPGI-PQSLDAVVLKATAKDPDDRYqSAAEMRA 263
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
21-294 7.49e-16

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 80.86  E-value: 7.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITE------TIGKGTYGKVFKVLNKKNGQKAAVKILD-PIHDI--DEEIEAEYNILKALSdHPNVVRFYGIYFKKDKV 91
Cdd:cd07878    11 WEVPEryqnltPVGSGAYGSVCSAYDTRLRQKVAVKKLSrPFQSLihARRTYRELRLLKHMK-HENVIGLLDVFTPATSI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   92 -NGDKLWLVLELCsGGSVTDLVKGflkrgERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFG 170
Cdd:cd07878    90 eNFNEVYLVTNLM-GADLNNIVKC-----QKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  171 VSAQltsTRHRRNTSVGTPFWMAPEVIACEQQldttYDARCDTWSLGITAIELGDGDP--PLAD-LHPMRALFKIPRNPP 247
Cdd:cd07878   164 LARQ---ADDEMTGYVATRWYRAPEIMLNWMH----YNQTVDIWSVGCIMAELLKGKAlfPGNDyIDQLKRIMEVVGTPS 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767960106  248 PKLRQ--------------PELWSAEFN-----------DFISKCLTKDYEKRPTVSELLQHKFITQIEGKD 294
Cdd:cd07878   237 PEVLKkisseharkyiqslPHMPQQDLKkifrganplaiDLLEKMLVLDSDKRISASEALAHPYFSQYHDPE 308
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
22-284 9.14e-16

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 78.87  E-value: 9.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVfkVLNKKNGQKAAVKILDpiHDIDEE-IEAEYNILKALSdHPNVVRFYGIYFKKDkvngDKLWLVL 100
Cdd:cd05082     9 KLLQTIGKGEFGDV--MLGDYRGNKVAVKCIK--NDATAQaFLAEASVMTQLR-HSNLVQLLGVIVEEK----GGLYIVT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCSGGSVTDLVKgflKRGERM--SEPLIAYILhEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTST 178
Cdd:cd05082    80 EYMAKGSLVDYLR---SRGRSVlgGDCLLKFSL-DVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASST 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  179 RHRRNTSVGtpfWMAPEVIAcEQQLDTtydaRCDTWSLGITAIELGD-GDPPLADLhPMRALfkIPR-NPPPKLRQPELW 256
Cdd:cd05082   156 QDTGKLPVK---WTAPEALR-EKKFST----KSDVWSFGILLWEIYSfGRVPYPRI-PLKDV--VPRvEKGYKMDAPDGC 224
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767960106  257 SAEFNDFISKCLTKDYEKRPT---VSELLQH 284
Cdd:cd05082   225 PPAVYDVMKNCWHLDAAMRPSflqLREQLEH 255
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
16-287 1.01e-15

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 78.95  E-value: 1.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTwEITETIGKGTYGKVFKVLNKKNGQK---AAVKILDPIHDIDEEIE--AEYNILKALsDHPNVVRFYGIYFKkdk 90
Cdd:cd05033     2 DASYV-TIEKVIGGGEFGEVCSGSLKLPGKKeidVAIKTLKSGYSDKQRLDflTEASIMGQF-DHPNVIRLEGVVTK--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   91 vnGDKLWLVLELCSGGSVtdlvKGFLKRGE-RMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDF 169
Cdd:cd05033    77 --SRPVMIVTEYMENGSL----DKFLRENDgKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  170 GVSAQLTSTRHRRNTSVG-TPF-WMAPEVIACEQqldttYDARCDTWSLGITAIE-LGDGDPPLADL---HPMRALFKIP 243
Cdd:cd05033   151 GLSRRLEDSEATYTTKGGkIPIrWTAPEAIAYRK-----FTSASDVWSFGIVMWEvMSYGERPYWDMsnqDVIKAVEDGY 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767960106  244 RNPPPK-----LRQPELWsaefndfiskCLTKDYEKRPTVSELLQ--HKFI 287
Cdd:cd05033   226 RLPPPMdcpsaLYQLMLD----------CWQKDRNERPTFSQIVStlDKMI 266
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
16-282 1.04e-15

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 78.64  E-value: 1.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITEtIGKGTYGKVfkVLNKKNGQ-KAAVKILDPIHDIDEEIEAEYNILKALSdHPNVVRFYGIYFKKDKvngd 94
Cdd:cd05059     2 DPSELTFLKE-LGSGQFGVV--HLGKWRGKiDVAIKMIKEGSMSEDDFIEEAKVMMKLS-HPKLVQLYGVCTKQRP---- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 kLWLVLELCSGGSVTDLVKgflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSA- 173
Cdd:cd05059    74 -IFIVTEYMANGCLLNYLR---ERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARy 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  174 ----QLTStrhrrntSVGTPF---WMAPEVIaceqqLDTTYDARCDTWSLGITAIEL-GDGDPPLADLHPMRALFKIPRN 245
Cdd:cd05059   150 vlddEYTS-------SVGTKFpvkWSPPEVF-----MYSKFSSKSDVWSFGVLMWEVfSEGKMPYERFSNSEVVEHISQG 217
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767960106  246 ppPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELL 282
Cdd:cd05059   218 --YRLYRPHLAPTEVYTIMYSCWHEKPEERPTFKILL 252
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
27-238 1.14e-15

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 78.73  E-value: 1.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKvlNKKNGQKAAVK-----ILDPIHDIDEEIEaEYNILKALsDHPNVVRFYGIYFKkdkvNGDKLWLVLE 101
Cdd:cd14064     1 IGSGSFGKVYK--GRCRNKIVAIKryranTYCSKSDVDMFCR-EVSILCRL-NHPCVIQFVGACLD----DPSQFAIVTQ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  102 LCSGGSVTDLVKGfLKRGERMSEPLIayILHEALMGLQHLHN--NKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTStR 179
Cdd:cd14064    73 YVSGGSLFSLLHE-QKRVIDLQSKLI--IAVDVAKGMEYLHNltQPIIHRDLNSHNILLYEDGHAVVADFGESRFLQS-L 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767960106  180 HRRNTSV--GTPFWMAPEVIAceqqLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRA 238
Cdd:cd14064   149 DEDNMTKqpGNLRWMAPEVFT----QCTRYSIKADVFSYALCLWELLTGEIPFAHLKPAAA 205
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
25-223 1.38e-15

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 79.02  E-value: 1.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKvlNKKNGQKAAVKILdPIHDiDEEIEAEYNILKA-LSDHPNVVRFYGIYfKKDKVNGDKLWLVLELC 103
Cdd:cd13998     1 EVIGKGRFGEVWK--ASLKNEPVAVKIF-SSRD-KQSWFREKEIYRTpMLKHENILQFIAAD-ERDTALRTELWLVTAFH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  104 SGGSVTDlvkgFLKRGERMSEPLIaYILHEALMGLQHLHNNKTI---------HRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:cd13998    76 PNGSL*D----YLSLHTIDWVSLC-RLALSVARGLAHLHSEIPGctqgkpaiaHRDLKSKNILVKNDGTCCIADFGLAVR 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767960106  175 LTSTRHR----RNTSVGTPFWMAPEVIACEQQLDTTYD-ARCDTWSLGITAIEL 223
Cdd:cd13998   151 LSPSTGEednaNNGQVGTKRYMAPEVLEGAINLRDFESfKRVDIYAMGLVLWEM 204
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
22-276 1.50e-15

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 78.29  E-value: 1.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITETIGKGTYGKVFKVLNKKNG----QKAAV--KILDPIH-DIDEEIEAEYNILKALSdHPNVVRFYGIYFKKDKVngd 94
Cdd:cd05037     2 TFHEHLGQGTFTNIYDGILREVGdgrvQEVEVllKVLDSDHrDISESFFETASLMSQIS-HKHLVKLYGVCVADENI--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 klwLVLELCSGGSVTDLVKgflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG------VKLVD 168
Cdd:cd05037    78 ---MVQEYVRYGPLDKYLR---RMGNNVPLSWKLQVAKQLASALHYLEDKKLIHGNVRGRNILLAREGLdgyppfIKLSD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  169 FGVSAQLTSTRHRRNTSvgtPfWMAPEviaCEQQLDTTYDARCDTWSLGITAIEL-GDGDPPLADLHPMRAL-FKIPRNP 246
Cdd:cd05037   152 PGVPITVLSREERVDRI---P-WIAPE---CLRNLQANLTIAADKWSFGTTLWEIcSGGEEPLSALSSQEKLqFYEDQHQ 224
                         250       260       270
                  ....*....|....*....|....*....|
gi 767960106  247 PPKLRQPELWSaefndFISKCLTKDYEKRP 276
Cdd:cd05037   225 LPAPDCAELAE-----LIMQCWTYEPTKRP 249
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
21-228 1.57e-15

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 79.83  E-value: 1.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKildPIHDIDEEIEAEYNILKA-----LSDHPNVVRFYGIYFKKDKVNGDK 95
Cdd:cd07859     2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIK---KINDVFEHVSDATRILREikllrLLRHPDIVEIKHIMLPPSRREFKD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSggsvTDLVKgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFG---VS 172
Cdd:cd07859    79 IYVVFELME----SDLHQ-VIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGlarVA 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767960106  173 AQLTSTRHRRNTSVGTPFWMAPEVIACeqqLDTTYDARCDTWSLGITAIELGDGDP 228
Cdd:cd07859   154 FNDTPTAIFWTDYVATRWYRAPELCGS---FFSKYTPAIDIWSIGCIFAEVLTGKP 206
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
18-226 1.79e-15

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 78.97  E-value: 1.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   18 SDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEA--EYNILKALSdHPNVVRFYGIYFKKDKvngdk 95
Cdd:cd07869     4 ADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAirEASLLKGLK-HANIVLLHDIIHTKET----- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSggsvTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL 175
Cdd:cd07869    78 LTLVFEYVH----TDLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAK 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767960106  176 TSTRHRRNTSVGTPFWMAPEVIACEqqldTTYDARCDTWSLGITAIELGDG 226
Cdd:cd07869   154 SVPSHTYSNEVVTLWYRPPDVLLGS----TEYSTCLDMWGVGCIFVEMIQG 200
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
27-288 1.90e-15

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 80.07  E-value: 1.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILD-PIHDIDEEIEA--EYNILKALsDHPNVVRFYGIYFKKDKVNG-DKLWLVLEL 102
Cdd:cd07876    29 IGSGAQGIVCAAFDTVLGINVAVKKLSrPFQNQTHAKRAyrELVLLKCV-NHKNIISLLNVFTPQKSLEEfQDVYLVMEL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGgSVTDLVKGFLKRgERMSepliaYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVsAQLTSTRHRR 182
Cdd:cd07876   108 MDA-NLCQVIHMELDH-ERMS-----YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGL-ARTACTNFMM 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  183 NTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGD--------------------PPLADLhpMRALFKI 242
Cdd:cd07876   180 TPYVVTRYYRAPEVI-----LGMGYKENVDIWSVGCIMGELVKGSvifqgtdhidqwnkvieqlgTPSAEF--MNRLQPT 252
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767960106  243 PRN-----P----------------PPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFIT 288
Cdd:cd07876   253 VRNyvenrPqypgisfeelfpdwifPSESERDKLKTSQARDLLSKMLVIDPDKRISVDEALRHPYIT 319
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
27-170 2.36e-15

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 74.40  E-value: 2.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKILDPIHDID-EEIEAEYNILKALSDH-PNVVRFYGIYfkkdkVNGDKLWLVLELCS 104
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNEEgEDLESEMDILRRLKGLeLNIPKVLVTE-----DVDGPNILLMELVK 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767960106  105 GGSVTDLVKGflkrgERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFG 170
Cdd:cd13968    76 GGTLIAYTQE-----EELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
25-286 2.48e-15

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 78.46  E-value: 2.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVLNKKNGQKAAVKIldpIHDIDEE-----IEAEYNILKALSdHPNVVRFYGIYFKKDKvngdkLWLV 99
Cdd:cd07870     6 EKLGEGSYATVYKGISRINGQLVALKV---ISMKTEEgvpftAIREASLLKGLK-HANIVLLHDIIHTKET-----LTFV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  100 LELCSggsvTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTR 179
Cdd:cd07870    77 FEYMH----TDLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIPS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  180 HRRNTSVGTPFWMAPEVIACEqqldTTYDARCDTWSLGITAIELGDGDP---------------------PLADLHPmrA 238
Cdd:cd07870   153 QTYSSEVVTLWYRPPDVLLGA----TDYSSALDIWGAGCIFIEMLQGQPafpgvsdvfeqlekiwtvlgvPTEDTWP--G 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767960106  239 LFKIPR--------NPPPKLRqpELWS-----AEFNDFISKCLTKDYEKRPTVSELLQHKF 286
Cdd:cd07870   227 VSKLPNykpewflpCKPQQLR--VVWKrlsrpPKAEDLASQMLMMFPKDRISAQDALLHPY 285
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
25-223 2.64e-15

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 78.52  E-value: 2.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKVlnKKNGQKAAVKILdPIHDiDEEIEAEYNILKALS-DHPNVVRFYGIYfKKDKVNGDKLWLVLELC 103
Cdd:cd14053     1 EIKARGRFGAVWKA--QYLNRLVAVKIF-PLQE-KQSWLTEREIYSLPGmKHENILQFIGAE-KHGESLEAEYWLITEFH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  104 SGGSVTDLVKG-------FLKRGERMSEPLiAYiLHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 176
Cdd:cd14053    76 ERGSLCDYLKGnviswneLCKIAESMARGL-AY-LHEDIPATNGGHKPSIAHRDFKSKNVLLKSDLTACIADFGLALKFE 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767960106  177 STRHRRNT--SVGTPFWMAPEVIacEQQLDTTYDA--RCDTWSLGITAIEL 223
Cdd:cd14053   154 PGKSCGDThgQVGTRRYMAPEVL--EGAINFTRDAflRIDMYAMGLVLWEL 202
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
27-289 2.70e-15

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 78.17  E-value: 2.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAA-VKILDPIHDIDEE--IEAEYNILKALSdHPNVVRFYGIYfkKDKVNGDK-LWLVLEL 102
Cdd:cd14030    33 IGRGSFKTVYKGLDTETTVEVAwCELQDRKLSKSERqrFKEEAGMLKGLQ-HPNIVRFYDSW--ESTVKGKKcIVLVTEL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGSVtdlvKGFLKRGERMSEPLIAYILHEALMGLQHLHNNK--TIHRDVKGNNILLT-TEGGVKLVDFGVSAQLTSTR 179
Cdd:cd14030   110 MTSGTL----KTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATLKRASF 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  180 HRrnTSVGTPFWMAPEViaceqqLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQPELWSAE 259
Cdd:cd14030   186 AK--SVIGTPEFMAPEM------YEEKYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRRVTSGVKPASFDKVAIPE 257
                         250       260       270
                  ....*....|....*....|....*....|
gi 767960106  260 FNDFISKCLTKDYEKRPTVSELLQHKFITQ 289
Cdd:cd14030   258 VKEIIEGCIRQNKDERYAIKDLLNHAFFQE 287
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
17-284 3.36e-15

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 78.87  E-value: 3.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   17 PSDTWEITETIGKGTYGKV-----FKVLNKKNGQKAAVKILD--PIHDIDEEIEAEYNILKALSDHPNVVRFYGIYFKKd 89
Cdd:cd05103     5 PRDRLKLGKPLGRGAFGQVieadaFGIDKTATCRTVAVKMLKegATHSEHRALMSELKILIHIGHHLNVVNLLGACTKP- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   90 kvnGDKLWLVLELCSGGSVTDLVKGflKRGE---------------------------RMS------------------- 123
Cdd:cd05103    84 ---GGPLMVIVEFCKFGNLSAYLRS--KRSEfvpyktkgarfrqgkdyvgdisvdlkrRLDsitssqssassgfveeksl 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  124 --------------------EPLIAYILHEAlMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL-TSTRHRR 182
Cdd:cd05103   159 sdveeeeagqedlykdfltlEDLICYSFQVA-KGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIyKDPDYVR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  183 NTSVGTPF-WMAPEVIaceqqLDTTYDARCDTWSLGITAIELGD-GDPPLADLHpMRALFKIPRNPPPKLRQPELWSAEF 260
Cdd:cd05103   238 KGDARLPLkWMAPETI-----FDRVYTIQSDVWSFGVLLWEIFSlGASPYPGVK-IDEEFCRRLKEGTRMRAPDYTTPEM 311
                         330       340
                  ....*....|....*....|....
gi 767960106  261 NDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd05103   312 YQTMLDCWHGEPSQRPTFSELVEH 335
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
21-287 3.55e-15

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 79.41  E-value: 3.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVRFYGIYFKKDKVNGDKLWLVL 100
Cdd:cd14224    67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRFHRQAAEEIRILEHLKKQDKDNTMNVIHMLESFTFRNHICMTF 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCSGgSVTDLVK-----GFlkrgermSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEG--GVKLVDFGVSA 173
Cdd:cd14224   147 ELLSM-NLYELIKknkfqGF-------SLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGrsGIKVIDFGSSC 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  174 qltsTRHRR-NTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDP--PLAD----LHPMRALFKIP--- 243
Cdd:cd14224   219 ----YEHQRiYTYIQSRFYRAPEVI-----LGARYGMPIDMWSFGCILAELLTGYPlfPGEDegdqLACMIELLGMPpqk 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  244 ------------------------------------RNPPPKLRQP---ELWSAE--------FNDFISKCLTKDYEKRP 276
Cdd:cd14224   290 lletskraknfisskgypryctvttlpdgsvvlnggRSRRGKMRGPpgsKDWVTAlkgcddplFLDFLKRCLEWDPAARM 369
                         330
                  ....*....|.
gi 767960106  277 TVSELLQHKFI 287
Cdd:cd14224   370 TPSQALRHPWL 380
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
18-284 3.81e-15

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 77.25  E-value: 3.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   18 SDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALsDHPNVVRFYGIYFKKDKVngdklW 97
Cdd:cd14108     1 TDYYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSARRELALLAEL-DHKSIVRFHDAFEKRRVV-----I 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSggsvTDLVKGFLKRgERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG--VKLVDFGVSAQL 175
Cdd:cd14108    75 IVTELCH----EELLERITKR-PTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTdqVRICDFGNAQEL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  176 TSTRHRRnTSVGTPFWMAPEVIACEQQLDTTydarcDTWSLGITAIELGDGDPPLADLHPMRALFKIpRNPPPKLRQPEL 255
Cdd:cd14108   150 TPNEPQY-CKYGTPEFVAPEIVNQSPVSKVT-----DIWPVGVIAYLCLTGISPFVGENDRTTLMNI-RNYNVAFEESMF 222
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767960106  256 --WSAEFNDFISKCLTKDyEKRPTVSELLQH 284
Cdd:cd14108   223 kdLCREAKGFIIKVLVSD-RLRPDAEETLEH 252
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
27-229 3.97e-15

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 77.54  E-value: 3.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKvLNKKNGQKAAVKILDPIHDIDEE--IEAEyniLKALSD--HPNVVRFYGIYFKKDkVNgdklWLVLEL 102
Cdd:cd14664     1 IGRGGAGTVYK-GVMPNGTLVAVKRLKGEGTQGGDhgFQAE---IQTLGMirHRNIVRLRGYCSNPT-TN----LLVYEY 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  103 CSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNN---KTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTR 179
Cdd:cd14664    72 MPNGSLGELLHSRPESQPPLDWETRQRIALGSARGLAYLHHDcspLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKD 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767960106  180 HRRNTSV-GTPFWMAPEVIACEQQldttyDARCDTWSLGITAIELGDGDPP 229
Cdd:cd14664   152 SHVMSSVaGSYGYIAPEYAYTGKV-----SEKSDVYSYGVVLLELITGKRP 197
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
20-293 4.36e-15

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 77.76  E-value: 4.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   20 TWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEA----EYNILKALSDHPNVVRFYGIYFKkdkvngDK 95
Cdd:cd05630     1 TFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAmalnEKQILEKVNSRFVVSLAYAYETK------DA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSGGsvtDLVKGFLKRGER-MSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:cd05630    75 LCLVLTLMNGG---DLKFHIYHMGQAgFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVH 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LTSTRHRRNtSVGTPFWMAPEVIACEQqldttYDARCDTWSLGITAIELGDGDPPLADLHPmralfKIPRNPPPKLRQ-- 252
Cdd:cd05630   152 VPEGQTIKG-RVGTVGYMAPEVVKNER-----YTFSPDWWALGCLLYEMIAGQSPFQQRKK-----KIKREEVERLVKev 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 767960106  253 PELWSAEFN-DFISKC---LTKDYEKR-----PTVSELLQHKFITQIEGK 293
Cdd:cd05630   221 PEEYSEKFSpQARSLCsmlLCKDPAERlgcrgGGAREVKEHPLFKKLNFK 270
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
22-283 4.88e-15

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 77.12  E-value: 4.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   22 EITeTIGKGTYGKVFKVLNKKNG-----QKAAVKILD--PIHDIDEEIEAEYNILKALSdHPNVVRFYGIYFKKDKvngd 94
Cdd:cd05046     9 EIT-TLGRGEFGEVFLAKAKGIEeeggeTLVLVKALQktKDENLQSEFRRELDMFRKLS-HKNVVRLLGLCREAEP---- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 kLWLVLELCSGGsvtDLvKGFLKRGERMSEPL---------IAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVK 165
Cdd:cd05046    83 -HYMILEYTDLG---DL-KQFLRATKSKDEKLkppplstkqKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  166 LVDFGVSAQLTSTR--HRRNTSVgtPF-WMAPEVIaceqqLDTTYDARCDTWSLGITAIEL-GDGDPPLADLHPMRALFK 241
Cdd:cd05046   158 VSLLSLSKDVYNSEyyKLRNALI--PLrWLAPEAV-----QEDDFSTKSDVWSFGVLMWEVfTQGELPFYGLSDEEVLNR 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767960106  242 IpRNPPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd05046   231 L-QAGKLELPVPEGCPSRLYKLMTRCWAVNPKDRPSFSELVS 271
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
17-283 5.50e-15

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 77.75  E-value: 5.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   17 PSDTWEITETIGKGTYGKVFKV----LNKKNGQKA---AVKIL-DPIHDID-EEIEAEYNILKALSDHPNVVRFYGIYfk 87
Cdd:cd05101    22 PRDKLTLGKPLGEGCFGQVVMAeavgIDKDKPKEAvtvAVKMLkDDATEKDlSDLVSEMEMMKMIGKHKNIINLLGAC-- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   88 kdkVNGDKLWLVLELCSGGSVTDLVKGFLKRG------------ERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNN 155
Cdd:cd05101   100 ---TQDGPLYVIVEYASKGNLREYLRARRPPGmeysydinrvpeEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARN 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  156 ILLTTEGGVKLVDFGVSAQLTSTRHRRNTSVGT-PF-WMAPEVIaceqqLDTTYDARCDTWSLGITAIELGD-GDPPLAD 232
Cdd:cd05101   177 VLVTENNVMKIADFGLARDINNIDYYKKTTNGRlPVkWMAPEAL-----FDRVYTHQSDVWSFGVLMWEIFTlGGSPYPG 251
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767960106  233 LhPMRALFKIPRNpPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd05101   252 I-PVEELFKLLKE-GHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVE 300
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
12-283 6.00e-15

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 77.03  E-value: 6.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   12 DNFPDPSDTWEITETIGKGTYGKVFKvlNKKNGQ-KAAVKILDPIHDIDEEIEAEYNILKALSdHPNVVRFYGIyfkkdk 90
Cdd:cd05070     2 DVWEIPRESLQLIKRLGNGQFGEVWM--GTWNGNtKVAIKTLKPGTMSPESFLEEAQIMKKLK-HDKLVQLYAV------ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   91 VNGDKLWLVLELCSGGSVTDlvkgFLKRGE--RMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVD 168
Cdd:cd05070    73 VSEEPIYIVTEYMSKGSLLD----FLKDGEgrALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIAD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  169 FGVSAQLTSTRHRRNTSVGTPF-WMAPEViaceqQLDTTYDARCDTWSLGITAIEL-GDGDPPLADLHPMRALFKIPRNp 246
Cdd:cd05070   149 FGLARLIEDNEYTARQGAKFPIkWTAPEA-----ALYGRFTIKSDVWSFGILLTELvTKGRVPYPGMNNREVLEQVERG- 222
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767960106  247 pPKLRQPELWSAEFNDFISKCLTKDYEKRPTVsELLQ 283
Cdd:cd05070   223 -YRMPCPQDCPISLHELMIHCWKKDPEERPTF-EYLQ 257
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
20-287 6.89e-15

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 77.61  E-value: 6.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   20 TWEITE------TIGKGTYGKVFKVLNKKNGQKAAVK-ILDPIHD--IDEEIEAEYNILKALSdHPNVVRFYGIYFKKdk 90
Cdd:cd07856     5 VFEITTrysdlqPVGMGAFGLVCSARDQLTGQNVAVKkIMKPFSTpvLAKRTYRELKLLKHLR-HENIISLSDIFISP-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   91 vnGDKLWLVLELCSggsvTDLVKgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFG 170
Cdd:cd07856    82 --LEDIYFVTELLG----TDLHR--LLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  171 VS----AQLTSTrhrrntsVGTPFWMAPEVIACEQQldttYDARCDTWSLGITAIELGDGDP--PLAD-LHPMRALFKIP 243
Cdd:cd07856   154 LAriqdPQMTGY-------VSTRYYRAPEIMLTWQK----YDVEVDIWSAGCIFAEMLEGKPlfPGKDhVNQFSIITELL 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  244 RNPP-------------------PKlRQPELWSAEFN-------DFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd07856   223 GTPPddvinticsentlrfvqslPK-RERVPFSEKFKnadpdaiDLLEKMLVFDPKKRISAAEALAHPYL 291
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
12-283 8.07e-15

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 76.60  E-value: 8.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   12 DNFPDPSDTWEITETIGKGTYGKVFKVLNKKNgQKAAVKILDPIHDIDEEIEAEYNILKALSdHPNVVRFYGIyfkkdkV 91
Cdd:cd05073     4 DAWEIPRESLKLEKKLGAGQFGEVWMATYNKH-TKVAVKTMKPGSMSVEAFLAEANVMKTLQ-HDKLVKLHAV------V 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   92 NGDKLWLVLELCSGGSVTDLVKGflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGV 171
Cdd:cd05073    76 TKEPIYIITEFMAKGSLLDFLKS--DEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  172 SAQLTSTRHRRNTSVGTPF-WMAPEVIACeqqldTTYDARCDTWSLGITAIELGDGD----PPLADLHPMRAL---FKIP 243
Cdd:cd05073   154 ARVIEDNEYTAREGAKFPIkWTAPEAINF-----GSFTIKSDVWSFGILLMEIVTYGripyPGMSNPEVIRALergYRMP 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 767960106  244 RNpppklrqpELWSAEFNDFISKCLTKDYEKRPTVsELLQ 283
Cdd:cd05073   229 RP--------ENCPEELYNIMMRCWKNRPEERPTF-EYIQ 259
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
27-281 8.16e-15

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 76.86  E-value: 8.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKV----FKVLNKKNGQKAAVKILDpiHDIDEEI---EAEYNILKALSdHPNVVRFYGIYFKKDKvngDKLWLV 99
Cdd:cd05081    12 LGKGNFGSVelcrYDPLGDNTGALVAVKQLQ--HSGPDQQrdfQREIQILKALH-SDFIVKYRGVSYGPGR---RSLRLV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  100 LELCSGGSVTDlvkgFLKRGERMSEP--LIAYIlHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 177
Cdd:cd05081    86 MEYLPSGCLRD----FLQRHRARLDAsrLLLYS-SQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  178 TRHR---RNTSVGTPFWMAPEVIAceqqlDTTYDARCDTWSLGITAIEL-----GDGDPPLADLHPMRalfkiPRNPPP- 248
Cdd:cd05081   161 DKDYyvvREPGQSPIFWYAPESLS-----DNIFSRQSDVWSFGVVLYELftycdKSCSPSAEFLRMMG-----CERDVPa 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 767960106  249 ------------KLRQPELWSAEFNDFISKCLTKDYEKRPTVSEL 281
Cdd:cd05081   231 lcrllelleegqRLPAPPACPAEVHELMKLCWAPSPQDRPSFSAL 275
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
25-279 9.25e-15

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 76.65  E-value: 9.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKV-LNKKNGQK---AAVKILdPIHD-----IDEEIEAEYNIlkalsDHPNVVRFYGIyfKKDKVNGDK 95
Cdd:cd14055     1 KLVGKGRFAEVWKAkLKQNASGQyetVAVKIF-PYEEyaswkNEKDIFTDASL-----KHENILQFLTA--EERGVGLDR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 -LWLVLELCSGGSVTD-LVKGFLKRGE--RMSEPLIAyilhealmGLQHLHNNKT---------IHRDVKGNNILLTTEG 162
Cdd:cd14055    73 qYWLITAYHENGSLQDyLTRHILSWEDlcKMAGSLAR--------GLAHLHSDRTpcgrpkipiAHRDLKSSNILVKNDG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  163 GVKLVDFGVSAQL---TSTRHRRNT-SVGTPFWMAPEVIACEQQL-DTTYDARCDTWSLGITAIEL----------GDGD 227
Cdd:cd14055   145 TCVLADFGLALRLdpsLSVDELANSgQVGTARYMAPEALESRVNLeDLESFKQIDVYSMALVLWEMasrceasgevKPYE 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767960106  228 PPLADL---HP----MRALFKIPRNPPPKlrqPELW-----SAEFNDFISKCLTKDYEKRPTVS 279
Cdd:cd14055   225 LPFGSKvreRPcvesMKDLVLRDRGRPEI---PDSWlthqgMCVLCDTITECWDHDPEARLTAS 285
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
37-283 9.40e-15

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 76.67  E-value: 9.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   37 KVLNKKNGQKAAVkildpihDIDEEIEAEYNILKALSdHPNVVRFYGIyfkkDKVNGDKLWLVLELCsGGSVTDLVKgfl 116
Cdd:cd14001    34 KKINSKCDKGQRS-------LYQERLKEEAKILKSLN-HPNIVGFRAF----TKSEDGSLCLAMEYG-GKSLNDLIE--- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  117 KRGERMSEPL-IAYILHEALM---GLQHLHNNKTI-HRDVKGNNILLTTE-GGVKLVDFGVSAQLTST----RHRRNTSV 186
Cdd:cd14001    98 ERYEAGLGPFpAATILKVALSiarALEYLHNEKKIlHGDIKSGNVLIKGDfESVKLCDFGVSLPLTENlevdSDPKAQYV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  187 GTPFWMAPEVIacEQQLDTTYDArcDTWSLGITAIELGDGDPPLADLHPM---------------RALFKIPRNPPPKLR 251
Cdd:cd14001   178 GTEPWKAKEAL--EEGGVITDKA--DIFAYGLVLWEMMTLSVPHLNLLDIedddedesfdedeedEEAYYGTLGTRPALN 253
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767960106  252 QPELwSAEFNDFI---SKCLTKDYEKRPTVSELLQ 283
Cdd:cd14001   254 LGEL-DDSYQKVIelfYACTQEDPKDRPSAAHIVE 287
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
25-291 9.98e-15

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 78.16  E-value: 9.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVfkVLNKKNGQKA--AVKILDP----IHDIDEEIEAEYNILkALSDHPNVVRFYgiYFKKDKvngDKLWL 98
Cdd:cd05625     7 KTLGIGAFGEV--CLARKVDTKAlyATKTLRKkdvlLRNQVAHVKAERDIL-AEADNEWVVRLY--YSFQDK---DNLYF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   99 VLELCSGGSVTDLvkgfLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGV------- 171
Cdd:cd05625    79 VMDYIPGGDMMSL----LIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwt 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  172 --SAQLTSTRHRRNTS--------------------------------------VGTPFWMAPEVIaceqqLDTTYDARC 211
Cdd:cd05625   155 hdSKYYQSGDHLRQDSmdfsnewgdpencrcgdrlkplerraarqhqrclahslVGTPNYIAPEVL-----LRTGYTQLC 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  212 DTWSLGITAIELGDGDPPLADLHPMRALFKIPR-----NPPPKLRqpelWSAEFNDFISKCL--TKDYEKRPTVSELLQH 284
Cdd:cd05625   230 DWWSVGVILFEMLVGQPPFLAQTPLETQMKVINwqtslHIPPQAK----LSPEASDLIIKLCrgPEDRLGKNGADEIKAH 305

                  ....*..
gi 767960106  285 KFITQIE 291
Cdd:cd05625   306 PFFKTID 312
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
17-283 1.01e-14

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 76.97  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   17 PSDTWEITETIGKGTYGKVFKV----LNKKNGQ---KAAVKIL--DPIHDIDEEIEAEYNILKALSDHPNVVRFYGIYfk 87
Cdd:cd05098    11 PRDRLVLGKPLGEGCFGQVVLAeaigLDKDKPNrvtKVAVKMLksDATEKDLSDLISEMEMMKMIGKHKNIINLLGAC-- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   88 kdkVNGDKLWLVLELCSGGSVTDLVKGFLKRG------------ERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNN 155
Cdd:cd05098    89 ---TQDGPLYVIVEYASKGNLREYLQARRPPGmeycynpshnpeEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  156 ILLTTEGGVKLVDFGVSAQLTSTRHRRNTSVGT-PF-WMAPEVIaceqqLDTTYDARCDTWSLGITAIELGD-GDPPLAD 232
Cdd:cd05098   166 VLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRlPVkWMAPEAL-----FDRIYTHQSDVWSFGVLLWEIFTlGGSPYPG 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767960106  233 LhPMRALFKIPRNpPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd05098   241 V-PVEELFKLLKE-GHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVE 289
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
21-283 1.36e-14

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 76.97  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEIT-------ETIGKGTYGKV-----FKVLNKKNGQKAAVKILDPIHDIDE--EIEAEYNILKALSDHPNVVRFYGIYF 86
Cdd:cd14207     2 WEFArerlklgKSLGRGAFGKVvqasaFGIKKSPTCRVVAVKMLKEGATASEykALMTELKILIHIGHHLNVVNLLGACT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   87 KkdkvNGDKLWLVLELCSGGSVTDLVK----------------------------------------------------- 113
Cdd:cd14207    82 K----SGGPLMVIVEYCKYGNLSNYLKskrdffvtnkdtslqeelikekkeaeptggkkkrlesvtssesfassgfqedk 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  114 -------------GFLKRGERMsEPLIAYILHEAlMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL-TSTR 179
Cdd:cd14207   158 slsdveeeeedsgDFYKRPLTM-EDLISYSFQVA-RGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIyKNPD 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  180 HRRNTSVGTPF-WMAPEVIaceqqLDTTYDARCDTWSLGITAIELGD-GDPPLADLHPMRALFKIPRNpPPKLRQPELWS 257
Cdd:cd14207   236 YVRKGDARLPLkWMAPESI-----FDKIYSTKSDVWSYGVLLWEIFSlGASPYPGVQIDEDFCSKLKE-GIRMRAPEFAT 309
                         330       340
                  ....*....|....*....|....*.
gi 767960106  258 AEFNDFISKCLTKDYEKRPTVSELLQ 283
Cdd:cd14207   310 SEIYQIMLDCWQGDPNERPRFSELVE 335
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
26-281 1.42e-14

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 76.15  E-value: 1.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   26 TIGKGTYGKV-----FKVLNKKNGQKAAVKILDPIHDIDE--EIEAEYNILKALSdHPNVVRFYGIYfkkdkVNGDKLWL 98
Cdd:cd05045     7 TLGEGEFGKVvkataFRLKGRAGYTTVAVKMLKENASSSElrDLLSEFNLLKQVN-HPHVIKLYGAC-----SQDGPLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   99 VLELCSGGSVTDLVK--------GFLKRGERMSEPLIAYILHEALM------------GLQHLHNNKTIHRDVKGNNILL 158
Cdd:cd05045    81 IVEYAKYGSLRSFLResrkvgpsYLGSDGNRNSSYLDNPDERALTMgdlisfawqisrGMQYLAEMKLVHRDLAARNVLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  159 TTEGGVKLVDFGVSAQLTSTRHRRNTSVG-TPF-WMAPEVIAceqqlDTTYDARCDTWSLGITAIELGD-GDPPLADLHP 235
Cdd:cd05045   161 AEGRKMKISDFGLSRDVYEEDSYVKRSKGrIPVkWMAIESLF-----DHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIAP 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767960106  236 MRaLFKIPRNpPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSEL 281
Cdd:cd05045   236 ER-LFNLLKT-GYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADI 279
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
21-287 1.43e-14

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 76.67  E-value: 1.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   21 WEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEA-----EYNILKALSDHPNVVRFYGIyfkkDKVNGDK 95
Cdd:cd07857     2 YELIKELGQGAYGIVCSARNAETSEEETVAIKKITNVFSKKILAkralrELKLLRHFRGHKNITCLYDM----DIVFPGN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 ---LWLVLELCSggsvTDLVKgFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVs 172
Cdd:cd07857    78 fneLYLYEELME----ADLHQ-IIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGL- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLTSTRHRRNTS-----VGTPFWMAPEVIACEQQldttYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKI----- 242
Cdd:cd07857   152 ARGFSENPGENAGfmteyVATRWYRAPEIMLSFQS----YTKAIDVWSVGCILAELLGRKPVFKGKDYVDQLNQIlqvlg 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767960106  243 -P-----------------RNPPPKLRQPELW-----SAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd07857   228 tPdeetlsrigspkaqnyiRSLPNIPKKPFESifpnaNPLALDLLEKLLAFDPTKRISVEEALEHPYL 295
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
19-277 1.55e-14

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 75.88  E-value: 1.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITET-------IGKGTYGKVFkvLNKKNGQ-KAAVKILDPIHDIDEEIEAEYNILKALSdHPNVVRFYGIyfkkdk 90
Cdd:cd05069     5 DAWEIPREslrldvkLGQGCFGEVW--MGTWNGTtKVAIKTLKPGTMMPEAFLQEAQIMKKLR-HDKLVPLYAV------ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   91 VNGDKLWLVLELCSGGSVTDlvkgFLKRGE--RMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVD 168
Cdd:cd05069    76 VSEEPIYIVTEFMGKGSLLD----FLKEGDgkYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIAD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  169 FGVSAQLTSTRHRRNTSVGTPF-WMAPEViaceqQLDTTYDARCDTWSLGITAIEL-GDGDPPLADLHPMRALFKIPRNp 246
Cdd:cd05069   152 FGLARLIEDNEYTARQGAKFPIkWTAPEA-----ALYGRFTIKSDVWSFGILLTELvTKGRVPYPGMVNREVLEQVERG- 225
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767960106  247 pPKLRQPELWSAEFNDFISKCLTKDYEKRPT 277
Cdd:cd05069   226 -YRMPCPQGCPESLHELMKLCWKKDPDERPT 255
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
19-228 1.82e-14

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 75.82  E-value: 1.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEA--EYNILKALSdHPNVVRFYgiyfkkDKVNGDK- 95
Cdd:cd07871     5 ETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAirEVSLLKNLK-HANIVTLH------DIIHTERc 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   96 LWLVLELCSggsvTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS-AQ 174
Cdd:cd07871    78 LTLVFEYLD----SDLKQYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLArAK 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767960106  175 LTSTRHRRNTSVgTPFWMAPEVIACEqqldTTYDARCDTWSLGITAIELGDGDP 228
Cdd:cd07871   154 SVPTKTYSNEVV-TLWYRPPDVLLGS----TEYSTPIDMWGVGCILYEMATGRP 202
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
17-283 1.83e-14

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 76.56  E-value: 1.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   17 PSDTWEITETIGKGTYGKVFKV----LNKKNG-QKAAVKILDPIHDIDEE--IEAEYNILKALSDHPNVVRFYGIYFKKd 89
Cdd:cd05102     5 PRDRLRLGKVLGHGAFGKVVEAsafgIDKSSScETVAVKMLKEGATASEHkaLMSELKILIHIGNHLNVVNLLGACTKP- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   90 kvNGdKLWLVLELCSGGSVTDLVK----GFLKRGERMS------------------------------------------ 123
Cdd:cd05102    84 --NG-PLMVIVEFCKYGNLSNFLRakreGFSPYRERSPrtrsqvrsmveavradrrsrqgsdrvasftestsstnqprqe 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  124 -----------EPLIAYILHEAlMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL-TSTRHRRNTSVGTPF- 190
Cdd:cd05102   161 vddlwqspltmEDLICYSFQVA-RGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIyKDPDYVRKGSARLPLk 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  191 WMAPEVIaceqqLDTTYDARCDTWSLGITAIELGD-GDPPLADLHPMRALFKIPRNpPPKLRQPELWSAEFNDFISKCLT 269
Cdd:cd05102   240 WMAPESI-----FDKVYTTQSDVWSFGVLLWEIFSlGASPYPGVQINEEFCQRLKD-GTRMRAPEYATPEIYRIMLSCWH 313
                         330
                  ....*....|....
gi 767960106  270 KDYEKRPTVSELLQ 283
Cdd:cd05102   314 GDPKERPTFSDLVE 327
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
17-287 2.04e-14

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 75.26  E-value: 2.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   17 PSDTWEITETIGKGTYGKVFKVLNKKN--GQKAAVKILdPIHDIDEEIEAEYNILKALSdHPNVVRFYGIYFKKDKvngd 94
Cdd:cd14112     1 PTGRFSFGSEIFRGRFSVIVKAVDSTTetDAHCAVKIF-EVSDEASEAVREFESLRTLQ-HENVQRLIAAFKPSNF---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 kLWLVLELCSggsvTDLVKGFLKRGErMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGG--VKLVDFGvS 172
Cdd:cd14112    75 -AYLVMEKLQ----EDVFTRFSSNDY-YSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSwqVKLVDFG-R 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLTStrhrRNTSVGTPFWM---APEVIACEQQLdttyDARCDTWSLGITAIELgdgdppLADLHPMRALF----KIPRN 245
Cdd:cd14112   148 AQKVS----KLGKVPVDGDTdwaSPEFHNPETPI----TVQSDIWGLGVLTFCL------LSGFHPFTSEYddeeETKEN 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767960106  246 PPPKLRQPELW----SAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14112   214 VIFVKCRPNLIfveaTQEALRFATWALKKSPTRRMRTDEALEHRWL 259
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
19-283 2.40e-14

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 75.11  E-value: 2.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITE-------TIGKGTYGKVFKvlNKKNGQ-KAAVKILDPIHDIDEEIEAEYNILKALSdHPNVVRFYGIyfkkdk 90
Cdd:cd05071     2 DAWEIPReslrlevKLGQGCFGEVWM--GTWNGTtRVAIKTLKPGTMSPEAFLQEAQVMKKLR-HEKLVQLYAV------ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   91 VNGDKLWLVLELCSGGSVTDLVKGflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFG 170
Cdd:cd05071    73 VSEEPIYIVTEYMSKGSLLDFLKG--EMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  171 VSAQLTSTRHRRNTSVGTPF-WMAPEViaceqQLDTTYDARCDTWSLGITAIELG-DGDPPLADLHPMRALFKIPRNppP 248
Cdd:cd05071   151 LARLIEDNEYTARQGAKFPIkWTAPEA-----ALYGRFTIKSDVWSFGILLTELTtKGRVPYPGMVNREVLDQVERG--Y 223
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767960106  249 KLRQPELWSAEFNDFISKCLTKDYEKRPTVsELLQ 283
Cdd:cd05071   224 RMPCPPECPESLHDLMCQCWRKEPEERPTF-EYLQ 257
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
16-282 3.10e-14

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 74.53  E-value: 3.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   16 DPSDTWEITEtIGKGTYGKVfkVLNKKNGQ-KAAVKILDPIHDIDEEIEAEYNILKALSdHPNVVRFYGIYFKKDKVngd 94
Cdd:cd05113     2 DPKDLTFLKE-LGTGQFGVV--KYGKWRGQyDVAIKMIKEGSMSEDEFIEEAKVMMNLS-HEKLVQLYGVCTKQRPI--- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 klWLVLELCSGGSVTDLVKGFLKRGErMSEPLiaYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 174
Cdd:cd05113    75 --FIITEYMANGCLLNYLREMRKRFQ-TQQLL--EMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRY 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  175 LTSTRHrrNTSVGTPF---WMAPEVIaceqqLDTTYDARCDTWSLGITAIELGD-GDPPLADLHPMRALFKIPRNppPKL 250
Cdd:cd05113   150 VLDDEY--TSSVGSKFpvrWSPPEVL-----MYSKFSSKSDVWAFGVLMWEVYSlGKMPYERFTNSETVEHVSQG--LRL 220
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767960106  251 RQPELWSAEFNDFISKCLTKDYEKRPTVSELL 282
Cdd:cd05113   221 YRPHLASEKVYTIMYSCWHEKADERPTFKILL 252
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
25-281 3.16e-14

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 74.88  E-value: 3.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKV-LNKKNGQ--KAAVKILDPIHDIDEEIE---AEYNILKALsDHPNVVRFYGIYFKKDKVNG-DKLW 97
Cdd:cd05035     5 KILGEGEFGSVMEAqLKQDDGSqlKVAVKTMKVDIHTYSEIEeflSEAACMKDF-DHPNVMRLIGVCFTASDLNKpPSPM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGSVTDLVkgFLKRGERMSE-----PLIAYILHEALmGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVS 172
Cdd:cd05035    84 VILPFMKHGDLHSYL--LYSRLGGLPEklplqTLLKFMVDIAK-GMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  173 AQLTSTRHRRNTSVGT-PF-WMAPEVIAceqqlDTTYDARCDTWSLGITAIELGD-GDPPLADL--HPMralFKIPRNpP 247
Cdd:cd05035   161 RKIYSGDYYRQGRISKmPVkWIALESLA-----DNVYTSKSDVWSFGVTMWEIATrGQTPYPGVenHEI---YDYLRN-G 231
                         250       260       270
                  ....*....|....*....|....*....|....
gi 767960106  248 PKLRQPELWSAEFNDFISKCLTKDYEKRPTVSEL 281
Cdd:cd05035   232 NRLKQPEDCLDEVYFLMYFCWTVDPKDRPTFTKL 265
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
25-281 3.67e-14

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 74.14  E-value: 3.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   25 ETIGKGTYGKVFKvlNKKNGQKAAVKILDPihDIDEEIEAEYNILKALSDHPNVVRFYGIYFKkdkvNGdkLWLVLELCS 104
Cdd:cd05083    12 EIIGEGEFGAVLQ--GEYMGQKVAVKNIKC--DVTAQAFLEETAVMTKLQHKNLVRLLGVILH----NG--LYIVMELMS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  105 GGsvtDLVKGFLKRGERMSEP--LIAYILHEAlMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGvsaqLTSTRHRR 182
Cdd:cd05083    82 KG---NLVNFLRSRGRALVPViqLLQFSLDVA-EGMEYLESKKLVHRDLAARNILVSEDGVAKISDFG----LAKVGSMG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  183 NTSVGTPF-WMAPEVIAceqqlDTTYDARCDTWSLGITAIEL---GDGDPPLADLHPMR-ALFKIPRNPPPKLRQPELWS 257
Cdd:cd05083   154 VDNSRLPVkWTAPEALK-----NKKFSSKSDVWSYGVLLWEVfsyGRAPYPKMSVKEVKeAVEKGYRMEPPEGCPPDVYS 228
                         250       260
                  ....*....|....*....|....
gi 767960106  258 aefndFISKCLTKDYEKRPTVSEL 281
Cdd:cd05083   229 -----IMTSCWEAEPGKRPSFKKL 247
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
27-283 3.88e-14

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 74.18  E-value: 3.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFkvLNKKNGQ-KAAVKILDPIHDIDEEIEAEYNILKALSdHPNVVRFYGIyfkkdkVNGDKLWLVLELCSG 105
Cdd:cd14203     3 LGQGCFGEVW--MGTWNGTtKVAIKTLKPGTMSPEAFLEEAQIMKKLR-HDKLVQLYAV------VSEEPIYIVTEFMSK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  106 GSVTDLVKGflKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRRNTS 185
Cdd:cd14203    74 GSLLDFLKD--GEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  186 VGTPF-WMAPEViaceqQLDTTYDARCDTWSLGITAIEL-GDGDPPLADLHPMRALFKIPRNppPKLRQPELWSAEFNDF 263
Cdd:cd14203   152 AKFPIkWTAPEA-----ALYGRFTIKSDVWSFGILLTELvTKGRVPYPGMNNREVLEQVERG--YRMPCPPGCPESLHEL 224
                         250       260
                  ....*....|....*....|
gi 767960106  264 ISKCLTKDYEKRPTVsELLQ 283
Cdd:cd14203   225 MCQCWRKDPEERPTF-EYLQ 243
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
23-236 4.13e-14

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 74.78  E-value: 4.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   23 ITETIGKGTYGKVFKvlNKKNGQKAAVKILDpihDIDEEI---EAE-YNILkaLSDHPNVVRFYG--IYFKKDKVngdKL 96
Cdd:cd14142     9 LVECIGKGRYGEVWR--GQWQGESVAVKIFS---SRDEKSwfrETEiYNTV--LLRHENILGFIAsdMTSRNSCT---QL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   97 WLVLELCSGGSVTDlvkgFLKRGErMSEPLIAYILHEALMGLQHLHNNKT--------IHRDVKGNNILLTTEGGVKLVD 168
Cdd:cd14142    79 WLITHYHENGSLYD----YLQRTT-LDHQEMLRLALSAASGLVHLHTEIFgtqgkpaiAHRDLKSKNILVKSNGQCCIAD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  169 FGVSAQLTSTRHR----RNTSVGTPFWMAPEVIacEQQLDTT-YDA--RCDTWSLGITAIELG----------DGDPPLA 231
Cdd:cd14142   154 LGLAVTHSQETNQldvgNNPRVGTKRYMAPEVL--DETINTDcFESykRVDIYAFGLVLWEVArrcvsggiveEYKPPFY 231

                  ....*
gi 767960106  232 DLHPM 236
Cdd:cd14142   232 DVVPS 236
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
27-237 7.97e-14

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 73.84  E-value: 7.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   27 IGKGTYGKVFKVLNKKNGQKAAVKI----LDPIHDidEEIEAEYNILKALSdHPNVVRFYGIYFKKDKVNGDKL-WLVLE 101
Cdd:cd14038     2 LGTGGFGNVLRWINQETGEQVAIKQcrqeLSPKNR--ERWCLEIQIMKRLN-HPNVVAARDVPEGLQKLAPNDLpLLAME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  102 LCSGGsvtDLVKgFLKRGER---MSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLtTEGGVKLV----DFGVSAQ 174
Cdd:cd14038    79 YCQGG---DLRK-YLNQFENccgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVL-QQGEQRLIhkiiDLGYAKE 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  175 LTSTrhRRNTS-VGTPFWMAPEVIacEQQldtTYDARCDTWSLGITAIELGDG-DPPLADLHPMR 237
Cdd:cd14038   154 LDQG--SLCTSfVGTLQYLAPELL--EQQ---KYTVTVDYWSFGTLAFECITGfRPFLPNWQPVQ 211
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
23-284 8.05e-14

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 73.82  E-value: 8.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   23 ITETIGKGTYGKVFK-VLNKKNG--QKAAVKILDPIHDIDEEIEAEYNILKALSD--HPNVVRFYGIYFKKDKVNGDKLW 97
Cdd:cd14204    11 LGKVLGEGEFGSVMEgELQQPDGtnHKVAVKTMKLDNFSQREIEEFLSEAACMKDfnHPNVIRLLGVCLEVGSQRIPKPM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   98 LVLELCSGGsvtDLvKGFLKRGERMSEP-------LIAYILHEALmGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFG 170
Cdd:cd14204    91 VILPFMKYG---DL-HSFLLRSRLGSGPqhvplqtLLKFMIDIAL-GMEYLSSRNFLHRDLAARNCMLRDDMTVCVADFG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  171 VSAQLTSTRHRRNTSVGTpfwMAPEVIACEQQLDTTYDARCDTWSLGITAIEL---GDGDPPLADLHPM-RALFKIPRnp 246
Cdd:cd14204   166 LSKKIYSGDYYRQGRIAK---MPVKWIAVESLADRVYTVKSDVWAFGVTMWEIatrGMTPYPGVQNHEIyDYLLHGHR-- 240
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767960106  247 ppkLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQH 284
Cdd:cd14204   241 ---LKQPEDCLDELYDIMYSCWRSDPTDRPTFTQLREN 275
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
28-287 9.09e-14

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 74.15  E-value: 9.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   28 GKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSDHP-------NVVRFYGiYFKKDKVNGDKLWLVL 100
Cdd:cd14136    19 GWGHFSTVWLCWDLQNKRFVALKVVKSAQHYTEAALDEIKLLKCVREADpkdpgreHVVQLLD-DFKHTGPNGTHVCMVF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  101 ELCsGGSVTDLVKGFLKRGerMSEPLIAYILHEALMGLQHLHNN-KTIHRDVKGNNILLT-TEGGVKLVDFGVSaqlTST 178
Cdd:cd14136    98 EVL-GPNLLKLIKRYNYRG--IPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLLCiSKIEVKIADLGNA---CWT 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  179 RHRRNTSVGTPFWMAPEVIaceqqLDTTYDARCDTWSLGITAIELGDGDpPLADLHP--------------MRALFKIPR 244
Cdd:cd14136   172 DKHFTEDIQTRQYRSPEVI-----LGAGYGTPADIWSTACMAFELATGD-YLFDPHSgedysrdedhlaliIELLGRIPR 245
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767960106  245 -------------NPPPKLRQ-------------------PELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFI 287
Cdd:cd14136   246 siilsgkysreffNRKGELRHisklkpwpledvlvekykwSKEEAKEFASFLLPMLEYDPEKRATAAQCLQHPWL 320
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
19-292 1.08e-13

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 73.70  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   19 DTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDpIHDIDEEIEA----EYNILKALSdHPNVVRFYgiyfkkDKVNGD 94
Cdd:PLN00009    2 DQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIR-LEQEDEGVPStairEISLLKEMQ-HGNIVRLQ------DVVHSE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106   95 K-LWLVLELCSggsvTDLVKGFLKRGERMSEP-LIAYILHEALMGLQHLHNNKTIHRDVKGNNILLT-TEGGVKLVDFGV 171
Cdd:PLN00009   74 KrLYLVFEYLD----LDLKKHMDSSPDFAKNPrLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDrRTNALKLADFGL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767960106  172 SAQLTSTRHRRNTSVGTPFWMAPEVIACEQqldtTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKI--------- 242
Cdd:PLN00009  150 ARAFGIPVRTFTHEVVTLWYRAPEILLGSR----HYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIfrilgtpne 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767960106  243 ----------------PRNPPPKLRQ--PELWSAEFnDFISKCLTKDYEKRPTVSELLQHKFITQIEG 292
Cdd:PLN00009  226 etwpgvtslpdyksafPKWPPKDLATvvPTLEPAGV-DLLSKMLRLDPSKRITARAALEHEYFKDLGD 292
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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