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Conserved domains on  [gi|167887698|gb|ACA06069|]
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rho-associated protein kinase 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
2-406 0e+00

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: 865.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698    2 STGDSFETRFEKMDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDNFLSRYKDTINKIRDLRMKAEDYEVVKV 81
Cdd:cd05622     1 STGESFETRFEKIDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDNFLSRYKDTINKIRDLRMKAEDYEVVKV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd05622    81 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYI 241
Cdd:cd05622   161 VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  242 SPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLTDRE 321
Cdd:cd05622   241 SPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLTDRE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  322 VRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDDLEEDKGEEETFPIPKAFVGNQLPFVGFTYYS 401
Cdd:cd05622   321 VRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDDLEEDKGEEETFPIPKAFVGNQLPFVGFTYYS 400

                  ....*
gi 167887698  402 NRRYL 406
Cdd:cd05622   401 NRRYL 405
PH_ROCK cd01242
Rho-associated coiled-coil containing protein kinase pleckstrin homology (PH) domain; ROCK is ...
1119-1225 4.10e-57

Rho-associated coiled-coil containing protein kinase pleckstrin homology (PH) domain; ROCK is a serine/threonine kinase that binds GTP-Rho. It consists of a kinase domain, a coiled coil region and a PH domain. The ROCK PH domain is interrupted by a C1 domain. ROCK plays a role in cellular functions, such as contraction, adhesion, migration, and proliferation and in the regulation of apoptosis. There are two ROCK isoforms, ROCK1 and ROCK2. In ROCK2 the Rho Binding Domain (RBD) and the PH domain work together in membrane localization with RBD receiving the RhoA signal and the PH domain receiving the phospholipid signal. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 269948  Cd Length: 110  Bit Score: 192.57  E-value: 4.10e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698 1119 SRIEGWLSVPNRGNIKRYGWKKQYVVVSSKKILFYNDEQDKEQSNPSMVLDIDKLFHVRPVTQGDVYRAETEEIPKIFQI 1198
Cdd:cd01242     1 SRLEGWLSLPNKQNIRRHGWKKQYVVVSSKKILFYNSEQDKANSNPILVLDIDKLFHVRSVTQGDVIRADAKEIPRIFQI 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 167887698 1199 LYANEGECRKDVEMEP---VQQAEKTNFQN 1225
Cdd:cd01242    81 LYANEGESSRPAEVTDtlsVSREEKPNTIL 110
C1_ROCK1 cd20874
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing ...
1222-1290 1.29e-52

protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing protein kinase 1 (ROCK1) and similar proteins; ROCK1 is a serine/threonine kinase, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1, also called Rho-associated protein kinase 1, renal carcinoma antigen NY-REN-35, Rho-associated, coiled-coil-containing protein kinase I (ROCK-I), p160 ROCK-1, or p160ROCK, 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 proteins contain 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), a pleckstrin homology (PH) domain and a C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


:

Pssm-ID: 410424  Cd Length: 69  Bit Score: 178.29  E-value: 1.29e-52
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167887698 1222 NFQNHKGHEFIPTLYHFPANCDACAKPLWHVFKPPPALECRRCHVKCHRDHLDKKEDLICPCKVSYDVT 1290
Cdd:cd20874     1 NFLPHKGHEFIPTLYHFPANCEACAKPLWHVFKPPPALECRRCHVKCHKDHLDKKEDMITPCKVNYDVT 69
HR1_ROCK1 cd11639
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated ...
489-554 1.24e-27

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated coiled-coil containing protein kinase 1; ROCK1 is a serine/threonine kinase and 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. ROCK1 contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a Rho-binding HR1 domain and a pleckstrin homology (PH) domain. It is auto-inhibited by HR1 and PH domains interacting with the catalytic domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


:

Pssm-ID: 212029 [Multi-domain]  Cd Length: 66  Bit Score: 106.63  E-value: 1.24e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167887698  489 MLLQHRINEYQRKAEQENEKRRNVENEVSTLKDQLEDLKKVSQNSQLANEKLSQLQKQLEEANDLL 554
Cdd:cd11639     1 MMLQHRINEYQRKAEQESEKRRNVENEVSTLKDQLEDLKKISQNSQITNEKINQLQKQLEEANDLL 66
ROCK_SBD cd22250
Shroom-binding domain found in Rho-associated coiled-coil containing protein kinase; ...
836-913 9.36e-23

Shroom-binding domain found in Rho-associated coiled-coil containing protein kinase; Rho-associated coiled-coil containing protein kinase (ROCK) is a serine/threonine kinase (STK) that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. It is also referred to as Rho-associated protein kinase or simply as Rho kinase. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Rho-associated protein kinase 1 (ROCK1) is also called renal carcinoma antigen NY-REN-35, Rho-associated, coiled-coil-containing protein kinase 1, ROCK-I, p160 ROCK-1, or p160ROCK, 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 in ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. Rho-associated protein kinase 2 (ROCK2), also called Rho kinase 2, Rho-associated, coiled-coil-containing protein kinase 2, ROCK-II, or p164 ROCK-2, is more prominent in brain and skeletal muscle. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK subfamily proteins contain an N-terminal extension, a catalytic kinase domain, a coiled-coil (CC) 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 proteolytic cleavage, binding of lipids to the PH domain, or binding of GTP-bound RhoA to the CC region. More recently, the Shroom family of proteins have been identified as an additional regulator of ROCK. This model corresponds to the Shroom-binding domain (SBD) of ROCK, which forms a parallel coiled coil with the Shroom domain 2 (SD2) of Shroom.


:

Pssm-ID: 409019 [Multi-domain]  Cd Length: 75  Bit Score: 93.09  E-value: 9.36e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  836 EGQMRELQDQLEAEQYFSTLYKTQVKELKEEIEEKNRENLkkiQELQNEKETLATQLDLAETKAESEQLARGLLEEQY 913
Cdd:cd22250     1 DLQMKELQDQLEAEQYFSTLYKTQVKELKEELEEKTRQIK---QELEDERESLSAQLELALAKADSEQLARSIAEEQI 75
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
518-1090 1.29e-19

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 95.39  E-value: 1.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  518 TLKDQLEDLKKVSQNSQL--ANEKLSQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSISQLESLNRELQERnrilens 595
Cdd:COG1196   217 ELKEELKELEAELLLLKLreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE------- 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  596 ksqtdkdYYQLQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVEGERKEAQDMLNHSEKEKNNLEIDLNy 675
Cdd:COG1196   290 -------EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA- 361
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  676 KLKSLQQRLEQEVNEHKVTKARLTDKHQSIEEAKSVAmcemEKKLKEEREAREKAENRVVQIEKQCSMLDVDLKQSQQKL 755
Cdd:COG1196   362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL----AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  756 EHLTGNKERMEDEVKNLTLQLEQESNKRLLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLEFELA--QLTKQYR 833
Cdd:COG1196   438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEgvKAALLLA 517
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  834 GNEGQMRELQDQLEAEQYFSTLYKTQVKELKEEIEEKNRENLKK-IQELQNEKETLAT--QLDLAETKAESEQLARGLLE 910
Cdd:COG1196   518 GLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAaIEYLKAAKAGRATflPLDKIRARAALAAALARGAI 597
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  911 EQYFELTQESKKAASRNRQEITDKDHTVSRLEEANSMLTKDIEILRRENEELTEKMKKAEEEYKLEKEEEISNLKAAFEK 990
Cdd:COG1196   598 GAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEA 677
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  991 NINTERTLKTQAVNKLAEIMNRKDFKIDRKKANTQDLRKKEKENRKLQLE--LNQEREKFNQMVVKHQKELNDMQAQLVE 1068
Cdd:COG1196   678 EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEeqLEAEREELLEELLEEEELLEEEALEELP 757
                         570       580
                  ....*....|....*....|..
gi 167887698 1069 ECAHRNELQMQLASKESDIEQL 1090
Cdd:COG1196   758 EPPDLEELERELERLEREIEAL 779
 
Name Accession Description Interval E-value
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
2-406 0e+00

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: 865.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698    2 STGDSFETRFEKMDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDNFLSRYKDTINKIRDLRMKAEDYEVVKV 81
Cdd:cd05622     1 STGESFETRFEKIDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDNFLSRYKDTINKIRDLRMKAEDYEVVKV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd05622    81 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYI 241
Cdd:cd05622   161 VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  242 SPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLTDRE 321
Cdd:cd05622   241 SPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLTDRE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  322 VRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDDLEEDKGEEETFPIPKAFVGNQLPFVGFTYYS 401
Cdd:cd05622   321 VRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDDLEEDKGEEETFPIPKAFVGNQLPFVGFTYYS 400

                  ....*
gi 167887698  402 NRRYL 406
Cdd:cd05622   401 NRRYL 405
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
76-338 2.01e-93

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 301.37  E-value: 2.01e-93
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698     76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKrsDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKK--DRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698    156 MPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGmvRCDTA 234
Cdd:smart00220   79 CEGGDLFDLLKKRGrLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGE--KLTTF 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698    235 VGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLIC 314
Cdd:smart00220  157 VGTPEYMAPEVLLGKG----YGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIR 232
                           250       260
                    ....*....|....*....|....*
gi 167887698    315 AFLT-DREVRLgrnGVEEIKRHLFF 338
Cdd:smart00220  233 KLLVkDPEKRL---TAEEALQHPFF 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
72-397 4.74e-71

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 241.26  E-value: 4.74e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   72 KAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYM 151
Cdd:PTZ00263   16 KLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  152 VMEYMPGGDL-VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKegmvR 230
Cdd:PTZ00263   96 LLEFVVGGELfTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPD----R 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  231 CDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnsLTFPddNDISKEAK 310
Cdd:PTZ00263  172 TFTLCGTPEYLAPEVIQSKG----HGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGR--LKFP--NWFDGRAR 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  311 NLICAFL-TDREVRLG--RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDDLEEdKGEEETFPIPKAf 387
Cdd:PTZ00263  244 DLVKGLLqTDHTKRLGtlKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFEKYPD-SPVDRLPPLTAA- 321
                         330
                  ....*....|
gi 167887698  388 vgNQLPFVGF 397
Cdd:PTZ00263  322 --QQAEFAGF 329
PH_ROCK cd01242
Rho-associated coiled-coil containing protein kinase pleckstrin homology (PH) domain; ROCK is ...
1119-1225 4.10e-57

Rho-associated coiled-coil containing protein kinase pleckstrin homology (PH) domain; ROCK is a serine/threonine kinase that binds GTP-Rho. It consists of a kinase domain, a coiled coil region and a PH domain. The ROCK PH domain is interrupted by a C1 domain. ROCK plays a role in cellular functions, such as contraction, adhesion, migration, and proliferation and in the regulation of apoptosis. There are two ROCK isoforms, ROCK1 and ROCK2. In ROCK2 the Rho Binding Domain (RBD) and the PH domain work together in membrane localization with RBD receiving the RhoA signal and the PH domain receiving the phospholipid signal. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269948  Cd Length: 110  Bit Score: 192.57  E-value: 4.10e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698 1119 SRIEGWLSVPNRGNIKRYGWKKQYVVVSSKKILFYNDEQDKEQSNPSMVLDIDKLFHVRPVTQGDVYRAETEEIPKIFQI 1198
Cdd:cd01242     1 SRLEGWLSLPNKQNIRRHGWKKQYVVVSSKKILFYNSEQDKANSNPILVLDIDKLFHVRSVTQGDVIRADAKEIPRIFQI 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 167887698 1199 LYANEGECRKDVEMEP---VQQAEKTNFQN 1225
Cdd:cd01242    81 LYANEGESSRPAEVTDtlsVSREEKPNTIL 110
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
76-293 8.67e-53

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 193.31  E-value: 8.67e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSK-----FEMIKRsdsafFWEERDIMAFANSPWVVQLFYAFQDDRYLY 150
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPelaadPEARER-----FRREARALARLNHPNIVRVYDVGEEDGRPY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMV 229
Cdd:COG0515    84 LVMEYVEGESLADLLRRRGpLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLT 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167887698  230 RCDTAVGTPDYISPEVLKSQGGDGYYgrecDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNH 293
Cdd:COG0515   164 QTGTVVGTPGYMAPEQARGEPVDPRS----DVYSLGVTLYELLTGRPPFDGDSPAELLRAHLRE 223
C1_ROCK1 cd20874
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing ...
1222-1290 1.29e-52

protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing protein kinase 1 (ROCK1) and similar proteins; ROCK1 is a serine/threonine kinase, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1, also called Rho-associated protein kinase 1, renal carcinoma antigen NY-REN-35, Rho-associated, coiled-coil-containing protein kinase I (ROCK-I), p160 ROCK-1, or p160ROCK, 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 proteins contain 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), a pleckstrin homology (PH) domain and a C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410424  Cd Length: 69  Bit Score: 178.29  E-value: 1.29e-52
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167887698 1222 NFQNHKGHEFIPTLYHFPANCDACAKPLWHVFKPPPALECRRCHVKCHRDHLDKKEDLICPCKVSYDVT 1290
Cdd:cd20874     1 NFLPHKGHEFIPTLYHFPANCEACAKPLWHVFKPPPALECRRCHVKCHKDHLDKKEDMITPCKVNYDVT 69
Pkinase pfam00069
Protein kinase domain;
76-338 1.53e-48

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 172.43  E-value: 1.53e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698    76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFfWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNI-LREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   156 MPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMgfihrdvkpdnmlldksghlkladfgtcmkmnkegmvrcDTA 234
Cdd:pfam00069   80 VEGGSLFDLLSEKGAfSEREAKFIMKQILEGLESGSSL---------------------------------------TTF 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   235 VGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNdISKEAKNLIC 314
Cdd:pfam00069  121 VGTPWYMAPEVLGGNP----YGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSN-LSEEAKDLLK 195
                          250       260
                   ....*....|....*....|....*
gi 167887698   315 AFLT-DREVRLgrnGVEEIKRHLFF 338
Cdd:pfam00069  196 KLLKkDPSKRL---TATQALQHPWF 217
HR1_ROCK1 cd11639
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated ...
489-554 1.24e-27

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated coiled-coil containing protein kinase 1; ROCK1 is a serine/threonine kinase and 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. ROCK1 contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a Rho-binding HR1 domain and a pleckstrin homology (PH) domain. It is auto-inhibited by HR1 and PH domains interacting with the catalytic domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212029 [Multi-domain]  Cd Length: 66  Bit Score: 106.63  E-value: 1.24e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167887698  489 MLLQHRINEYQRKAEQENEKRRNVENEVSTLKDQLEDLKKVSQNSQLANEKLSQLQKQLEEANDLL 554
Cdd:cd11639     1 MMLQHRINEYQRKAEQESEKRRNVENEVSTLKDQLEDLKKISQNSQITNEKINQLQKQLEEANDLL 66
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
76-284 7.23e-26

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 114.12  E-value: 7.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVR-HKSTRKVyAMKLLsKFEMikRSDSAF---FweERDIMAFA--NSPWVVQLFYAFQDDRYL 149
Cdd:NF033483    9 YEIGERIGRGGMAEVYLAKdTRLDRDV-AVKVL-RPDL--ARDPEFvarF--RREAQSAAslSHPNIVSVYDVGEDGGIP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 YMVMEYMPGGDLVNLM-SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGM 228
Cdd:NF033483   83 YIVMEYVDGRTLKDYIrEHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARALSSTTM 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167887698  229 VRCDTAVGTPDYISPEvlksQ--GG------DGYygrecdwwSVGVFLYEMLVGDTPFYADSLV 284
Cdd:NF033483  163 TQTNSVLGTVHYLSPE----QarGGtvdarsDIY--------SLGIVLYEMLTGRPPFDGDSPV 214
ROCK_SBD cd22250
Shroom-binding domain found in Rho-associated coiled-coil containing protein kinase; ...
836-913 9.36e-23

Shroom-binding domain found in Rho-associated coiled-coil containing protein kinase; Rho-associated coiled-coil containing protein kinase (ROCK) is a serine/threonine kinase (STK) that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. It is also referred to as Rho-associated protein kinase or simply as Rho kinase. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Rho-associated protein kinase 1 (ROCK1) is also called renal carcinoma antigen NY-REN-35, Rho-associated, coiled-coil-containing protein kinase 1, ROCK-I, p160 ROCK-1, or p160ROCK, 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 in ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. Rho-associated protein kinase 2 (ROCK2), also called Rho kinase 2, Rho-associated, coiled-coil-containing protein kinase 2, ROCK-II, or p164 ROCK-2, is more prominent in brain and skeletal muscle. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK subfamily proteins contain an N-terminal extension, a catalytic kinase domain, a coiled-coil (CC) 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 proteolytic cleavage, binding of lipids to the PH domain, or binding of GTP-bound RhoA to the CC region. More recently, the Shroom family of proteins have been identified as an additional regulator of ROCK. This model corresponds to the Shroom-binding domain (SBD) of ROCK, which forms a parallel coiled coil with the Shroom domain 2 (SD2) of Shroom.


Pssm-ID: 409019 [Multi-domain]  Cd Length: 75  Bit Score: 93.09  E-value: 9.36e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  836 EGQMRELQDQLEAEQYFSTLYKTQVKELKEEIEEKNRENLkkiQELQNEKETLATQLDLAETKAESEQLARGLLEEQY 913
Cdd:cd22250     1 DLQMKELQDQLEAEQYFSTLYKTQVKELKEELEEKTRQIK---QELEDERESLSAQLELALAKADSEQLARSIAEEQI 75
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
518-1090 1.29e-19

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 95.39  E-value: 1.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  518 TLKDQLEDLKKVSQNSQL--ANEKLSQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSISQLESLNRELQERnrilens 595
Cdd:COG1196   217 ELKEELKELEAELLLLKLreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE------- 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  596 ksqtdkdYYQLQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVEGERKEAQDMLNHSEKEKNNLEIDLNy 675
Cdd:COG1196   290 -------EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA- 361
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  676 KLKSLQQRLEQEVNEHKVTKARLTDKHQSIEEAKSVAmcemEKKLKEEREAREKAENRVVQIEKQCSMLDVDLKQSQQKL 755
Cdd:COG1196   362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL----AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  756 EHLTGNKERMEDEVKNLTLQLEQESNKRLLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLEFELA--QLTKQYR 833
Cdd:COG1196   438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEgvKAALLLA 517
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  834 GNEGQMRELQDQLEAEQYFSTLYKTQVKELKEEIEEKNRENLKK-IQELQNEKETLAT--QLDLAETKAESEQLARGLLE 910
Cdd:COG1196   518 GLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAaIEYLKAAKAGRATflPLDKIRARAALAAALARGAI 597
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  911 EQYFELTQESKKAASRNRQEITDKDHTVSRLEEANSMLTKDIEILRRENEELTEKMKKAEEEYKLEKEEEISNLKAAFEK 990
Cdd:COG1196   598 GAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEA 677
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  991 NINTERTLKTQAVNKLAEIMNRKDFKIDRKKANTQDLRKKEKENRKLQLE--LNQEREKFNQMVVKHQKELNDMQAQLVE 1068
Cdd:COG1196   678 EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEeqLEAEREELLEELLEEEELLEEEALEELP 757
                         570       580
                  ....*....|....*....|..
gi 167887698 1069 ECAHRNELQMQLASKESDIEQL 1090
Cdd:COG1196   758 EPPDLEELERELERLEREIEAL 779
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
426-1097 2.06e-19

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 95.12  E-value: 2.06e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   426 ESLQKTIYKLE-EQLHNEM----QLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKEKMLLQHRINEYQR 500
Cdd:TIGR02168  223 RELELALLVLRlEELREELeelqEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   501 KAEQENEKRRNVENEVSTLKDQLEDLKkvsQNSQLANEKLSQLQKQLEEANdllrtesdtavrlrkshtemsksiSQLES 580
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEELE---SKLDELAEELAELEEKLEELK------------------------EELES 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   581 LNRELQERNRILENSKSQTDkdyyQLQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVEGERKEAQDMLN 660
Cdd:TIGR02168  356 LEAELEELEAELEELESRLE----ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   661 HSEKEKNNLEID-LNYKLKSLQQRLEQEVNEHKVTKARLTDKHQSI-----EEAKSVAMCEMEKKLKEEREAREKAENRV 734
Cdd:TIGR02168  432 EAELKELQAELEeLEEELEELQEELERLEEALEELREELEEAEQALdaaerELAQLQARLDSLERLQENLEGFSEGVKAL 511
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   735 VQIEKQCSMLDVDLKQS-------QQKLEHLTGnkERMED-EVKNLTLQ------LEQESNKRL--LLQNELKTQAFEAD 798
Cdd:TIGR02168  512 LKNQSGLSGILGVLSELisvdegyEAAIEAALG--GRLQAvVVENLNAAkkaiafLKQNELGRVtfLPLDSIKGTEIQGN 589
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   799 NLKGLEKQ------MKQEINTLLEAKRLLEFELAQLTKQYRGNEGQmrELQDQLEAEQYFSTLYKTQVKELKEEIEEKNR 872
Cdd:TIGR02168  590 DREILKNIegflgvAKDLVKFDPKLRKALSYLLGGVLVVDDLDNAL--ELAKKLRPGYRIVTLDGDLVRPGGVITGGSAK 667
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   873 ENLkKIQELQNEKETLATQLDLAETKAESEQLARGLLEEQYFELTQESKKAASR---NRQEITDKDHTVSRLEEANSMLT 949
Cdd:TIGR02168  668 TNS-SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEleeLSRQISALRKDLARLEAEVEQLE 746
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   950 KDIEILRRENEELTEKMKKAEEEYKLEKEE-------------EISNLKAAFEKNI------NTERTLKTQAVNKLAEIM 1010
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEElaeaeaeieeleaQIEQLKEELKALRealdelRAELTLLNEEAANLRERL 826
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  1011 NRKDFKIDRKKANTQDLRKKEKENRKLQLELNQEREKFNQMVVKHQKELNDMQAQLVEECAHRNELQMQLASKESDIEQL 1090
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906

                   ....*..
gi 167887698  1091 RAKLLDL 1097
Cdd:TIGR02168  907 ESKRSEL 913
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
493-1100 1.69e-17

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 88.64  E-value: 1.69e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   493 HRINEYQRKAEQENEKRrnvENEVSTLKDQLEDLKKVSQNSQLANEKLSQLQKQLEEANDLLRTESDTAVR--------- 563
Cdd:pfam15921   85 HQVKDLQRRLNESNELH---EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHeleaakclk 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   564 ---LRKSHTEMSKSISQLESLNRELQERNRILENSKSQTDKDYYQLQAILEAERRDRGHD-SEMIGDLQARITSLQEEVK 639
Cdd:pfam15921  162 edmLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAiSKILRELDTEISYLKGRIF 241
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   640 HLKHNLEKVEGERKEAQDMLnhsekeknnleidlnykLKSLQQRLEQEVNEHKVTKARLTDKHQSI-------------- 705
Cdd:pfam15921  242 PVEDQLEALKSESQNKIELL-----------------LQQHQDRIEQLISEHEVEITGLTEKASSArsqansiqsqleii 304
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   706 -EEAK---SVAMC---EMEKKLKEEREA----REKAENRVVQIEKQCSMLDVDLKQSQQKLEHLTGNKERMEDEVKNL-- 772
Cdd:pfam15921  305 qEQARnqnSMYMRqlsDLESTVSQLRSElreaKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLla 384
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   773 -------TLQLEQESNKRLL------------LQNELKTQAFEADNLKGLEKQMKQEINTLLEAK--------RLLEfEL 825
Cdd:pfam15921  385 dlhkrekELSLEKEQNKRLWdrdtgnsitidhLRRELDDRNMEVQRLEALLKAMKSECQGQMERQmaaiqgknESLE-KV 463
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   826 AQLTKQYRGNEGQMRELQDQLEAEQYfsTLYKTQVKELKEEIEEKNREnlKKIQELQNEKETLATQLDLaetkaESEQLA 905
Cdd:pfam15921  464 SSLTAQLESTKEMLRKVVEELTAKKM--TLESSERTVSDLTASLQEKE--RAIEATNAEITKLRSRVDL-----KLQELQ 534
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   906 RGLLEEQYFELTQESKKAAsrnRQEITDKDhtvsrleeansmltKDIEILRRENEELTEKMKKAEEEYKLEKEEeisnlK 985
Cdd:pfam15921  535 HLKNEGDHLRNVQTECEAL---KLQMAEKD--------------KVIEILRQQIENMTQLVGQHGRTAGAMQVE-----K 592
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   986 AAFEKNINtERTLKTQAVNKLAEimnRKDFKIDRKKANTQDLRKKE-------KENRKLQLELNQEREKFNQMVVKHQKE 1058
Cdd:pfam15921  593 AQLEKEIN-DRRLELQEFKILKD---KKDAKIRELEARVSDLELEKvklvnagSERLRAVKDIKQERDQLLNEVKTSRNE 668
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  1059 LNDMQAQLveECAHR-------------NELQMQLASKESDIEQLRAKLLDLSDS 1100
Cdd:pfam15921  669 LNSLSEDY--EVLKRnfrnkseemetttNKLKMQLKSAQSELEQTRNTLKSMEGS 721
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
419-965 4.02e-15

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 80.88  E-value: 4.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  419 NADKSLQEsLQKTIYKLEEQLHNEMQLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKEKMLLQ---HRI 495
Cdd:PRK03918  162 NAYKNLGE-VIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEelkEEI 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  496 NEYQRKAEQENEKRRNVENEVSTLKDQLEDLKKVSQNSQLANEKLSQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSI 575
Cdd:PRK03918  241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  576 SQLESLNRELQERN------RILENSKSQTDKDYYQLQAILEAERRDRGHDSEMIGdLQARITSLqeEVKHLKHNLEKVE 649
Cdd:PRK03918  321 EEINGIEERIKELEekeerlEELKKKLKELEKRLEELEERHELYEEAKAKKEELER-LKKRLTGL--TPEKLEKELEELE 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  650 GERKEAQDMLNHSEKEKNNLEIDLNYKLKSLqQRLEQEVNEHKVTKARLTDKHQ-SIEEAKSVAMCEMEKKLKEEREARE 728
Cdd:PRK03918  398 KAKEEIEEEISKITARIGELKKEIKELKKAI-EELKKAKGKCPVCGRELTEEHRkELLEEYTAELKRIEKELKEIEEKER 476
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  729 KAENRVVQIEKQCSmldvdlkqsqqKLEHLTGNKErMEDEVKNLTLQLEQESNKrlllqnELKTQAFEADNLKGLEKQMK 808
Cdd:PRK03918  477 KLRKELRELEKVLK-----------KESELIKLKE-LAEQLKELEEKLKKYNLE------ELEKKAEEYEKLKEKLIKLK 538
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  809 QEINTL---LEAKRLLEFELAQLTKQYRGNEGQMRELQDQLEaEQYFSTLykTQVKELKEEIEEKNRENL------KKIQ 879
Cdd:PRK03918  539 GEIKSLkkeLEKLEELKKKLAELEKKLDELEEELAELLKELE-ELGFESV--EELEERLKELEPFYNEYLelkdaeKELE 615
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  880 ELQNEKETLATQLD-----LAETKAESEQLaRGLLEEQYFELTQESKKAASRN----RQEITDKDHTVSRLEEANSMLTK 950
Cdd:PRK03918  616 REEKELKKLEEELDkafeeLAETEKRLEEL-RKELEELEKKYSEEEYEELREEylelSRELAGLRAELEELEKRREEIKK 694
                         570
                  ....*....|....*
gi 167887698  951 DIEILRRENEELTEK 965
Cdd:PRK03918  695 TLEKLKEELEEREKA 709
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
1229-1275 4.33e-12

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 62.10  E-value: 4.33e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 167887698   1229 HEFIPTLYHFPANCDACAKPLWHVFKPppALECRRCHVKCHRDHLDK 1275
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGSFKQ--GLRCSECKVKCHKKCADK 45
ROCK_SBD cd22250
Shroom-binding domain found in Rho-associated coiled-coil containing protein kinase; ...
1002-1058 1.99e-03

Shroom-binding domain found in Rho-associated coiled-coil containing protein kinase; Rho-associated coiled-coil containing protein kinase (ROCK) is a serine/threonine kinase (STK) that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. It is also referred to as Rho-associated protein kinase or simply as Rho kinase. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Rho-associated protein kinase 1 (ROCK1) is also called renal carcinoma antigen NY-REN-35, Rho-associated, coiled-coil-containing protein kinase 1, ROCK-I, p160 ROCK-1, or p160ROCK, 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 in ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. Rho-associated protein kinase 2 (ROCK2), also called Rho kinase 2, Rho-associated, coiled-coil-containing protein kinase 2, ROCK-II, or p164 ROCK-2, is more prominent in brain and skeletal muscle. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK subfamily proteins contain an N-terminal extension, a catalytic kinase domain, a coiled-coil (CC) 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 proteolytic cleavage, binding of lipids to the PH domain, or binding of GTP-bound RhoA to the CC region. More recently, the Shroom family of proteins have been identified as an additional regulator of ROCK. This model corresponds to the Shroom-binding domain (SBD) of ROCK, which forms a parallel coiled coil with the Shroom domain 2 (SD2) of Shroom.


Pssm-ID: 409019 [Multi-domain]  Cd Length: 75  Bit Score: 38.40  E-value: 1.99e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698 1002 AVNKLAEIMNRKDfkIDRKKANTQDLRKKEKENRKLQLELNQEREKFNQMVVKHQKE 1058
Cdd:cd22250    19 TLYKTQVKELKEE--LEEKTRQIKQELEDERESLSAQLELALAKADSEQLARSIAEE 73
 
Name Accession Description Interval E-value
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
2-406 0e+00

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: 865.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698    2 STGDSFETRFEKMDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDNFLSRYKDTINKIRDLRMKAEDYEVVKV 81
Cdd:cd05622     1 STGESFETRFEKIDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDNFLSRYKDTINKIRDLRMKAEDYEVVKV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd05622    81 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYI 241
Cdd:cd05622   161 VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  242 SPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLTDRE 321
Cdd:cd05622   241 SPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLTDRE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  322 VRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDDLEEDKGEEETFPIPKAFVGNQLPFVGFTYYS 401
Cdd:cd05622   321 VRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDDLEEDKGEEETFPIPKAFVGNQLPFVGFTYYS 400

                  ....*
gi 167887698  402 NRRYL 406
Cdd:cd05622   401 NRRYL 405
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
49-400 0e+00

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: 803.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   49 NKNIDNFLSRYKDTINKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIM 128
Cdd:cd05596     1 NKNIENFLNRYEKPVNEITKLRMNAEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAFFWEERDIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  129 AFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDK 208
Cdd:cd05596    81 AHANSEWIVQLHYAFQDDKYLYMVMDYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  209 SGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYS 288
Cdd:cd05596   161 SGHLKLADFGTCMKMDKDGLVRSDTAVGTPDYISPEVLKSQGGDGVYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  289 KIMNHKNSLTFPDDNDISKEAKNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNF 368
Cdd:cd05596   241 KIMNHKNSLQFPDDVEISKDAKSLICAFLTDREVRLGRNGIEEIKAHPFFKNDQWTWDNIRETVPPVVPELSSDIDTSNF 320
                         330       340       350
                  ....*....|....*....|....*....|..
gi 167887698  369 DDLEEDKGEEETFPIPKAFVGNQLPFVGFTYY 400
Cdd:cd05596   321 DDIEEDETPEETFPVPKAFVGNHLPFVGFTYS 352
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
23-400 0e+00

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: 757.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   23 SEVNSDCLLDGLDALVYDLDFPALRKNKNIDNFLSRYKDTINKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVY 102
Cdd:cd05621     1 SPINVESLLDGLNSLVLDLDFPALRKNKNIDNFLNRYEKIVNKIRELQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  103 AMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEV 182
Cdd:cd05621    81 AMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEYMPGGDLVNLMSNYDVPEKWAKFYTAEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  183 VLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYISPEVLKSQGGDGYYGRECDWW 262
Cdd:cd05621   161 VLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKMDETGMVHCDTAVGTPDYISPEVLKSQGGDGYYGRECDWW 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  263 SVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQ 342
Cdd:cd05621   241 SVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKNSLNFPDDVEISKHAKNLICAFLTDREVRLGRNGVEEIKQHPFFRNDQ 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  343 WAWETLRDTVAPVVPDLSSDIDTSNFDDLEEDKGEEETFPIPKAFVGNQLPFVGFTYY 400
Cdd:cd05621   321 WNWDNIRETAAPVVPELSSDIDTSNFDDIEDDKGDVETFPIPKAFVGNQLPFVGFTYY 378
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
74-400 0e+00

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: 575.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd05573     1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHVRAERDILADADSPWIVRLHYAFQDEDHLYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEG----- 227
Cdd:cd05573    81 EYMPGGDLMNLLIKYDVfPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMNKSGdresy 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  228 -----------------------MVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLV 284
Cdd:cd05573   161 lndsvntlfqdnvlarrrphkqrRVRAYSAVGTPDYIAPEVLRGTG----YGPECDWWSLGVILYEMLYGFPPFYSDSLV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  285 GTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLTDREVRLGRngVEEIKRHLFFKNDQWAWetLRDTVAPVVPDLSSDID 364
Cdd:cd05573   237 ETYSKIMNWKESLVFPDDPDVSPEAIDLIRRLLCDPEDRLGS--AEEIKAHPFFKGIDWEN--LRESPPPFVPELSSPTD 312
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 167887698  365 TSNFDDLEEDKGEEE--TFPIPKAFVGNQLPFVGFTYY 400
Cdd:cd05573   313 TSNFDDFEDDLLLSEylSNGSPLLGKGKQLAFVGFTFK 350
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
74-399 1.51e-167

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: 503.03  E-value: 1.51e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd05597     1 DDFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAETACFREERDVLVNGDRRWITKLHYAFQDENYLYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYD--VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRC 231
Cdd:cd05597    81 DYYCGGDLLTLLSKFEdrLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSCLKLREDGTVQS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  232 DTAVGTPDYISPEVLK-SQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDD-NDISKEA 309
Cdd:cd05597   161 SVAVGTPDYISPEILQaMEDGKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKEHFSFPDDeDDVSEEA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  310 KNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQwaWETLRDTVAPVVPDLSSDIDTSNFDDLEEDKGEEETFPIPK--AF 387
Cdd:cd05597   241 KDLIRRLICSRERRLGQNGIDDFKKHPFFEGID--WDNIRDSTPPYIPEVTSPTDTSNFDVDDDDLRHTDSLPPPSnaAF 318
                         330
                  ....*....|..
gi 167887698  388 VGNQLPFVGFTY 399
Cdd:cd05597   319 SGLHLPFVGFTY 330
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
74-399 1.98e-147

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: 449.84  E-value: 1.98e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd05601     1 KDFEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSFFEEERDIMAKANSPWITKLQYAFQDSENLYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYD--VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRC 231
Cdd:cd05601    81 EYHPGGDLLSLLSRYDdiFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSSDKTVTS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  232 DTAVGTPDYISPEVLKSQGGD--GYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEA 309
Cdd:cd05601   161 KMPVGTPDYIAPEVLTSMNGGskGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFKKFLKFPEDPKVSESA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  310 KNLICAFLTDREVRLGRNGveeIKRHLFFKNDQwaWETLRDTVAPVVPDLSSDIDTSNFDDLEEDK--GEEETFPIPKAF 387
Cdd:cd05601   241 VDLIKGLLTDAKERLGYEG---LCCHPFFSGID--WNNLRQTVPPFVPTLTSDDDTSNFDEFEPKKtrPSYENFNKSKGF 315
                         330
                  ....*....|..
gi 167887698  388 VGNQLPFVGFTY 399
Cdd:cd05601   316 SGKDLPFVGFTF 327
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
8-399 7.28e-144

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: 443.68  E-value: 7.28e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698    8 ETRFEKMDNLLRD----PKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDNFLSRYKDTINKIRDLRMKAEDYEVVKVIG 83
Cdd:cd05624     2 KVRLKKLEQLLLDgpqrNESALSVETLLDVLVCLYTECSHSPLRRDKYVSEFLEWAKPFTQLVKEMQLHRDDFEIIKVIG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   84 RGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVN 163
Cdd:cd05624    82 RGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERNVLVNGDCQWITTLHYAFQDENYLYLVMDYYVGGDLLT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  164 LMSNYD--VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYI 241
Cdd:cd05624   162 LLSKFEdkLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCLKMNDDGTVQSSVAVGTPDYI 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  242 SPEVLKS-QGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDD-NDISKEAKNLICAFLTD 319
Cdd:cd05624   242 SPEILQAmEDGMGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEERFQFPSHvTDVSEEAKDLIQRLICS 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  320 REVRLGRNGVEEIKRHLFFKNDQwaWETLRDTVAPVVPDLSSDIDTSNFDDLEEDKGEEETFPIPK--AFVGNQLPFVGF 397
Cdd:cd05624   322 RERRLGQNGIEDFKKHAFFEGLN--WENIRNLEAPYIPDVSSPSDTSNFDVDDDVLRNPEILPPSShtGFSGLHLPFVGF 399

                  ..
gi 167887698  398 TY 399
Cdd:cd05624   400 TY 401
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
74-399 4.37e-143

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: 438.20  E-value: 4.37e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd05599     1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVAHVRAERDILAEADNPWVVKLYYSFQDEENLYLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRcd 232
Cdd:cd05599    81 EFLPGGDMMTLLMKKDTlTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGLKKSHLAY-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  233 TAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNL 312
Cdd:cd05599   159 STVGTPDYIAPEVFLQKG----YGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNWRETLVFPPEVPISPEAKDL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  313 ICAFLTDREVRLGRNGVEEIKRHLFFKN-DqwaWETLRDTVAPVVPDLSSDIDTSNFDDLEEDKGEEETFPIPKAFVGNQ 391
Cdd:cd05599   235 IERLLCDAEHRLGANGVEEIKSHPFFKGvD---WDHIRERPAPILPEVKSILDTSNFDEFEEVDLQIPSSPEAGKDSKEL 311
                         330
                  ....*....|..
gi 167887698  392 ----LPFVGFTY 399
Cdd:cd05599   312 kskdWVFIGYTY 323
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
8-402 9.52e-137

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: 424.81  E-value: 9.52e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698    8 ETRFEKMDNLLRDPKSEVNSDC-----LLDGLDALVYDLDFPALRKNKNIDNFLSRYKDTINKIRDLRMKAEDYEVVKVI 82
Cdd:cd05623     1 EVRLRQLEQLILDGPGQTNGQCfsvetLLDILICLYDECSNSPLRREKNILEYLEWAKPFTSKVKQMRLHKEDFEILKVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   83 GRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLV 162
Cdd:cd05623    81 GRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGDSQWITTLHYAFQDDNNLYLVMDYYVGGDLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  163 NLMSNYD--VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDY 240
Cdd:cd05623   161 TLLSKFEdrLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMEDGTVQSSVAVGTPDY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  241 ISPEVLKS-QGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDD-NDISKEAKNLICAFLT 318
Cdd:cd05623   241 ISPEILQAmEDGKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKERFQFPTQvTDVSENAKDLIRRLIC 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  319 DREVRLGRNGVEEIKRHLFFKNDQwaWETLRDTVAPVVPDLSSDIDTSNFDDLEEDKGEEETFPIPK--AFVGNQLPFVG 396
Cdd:cd05623   321 SREHRLGQNGIEDFKNHPFFVGID--WDNIRNCEAPYIPEVSSPTDTSNFDVDDDCLKNCETMPPPThtAFSGHHLPFVG 398

                  ....*.
gi 167887698  397 FTYYSN 402
Cdd:cd05623   399 FTYTSS 404
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
75-405 1.06e-120

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: 378.97  E-value: 1.06e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVME 154
Cdd:cd05598     2 MFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNQVAHVKAERDILAEADNEWVVKLYYSFQDKENLYFVMD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCM----KMNKEGMV 229
Cdd:cd05598    82 YIPGGDLMSLLIKKGIfEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwTHDSKYYL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  230 RCdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEA 309
Cdd:cd05598   162 AH-SLVGTPNYIAPEVLLRTG----YTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVINWRTTLKIPHEANLSPEA 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  310 KNLICAFLTDREVRLGRNGVEEIKRHLFFKNdqWAWETLRDTVAPVVPDLSSDIDTSNFDDLEEDK-----GEEETFPIP 384
Cdd:cd05598   237 KDLILRLCCDAEDRLGRNGADEIKAHPFFAG--IDWEKLRKQKAPYIPTIRHPTDTSNFDPVDPEKlrssdEEPTTPNDP 314
                         330       340
                  ....*....|....*....|.
gi 167887698  385 KAFVGNQLPFVGFTYysnRRY 405
Cdd:cd05598   315 DNGKHPEHAFYEFTF---RRF 332
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
82-338 4.92e-118

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: 368.38  E-value: 4.92e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNY-DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmKMNKEGMVRCDTAVGTPDY 240
Cdd:cd05123    81 FSHLSKEgRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLA-KELSSDGDRTYTFCGTPEY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  241 ISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFPDdnDISKEAKNLICAFLT-D 319
Cdd:cd05123   160 LAPEVLLGKG----YGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKIL--KSPLKFPE--YVSPEAKSLISGLLQkD 231
                         250
                  ....*....|....*....
gi 167887698  320 REVRLGRNGVEEIKRHLFF 338
Cdd:cd05123   232 PTKRLGSGGAEEIKAHPFF 250
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
74-405 8.71e-112

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: 356.47  E-value: 8.71e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd05629     1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLAHVKAERDVLAESDSPWVVSLYYSFQDAQYLYLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCM----------- 221
Cdd:cd05629    81 EFLPGGDLMTMLIKYDTfSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLSTgfhkqhdsayy 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  222 ------KMNKEGMVRCDT-----------------------------AVGTPDYISPEVLKSQGgdgyYGRECDWWSVGV 266
Cdd:cd05629   161 qkllqgKSNKNRIDNRNSvavdsinltmsskdqiatwkknrrlmaysTVGTPDYIAPEIFLQQG----YGQECDWWSLGA 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  267 FLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQWAwe 346
Cdd:cd05629   237 IMFECLIGWPPFCSENSHETYRKIINWRETLYFPDDIHLSVEAEDLIRRLITNAENRLGRGGAHEIKSHPFFRGVDWD-- 314
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  347 TLRDTVAPVVPDLSSDIDTSNFDDLEEDKGEEETFPIPKAFVGNQ------LPFVGFTYysnRRY 405
Cdd:cd05629   315 TIRQIRAPFIPQLKSITDTSYFPTDELEQVPEAPALKQAAPAQQEesveldLAFIGYTY---KRF 376
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
82-343 1.23e-100

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: 321.86  E-value: 1.23e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRS--DSAFFweERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 159
Cdd:cd05579     1 ISRGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNqvDSVLA--ERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGtcmkMNKEGMVR-------- 230
Cdd:cd05579    79 DLYSLLENVGAlDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFG----LSKVGLVRrqiklsiq 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  231 ----------CDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnsLTFP 300
Cdd:cd05579   155 kksngapekeDRRIVGTPDYLAPEILLGQG----HGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGK--IEWP 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 167887698  301 DDNDISKEAKNLICAFLT-DREVRLGRNGVEEIKRHLFFKNDQW 343
Cdd:cd05579   229 EDPEVSDEAKDLISKLLTpDPEKRLGAKGIEEIKNHPFFKGIDW 272
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
76-338 2.01e-93

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 301.37  E-value: 2.01e-93
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698     76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKrsDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKK--DRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698    156 MPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGmvRCDTA 234
Cdd:smart00220   79 CEGGDLFDLLKKRGrLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGE--KLTTF 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698    235 VGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLIC 314
Cdd:smart00220  157 VGTPEYMAPEVLLGKG----YGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIR 232
                           250       260
                    ....*....|....*....|....*
gi 167887698    315 AFLT-DREVRLgrnGVEEIKRHLFF 338
Cdd:smart00220  233 KLLVkDPEKRL---TAEEALQHPFF 254
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
74-370 6.49e-91

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: 295.64  E-value: 6.49e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd05580     1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKegmvRCD 232
Cdd:cd05580    81 EYVPGGELFSLLRRSGrFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVKD----RTY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  233 TAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnsLTFPddNDISKEAKNL 312
Cdd:cd05580   157 TLCGTPEYLAPEIILSKG----HGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGK--IRFP--SFFDPDAKDL 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167887698  313 ICAFLT-DREVRLG--RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDD 370
Cdd:cd05580   229 IKRLLVvDLTKRLGnlKNGVEDIKNHPWFAGIDWDALLQRKIPAPYVPKVRGPGDTSNFDK 289
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
67-399 3.20e-89

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: 295.02  E-value: 3.20e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   67 RDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDD 146
Cdd:cd05600     4 RRTRLKLSDFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNEVNHVLTERDILTTTNSPWLVKLLYAFQDP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  147 RYLYMVMEYMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTC----- 220
Cdd:cd05600    84 ENVYLAMEYVPGGDFRTLLNNSGIlSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLAsgtls 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  221 ------MK-------------------------MNKEGMVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLY 269
Cdd:cd05600   164 pkkiesMKirleevkntafleltakerrniyraMRKEDQNYANSVVGSPDYMAPEVLRGEG----YDLTVDYWSLGCILF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  270 EMLVGDTPFYADSLVGTYSKIMNHKNSLTFP--DDND----ISKEAKNLICAFLTDREVRLGRngVEEIKRHLFFKNDQw 343
Cdd:cd05600   240 ECLVGFPPFSGSTPNETWANLYHWKKTLQRPvyTDPDlefnLSDEAWDLITKLITDPQDRLQS--PEQIKNHPFFKNID- 316
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167887698  344 aWETLRD-TVAPVVPDLSSDIDTSNFDDLEEDKGEEETFPI---PKAFVG---------NQLPFVGFTY 399
Cdd:cd05600   317 -WDRLREgSKPPFIPELESEIDTSYFDDFNDEADMAKYKDVhekQKSLEGsgknggdngNRSLFVGFTF 384
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
74-373 3.64e-87

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: 288.49  E-value: 3.64e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd05627     2 DDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVR-- 230
Cdd:cd05627    82 EFLPGGDMMTLLMKKDtLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTGLKKAHRTEfy 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  231 --------------------------------CDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd05627   162 rnlthnppsdfsfqnmnskrkaetwkknrrqlAYSTVGTPDYIAPEVFMQTG----YNKLCDWWSLGVIMYEMLIGYPPF 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  279 YADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQwaWETLRDTVAPVVPD 358
Cdd:cd05627   238 CSETPQETYRKVMNWKETLVFPPEVPISEKAKDLILRFCTDAENRIGSNGVEEIKSHPFFEGVD--WEHIRERPAAIPIE 315
                         330
                  ....*....|....*
gi 167887698  359 LSSDIDTSNFDDLEE 373
Cdd:cd05627   316 IKSIDDTSNFDDFPE 330
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
79-376 1.53e-83

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: 278.82  E-value: 1.53e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   79 VKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPG 158
Cdd:cd05626     6 IKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDYIPG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  159 GDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKM---------NKEGM 228
Cdd:cd05626    86 GDMMSLLIRMEVfPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTGFrwthnskyyQKGSH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  229 VRCDTA-------------------------------------VGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEM 271
Cdd:cd05626   166 IRQDSMepsdlwddvsncrcgdrlktleqratkqhqrclahslVGTPNYIAPEVLLRKG----YTQLCDWWSVGVILFEM 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  272 LVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQWAwETLRDT 351
Cdd:cd05626   242 LVGQPPFLAPTPTETQLKVINWENTLHIPPQVKLSPEAVDLITKLCCSAEERLGRNGADDIKAHPFFSEVDFS-SDIRTQ 320
                         330       340
                  ....*....|....*....|....*
gi 167887698  352 VAPVVPDLSSDIDTSNFDDLEEDKG 376
Cdd:cd05626   321 PAPYVPKISHPMDTSNFDPVEEESP 345
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
75-364 2.00e-83

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: 276.04  E-value: 2.00e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVME 154
Cdd:cd05574     2 HFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRVLTEREILATLDHPFLPTLYASFQTSTHLCFVMD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDLVNLM---SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRC 231
Cdd:cd05574    82 YCPGGELFRLLqkqPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKQSSVTPPPVR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  232 DTA----------------------------VGTPDYISPEVLKsqgGDGYyGRECDWWSVGVFLYEMLVGDTPFYADSL 283
Cdd:cd05574   162 KSLrkgsrrssvksieketfvaepsarsnsfVGTEEYIAPEVIK---GDGH-GSAVDWWTLGILLYEMLYGTTPFKGSNR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  284 VGTYSKIMnhKNSLTFPDDNDISKEAKNLICAFL-TDREVRLG-RNGVEEIKRHLFFKNDQWAweTLRDTVAPVVPDLSS 361
Cdd:cd05574   238 DETFSNIL--KKELTFPESPPVSSEAKDLIRKLLvKDPSKRLGsKRGASEIKRHPFFRGVNWA--LIRNMTPPIIPRPDD 313

                  ...
gi 167887698  362 DID 364
Cdd:cd05574   314 PID 316
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
80-400 3.69e-83

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: 275.25  E-value: 3.69e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANS-PWVVQLFYAFQDDRYLYMVMEYMPG 158
Cdd:cd05570     1 KVLGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTMTEKRVLALANRhPFLTGLHACFQTEDRLYFVMEYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  159 GDLV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmkmnKEGM---VRCDTA 234
Cdd:cd05570    81 GDLMfHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMC----KEGIwggNTTSTF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  235 VGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnsLTFPddNDISKEAKNLIC 314
Cdd:cd05570   157 CGTPDYIAPEILREQD----YGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDE--VLYP--RWLSREAVSILK 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  315 AFLT-DREVRLG--RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDDlEEDKGEEETFPIPKAFVGN- 390
Cdd:cd05570   229 GLLTkDPARRLGcgPKGEADIKAHPFFRNIDWDKLEKKEVEPPFKPKVKSPRDTSNFDP-EFTSESPRLTPVDSDLLTNi 307
                         330
                  ....*....|.
gi 167887698  391 -QLPFVGFTYY 400
Cdd:cd05570   308 dQEEFRGFSYI 318
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
74-373 4.57e-83

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: 277.31  E-value: 4.57e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd05628     1 EDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVR-- 230
Cdd:cd05628    81 EFLPGGDMMTLLMKKDtLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKKAHRTEfy 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  231 --------------------------------CDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd05628   161 rnlnhslpsdftfqnmnskrkaetwkrnrrqlAFSTVGTPDYIAPEVFMQTG----YNKLCDWWSLGVIMYEMLIGYPPF 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  279 YADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQwaWETLRDTVAPVVPD 358
Cdd:cd05628   237 CSETPQETYKKVMNWKETLIFPPEVPISEKAKDLILRFCCEWEHRIGAPGVEEIKTNPFFEGVD--WEHIRERPAAIPIE 314
                         330
                  ....*....|....*
gi 167887698  359 LSSDIDTSNFDDLEE 373
Cdd:cd05628   315 IKSIDDTSNFDEFPD 329
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
75-343 9.83e-80

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: 263.88  E-value: 9.83e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVME 154
Cdd:cd05609     1 DFETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDLVNLMSNY-DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTC----MKMNK---E 226
Cdd:cd05609    81 YVEGGDCATLLKNIgPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSkiglMSLTTnlyE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  227 GMVRCDT-------AVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNhkNSLTF 299
Cdd:cd05609   161 GHIEKDTrefldkqVCGTPEYIAPEVILRQG----YGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVIS--DEIEW 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 167887698  300 PDDND-ISKEAKNLICAFL-TDREVRLGRNGVEEIKRHLFFKNDQW 343
Cdd:cd05609   235 PEGDDaLPDDAQDLITRLLqQNPLERLGTGGAEEVKQHPFFQDLDW 280
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
74-370 6.69e-77

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: 256.56  E-value: 6.69e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd14209     1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCd 232
Cdd:cd14209    81 EYVPGGEMFSHLRRIGrFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKGRTWTLC- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  233 tavGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnsLTFPD--DNDISKEAK 310
Cdd:cd14209   160 ---GTPEYLAPEIILSKG----YNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGK--VRFPShfSSDLKDLLR 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  311 NLICAFLTDREVRLgRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDD 370
Cdd:cd14209   231 NLLQVDLTKRFGNL-KNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKLKGPGDTSNFDD 289
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
79-375 2.29e-76

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: 258.44  E-value: 2.29e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   79 VKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPG 158
Cdd:cd05625     6 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  159 GDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTC----------------- 220
Cdd:cd05625    86 GDMMSLLIRMGVfPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyqsgdh 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  221 -----MKMNKE----GMVRC--------------------DTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEM 271
Cdd:cd05625   166 lrqdsMDFSNEwgdpENCRCgdrlkplerraarqhqrclaHSLVGTPNYIAPEVLLRTG----YTQLCDWWSVGVILFEM 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  272 LVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQWAwETLRDT 351
Cdd:cd05625   242 LVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKNGADEIKAHPFFKTIDFS-SDLRQQ 320
                         330       340
                  ....*....|....*....|....
gi 167887698  352 VAPVVPDLSSDIDTSNFDDLEEDK 375
Cdd:cd05625   321 SAPYIPKITHPTDTSNFDPVDPDK 344
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
74-373 1.88e-75

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: 252.36  E-value: 1.88e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd05612     1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGtcmkMNKEGMVRCD 232
Cdd:cd05612    81 EYVPGGELFSyLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFG----FAKKLRDRTW 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  233 TAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnsLTFPDDNDISkeAKNL 312
Cdd:cd05612   157 TLCGTPEYLAPEVIQSKG----HNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGK--LEFPRHLDLY--AKDL 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167887698  313 ICAFLT-DREVRLG--RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDDLEE 373
Cdd:cd05612   229 IKKLLVvDRTRRLGnmKNGADDVKNHRWFKSVDWDDVPQRKLKPPIVPKVSHDGDTSNFDDYPE 292
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
74-338 3.13e-74

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: 248.28  E-value: 3.13e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd05581     1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKKVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDL---VNLMSNYDvpEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGM-- 228
Cdd:cd05581    81 EYAPNGDLleyIRKYGSLD--EKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKVLGPDSSpe 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  229 --------------VRCDTAVGTPDYISPEVLksqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNhk 294
Cdd:cd05581   159 stkgdadsqiaynqARAASFVGTAEYVSPELL----NEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVK-- 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 167887698  295 NSLTFPddNDISKEAKNLICAFL-TDREVRLG---RNGVEEIKRHLFF 338
Cdd:cd05581   233 LEYEFP--ENFPPDAKDLIQKLLvLDPSKRLGvneNGGYDELKAHPFF 278
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
80-399 4.34e-73

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: 246.85  E-value: 4.34e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSdsaffwEERDIMAFAN-------SPWVVQLFYAFQDDRYLYMV 152
Cdd:cd05575     1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRN------EVKHIMAERNvllknvkHPFLVGLHYSFQTKDKLYFV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGGDLV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmkmnKEGMVRC 231
Cdd:cd05575    75 LDYVNGGELFfHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLC----KEGIEPS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  232 DTA---VGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnsLTFPDdnDISKE 308
Cdd:cd05575   151 DTTstfCGTPEYLAPEVLRKQP----YDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKP--LRLRT--NVSPS 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  309 AKNLICAFL-TDREVRLG-RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDDleedkgEEETFPIPKA 386
Cdd:cd05575   223 ARDLLEGLLqKDRTKRLGsGNDFLEIKNHSFFRPINWDDLEAKKIPPPFNPNVSGPLDLRNIDP------EFTREPVPAS 296
                         330       340
                  ....*....|....*....|....*.
gi 167887698  387 FVGNQ-------------LPFVGFTY 399
Cdd:cd05575   297 VGKSAdsvavsasvqeadNAFDGFSY 322
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
79-343 1.61e-71

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: 240.07  E-value: 1.61e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   79 VKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAF-ANSPWVVQLFYAFQDDRYLYMVMEYMP 157
Cdd:cd05611     1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNVKAERAIMMIqGESPYVAKLYYSFQSKDYLYLVMEYLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  158 GGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGtcmkMNKEGMVRCDTA-- 234
Cdd:cd05611    81 GGDCASLIKTLGGlPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFG----LSRNGLEKRHNKkf 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  235 VGTPDYISPEVLKSQGGDgyygRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFPDDND--ISKEAKNL 312
Cdd:cd05611   157 VGTPDYLAPETILGVGDD----KMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNIL--SRRINWPEEVKefCSPEAVDL 230
                         250       260       270
                  ....*....|....*....|....*....|..
gi 167887698  313 ICAFLT-DREVRLGRNGVEEIKRHLFFKNDQW 343
Cdd:cd05611   231 INRLLCmDPAKRLGANGYQEIKSHPFFKSINW 262
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
72-397 4.74e-71

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 241.26  E-value: 4.74e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   72 KAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYM 151
Cdd:PTZ00263   16 KLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  152 VMEYMPGGDL-VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKegmvR 230
Cdd:PTZ00263   96 LLEFVVGGELfTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPD----R 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  231 CDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnsLTFPddNDISKEAK 310
Cdd:PTZ00263  172 TFTLCGTPEYLAPEVIQSKG----HGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGR--LKFP--NWFDGRAR 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  311 NLICAFL-TDREVRLG--RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDDLEEdKGEEETFPIPKAf 387
Cdd:PTZ00263  244 DLVKGLLqTDHTKRLGtlKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFEKYPD-SPVDRLPPLTAA- 321
                         330
                  ....*....|
gi 167887698  388 vgNQLPFVGF 397
Cdd:PTZ00263  322 --QQAEFAGF 329
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
76-402 1.00e-70

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: 240.28  E-value: 1.00e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANS---PWVVQLFYAFQDDRYLYMV 152
Cdd:cd05589     1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVESLMCEKRIFETVNSarhPFLVNLFACFQTPEHVCFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmkmnKEGM---V 229
Cdd:cd05589    81 MEYAAGGDLMMHIHEDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC----KEGMgfgD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  230 RCDTAVGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNhkNSLTFPddNDISKEA 309
Cdd:cd05589   157 RTSTFCGTPEFLAPEVLT----DTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVN--DEVRYP--RFLSTEA 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  310 KNLICAFL-TDREVRLG--RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDdlEEDKGEEETFPIPKA 386
Cdd:cd05589   229 ISIMRRLLrKNPERRLGasERDAEDVKKQPFFRNIDWEALLARKIKPPFVPTIKSPEDVSNFD--EEFTSEKPVLTPPKE 306
                         330       340
                  ....*....|....*....|
gi 167887698  387 F----VGNQLPFVGFTYYSN 402
Cdd:cd05589   307 PrpltEEEQALFKDFDYVAD 326
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
80-399 3.86e-69

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: 235.38  E-value: 3.86e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTR---KVYAMKLLSKfEMIKRS--DSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVME 154
Cdd:cd05584     2 KVLGKGGYGKVFQVRKTTGSdkgKIFAMKVLKK-ASIVRNqkDTAHTKAERNILEAVKHPFIVDLHYAFQTGGKLYLILE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVrCDT 233
Cdd:cd05584    81 YLSGGELFMHLEREGIfMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIHDGTV-THT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  234 AVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFPddNDISKEAKNLI 313
Cdd:cd05584   160 FCGTIEYMAPEILTRSG----HGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKIL--KGKLNLP--PYLTNEARDLL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  314 CAFLTDREV-RLGR--NGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFD-----DLEEDKGEEETFPIPK 385
Cdd:cd05584   232 KKLLKRNVSsRLGSgpGDAEEIKAHPFFRHINWDDLLAKKVEPPFKPLLQSEEDVSQFDskftkQTPVDSPDDSTLSESA 311
                         330
                  ....*....|....
gi 167887698  386 afvgnQLPFVGFTY 399
Cdd:cd05584   312 -----NQVFQGFTY 320
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
82-343 4.13e-69

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: 232.89  E-value: 4.13e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 ------VNLMSNYDvpekwARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMnkEGMVRCDTAV 235
Cdd:cd05572    81 wtilrdRGLFDEYT-----ARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKL--GSGRKTWTFC 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  236 GTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSL--VGTYSKIMNHKNSLTFPddNDISKEAKNLI 313
Cdd:cd05572   154 GTPEYVAPEIILNKG----YDFSVDYWSLGILLYELLTGRPPFGGDDEdpMKIYNIILKGIDKIEFP--KYIDKNAKNLI 227
                         250       260       270
                  ....*....|....*....|....*....|...
gi 167887698  314 CAFLTDR-EVRLG--RNGVEEIKRHLFFKNDQW 343
Cdd:cd05572   228 KQLLRRNpEERLGylKGGIRDIKKHKWFEGFDW 260
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
80-370 4.98e-69

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: 235.33  E-value: 4.98e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 159
Cdd:cd05571     1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmkmnKEGMVRCDTA---V 235
Cdd:cd05571    81 ELFFHLSRERVfSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLC----KEEISYGATTktfC 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  236 GTPDYISPEVLKsqggDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFPDdnDISKEAKNLICA 315
Cdd:cd05571   157 GTPEYLAPEVLE----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELIL--MEEVRFPS--TLSPEAKSLLAG 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  316 FLT-DREVRLG--RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDD 370
Cdd:cd05571   229 LLKkDPKKRLGggPRDAKEIMEHPFFASINWDDLYQKKIPPPFKPQVTSETDTRYFDE 286
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
80-399 5.62e-69

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: 234.97  E-value: 5.62e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFA-NSPWVVQLFYAFQDDRYLYMVMEYMPG 158
Cdd:cd05592     1 KVLGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDVECTMIERRVLALAsQHPFLTHLFCTFQTESHLFFVMEYLNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  159 GDLV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmKMNKEGMVRCDTAVGT 237
Cdd:cd05592    81 GDLMfHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMC-KENIYGENKASTFCGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  238 PDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnsLTFPddNDISKEAKNLICAFL 317
Cdd:cd05592   160 PDYIAPEILKGQ----KYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDT--PHYP--RWLTKEAASCLSLLL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  318 T-DREVRLGRNGVE--EIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDdleEDKGEEETF--PIPKAFVG--N 390
Cdd:cd05592   232 ErNPEKRLGVPECPagDIRDHPFFKTIDWDKLERREIDPPFKPKVKSANDVSNFD---PDFTMEKPVltPVDKKLLAsmD 308

                  ....*....
gi 167887698  391 QLPFVGFTY 399
Cdd:cd05592   309 QEQFKGFSF 317
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
81-399 1.39e-68

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: 233.62  E-value: 1.39e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   81 VIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGD 160
Cdd:cd05585     1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  161 LV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmKMNKEGMVRCDTAVGTPD 239
Cdd:cd05585    81 LFhHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLC-KLNMKDDDKTNTFCGTPE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  240 YISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFPDDNDisKEAKNLICAFLT- 318
Cdd:cd05585   160 YLAPELLLGHG----YTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKIL--QEPLRFPDGFD--RDAKDLLIGLLNr 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  319 DREVRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDdleedkgEEETFPIPKAFV--------GN 390
Cdd:cd05585   232 DPTKRLGYNGAQEIKNHPFFDQIDWKRLLMKKIQPPFKPAVENAIDTSNFD-------EEFTREKPIDSVvddshlseSV 304

                  ....*....
gi 167887698  391 QLPFVGFTY 399
Cdd:cd05585   305 QQQFEGWSY 313
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
75-318 1.12e-67

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: 228.90  E-value: 1.12e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFwEERDIMAFANSPWVVQLFYAFQDDRYLYMVME 154
Cdd:cd05117     1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLR-REIEILKRLDHPNIVKLYEVFEDDKNLYLVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL---DKSGHLKLADFGTCMKMNKEGMVR 230
Cdd:cd05117    80 LCTGGELFDRIVKKGSfSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLAKIFEEGEKLK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  231 cdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFPDD--NDISKE 308
Cdd:cd05117   160 --TVCGTPYYVAPEVLKGKG----YGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKIL--KGKYSFDSPewKNVSEE 231
                         250
                  ....*....|
gi 167887698  309 AKNLICAFLT 318
Cdd:cd05117   232 AKDLIKRLLV 241
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
80-399 2.97e-66

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: 227.28  E-value: 2.97e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSP-WVVQLFYAFQDDRYLYMVMEYMPG 158
Cdd:cd05587     2 MVLGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDDVECTMVEKRVLALSGKPpFLTQLHSCFQTMDRLYFVMEYVNG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  159 GDLV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmKMNKEGMVRCDTAVGT 237
Cdd:cd05587    82 GDLMyHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMC-KEGIFGGKTTRTFCGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  238 PDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHknSLTFPddNDISKEAKNLICAFL 317
Cdd:cd05587   161 PDYIAPEIIAYQ----PYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEH--NVSYP--KSLSKEAVSICKGLL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  318 T-DREVRLG--RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDDlEEDKGEEETFPIPKAFVGN--QL 392
Cdd:cd05587   233 TkHPAKRLGcgPTGERDIKEHPFFRRIDWEKLERREIQPPFKPKIKSPRDAENFDK-EFTKEPPVLTPTDKLVIMNidQS 311

                  ....*..
gi 167887698  393 PFVGFTY 399
Cdd:cd05587   312 EFEGFSF 318
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
75-339 1.70e-65

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: 222.35  E-value: 1.70e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVME 154
Cdd:cd14007     1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEgmvRCDT 233
Cdd:cd14007    81 YAPNGELYKeLKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVHAPSN---RRKT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  234 AVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnsLTFPDdnDISKEAKNLI 313
Cdd:cd14007   158 FCGTLDYLPPEMVEGKE----YDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVD--IKFPS--SVSPEAKDLI 229
                         250       260
                  ....*....|....*....|....*..
gi 167887698  314 CAFLT-DREVRLgrnGVEEIKRHLFFK 339
Cdd:cd14007   230 SKLLQkDPSKRL---SLEQVLNHPWIK 253
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
80-399 5.27e-64

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: 220.73  E-value: 5.27e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTR---KVYAMKLLSKfEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYM 156
Cdd:cd05582     1 KVLGQGSFGKVFLVRKITGPdagTLYAMKVLKK-ATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  157 PGGDLVNLMSN-YDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmKMNKEGMVRCDTAV 235
Cdd:cd05582    80 RGGDLFTRLSKeVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLS-KESIDHEKKAYSFC 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  236 GTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFPddNDISKEAKNLICA 315
Cdd:cd05582   159 GTVEYMAPEVVNRRG----HTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMIL--KAKLGMP--QFLSPEAQSLLRA 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  316 -FLTDREVRLG--RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDDLEEDKGEEETFPIPKAFVGNQL 392
Cdd:cd05582   231 lFKRNPANRLGagPDGVEEIKRHPFFATIDWNKLYRKEIKPPFKPAVSRPDDTFYFDPEFTSRTPKDSPGVPPSANAHQL 310

                  ....*..
gi 167887698  393 pFVGFTY 399
Cdd:cd05582   311 -FRGFSF 316
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
76-338 8.97e-64

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: 217.51  E-value: 8.97e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd05578     2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDL-VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVrcDTA 234
Cdd:cd05578    82 LLGGDLrYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTDGTLA--TST 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  235 VGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKI-MNHKNSLTFPddNDISKEAKNLI 313
Cdd:cd05578   160 SGTKPYMAPEVFMRAG----YSFAVDWWSLGVTAYEMLRGKRPYEIHSRTSIEEIRaKFETASVLYP--AGWSEEAIDLI 233
                         250       260
                  ....*....|....*....|....*.
gi 167887698  314 CAFLT-DREVRLGrnGVEEIKRHLFF 338
Cdd:cd05578   234 NKLLErDPQKRLG--DLSDLKNHPYF 257
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
80-370 3.25e-63

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: 218.72  E-value: 3.25e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 159
Cdd:cd05595     1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmkmnKEGM---VRCDTAV 235
Cdd:cd05595    81 ELFFHLSRERVfTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLC----KEGItdgATMKTFC 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  236 GTPDYISPEVLKsqggDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnsLTFPddNDISKEAKNLICA 315
Cdd:cd05595   157 GTPEYLAPEVLE----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEE--IRFP--RTLSPEAKSLLAG 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  316 FL-TDREVRL--GRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDD 370
Cdd:cd05595   229 LLkKDPKQRLggGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDD 286
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
75-335 7.17e-62

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: 211.99  E-value: 7.17e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSK-------FEMIKRsdsaffweERDIMAFANSPWVVQLFYAFQDDR 147
Cdd:cd14003     1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKsklkeeiEEKIKR--------EIEIMKLLNHPNIIKLYEVIETEN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  148 YLYMVMEYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKE 226
Cdd:cd14003    73 KIYLVMEYASGGELFDyIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  227 GMvrCDTAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnsltFPDDNDIS 306
Cdd:cd14003   153 SL--LKTFCGTPAYAAPEVLL---GRKYDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGK----YPIPSHLS 223
                         250       260       270
                  ....*....|....*....|....*....|
gi 167887698  307 KEAKNLICAFLT-DREVRLgrnGVEEIKRH 335
Cdd:cd14003   224 PDARDLIRRMLVvDPSKRI---TIEEILNH 250
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
80-401 1.44e-61

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: 213.62  E-value: 1.44e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFA-NSPWVVQLFYAFQDDRYLYMVMEYMPG 158
Cdd:cd05590     1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECTMTEKRILSLArNHPFLTQLYCCFQTPDRLFFVMEFVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  159 GDLV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmkmnKEGM---VRCDTA 234
Cdd:cd05590    81 GDLMfHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMC----KEGIfngKTTSTF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  235 VGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNhkNSLTFPddNDISKEAKNLIC 314
Cdd:cd05590   157 CGTPDYIAPEILQEM----LYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILN--DEVVYP--TWLSQDAVDILK 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  315 AFLT-DREVRLG---RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDD--LEEDKG----EEETFPIP 384
Cdd:cd05590   229 AFMTkNPTMRLGsltLGGEEAILRHPFFKELDWEKLNRRQIEPPFRPRIKSREDVSNFDPdfIKEDPVltpiEESLLPMI 308
                         330
                  ....*....|....*..
gi 167887698  385 kafvgNQLPFVGFTYYS 401
Cdd:cd05590   309 -----NQDEFRNFSYTA 320
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
80-399 5.43e-61

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: 211.97  E-value: 5.43e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANS-PWVVQLFYAFQDDRYLYMVMEYMPG 158
Cdd:cd05591     1 KVLGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDDVDCTMTEKRILALAAKhPFLTALHSCFQTKDRLFFVMEYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  159 GDL---VNLMSNYDVPEkwARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmkmnKEGM---VRCD 232
Cdd:cd05591    81 GDLmfqIQRARKFDEPR--ARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMC----KEGIlngKTTT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  233 TAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNhkNSLTFPddNDISKEAKNL 312
Cdd:cd05591   155 TFCGTPDYIAPEILQELE----YGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH--DDVLYP--VWLSKEAVSI 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  313 ICAFLTDREV-RLG----RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDDlEEDKGEEETFPIPKAF 387
Cdd:cd05591   227 LKAFMTKNPAkRLGcvasQGGEDAIRQHPFFREIDWEALEQRKVKPPFKPKIKTKRDANNFDQ-DFTKEEPVLTPVDPAV 305
                         330
                  ....*....|....
gi 167887698  388 VG--NQLPFVGFTY 399
Cdd:cd05591   306 IKqiNQEEFRGFSF 319
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
74-369 6.86e-61

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: 212.82  E-value: 6.86e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd05610     4 EEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG-------------- 218
Cdd:cd05610    84 EYLIGGDVKSLLHIYGyFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGlskvtlnrelnmmd 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  219 --TCMKMNK----------------------------------EGMVRCDTA--VGTPDYISPEVLKSQGgdgyYGRECD 260
Cdd:cd05610   164 ilTTPSMAKpkndysrtpgqvlslisslgfntptpyrtpksvrRGAARVEGEriLGTPDYLAPELLLGKP----HGPAVD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  261 WWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNhkNSLTFPD-DNDISKEAKNLICAFLTDREVRlgRNGVEEIKRHLFFk 339
Cdd:cd05610   240 WWALGVCLFEFLTGIPPFNDETPQQVFQNILN--RDIPWPEgEEELSVNAQNAIEILLTMDPTK--RAGLKELKQHPLF- 314
                         330       340       350
                  ....*....|....*....|....*....|
gi 167887698  340 nDQWAWETLRDTVAPVVPDLSSDIDTSNFD 369
Cdd:cd05610   315 -HGVDWENLQNQTMPFIPQPDDETDTSYFE 343
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
82-369 4.44e-60

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: 209.73  E-value: 4.44e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIM---AFANSPWVVQLFYAFQDDRYLYMVMEYMPG 158
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHTIGERNILvrtALDESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  159 GDLV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmKMNKEGMVRCDTAVGT 237
Cdd:cd05586    81 GELFwHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLS-KADLTDNKTTNTFCGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  238 PDYISPEVLKSQGGdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnsLTFPDDNdISKEAKNLICAFL 317
Cdd:cd05586   160 TEYLAPEVLLDEKG---YTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGK--VRFPKDV-LSDEGRSFVKGLL 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 167887698  318 T-DREVRLGR-NGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFD 369
Cdd:cd05586   234 NrNPKHRLGAhDDAVELKEHPFFADIDWDLLSKKKITPPFKPIVDSDTDVSNFD 287
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
79-399 8.85e-60

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: 208.66  E-value: 8.85e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   79 VKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIM-AFANSPWVVQLFYAFQDDRYLYMVMEYMP 157
Cdd:cd05604     1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTDKLYFVLDFVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  158 GGDLV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmkmnKEGMVRCDTAV- 235
Cdd:cd05604    81 GGELFfHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLC----KEGISNSDTTTt 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  236 --GTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnHKNSLTFPddnDISKEAKNLI 313
Cdd:cd05604   157 fcGTPEYLAPEVIRKQP----YDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENIL-HKPLVLRP---GISLTAWSIL 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  314 CAFL-TDREVRLG-RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDdleeDKGEEETFPIPKAFVGNQ 391
Cdd:cd05604   229 EELLeKDRQLRLGaKEDFLEIKNHPFFESINWTDLVQKKIPPPFNPNVNGPDDISNFD----AEFTEEMVPYSVCVSSDY 304
                         330
                  ....*....|....*....
gi 167887698  392 L-----------PFVGFTY 399
Cdd:cd05604   305 SivnasvleaddAFVGFSY 323
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
72-369 2.80e-59

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: 207.95  E-value: 2.80e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   72 KAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIM-AFANSPWVVQLFYAFQDDRYLY 150
Cdd:cd05602     5 KPSDFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSERNVLlKNVKHPFLVGLHFSFQTTDKLY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGGDLV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmKMNKEGMV 229
Cdd:cd05602    85 FVLDYINGGELFyHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLC-KENIEPNG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  230 RCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTfpddNDISKEA 309
Cdd:cd05602   164 TTSTFCGTPEYLAPEVLHKQP----YDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLK----PNITNSA 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887698  310 KNLICAFL-TDREVRLG-RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFD 369
Cdd:cd05602   236 RHLLEGLLqKDRTKRLGaKDDFTEIKNHIFFSPINWDDLINKKITPPFNPNVSGPNDLRHFD 297
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
75-368 4.67e-59

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: 206.69  E-value: 4.67e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKS---TRKVYAMKLLSKFEMIKRSDSAFFWE-ERDIMAFA-NSPWVVQLFYAFQDDRYL 149
Cdd:cd05614     1 NFELLKVLGTGAYGKVFLVRKVSghdANKLYAMKVLRKAALVQKAKTVEHTRtERNVLEHVrQSPFLVTLHYAFQTDAKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 YMVMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGM 228
Cdd:cd05614    81 HLILDYVSGGELFTHLYQRDhFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  229 VRCDTAVGTPDYISPEVLKSQGGdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNH--KNSLTFPddNDIS 306
Cdd:cd05614   161 ERTYSFCGTIEYMAPEIIRGKSG---HGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSEVSRRilKCDPPFP--SFIG 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  307 KEAKNLICAFL-TDREVRLGR--NGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNF 368
Cdd:cd05614   236 PVARDLLQKLLcKDPKKRLGAgpQGAQEIKEHPFFKGLDWEALALRKVNPPFRPSIRSELDVGNF 300
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
81-340 1.84e-58

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: 202.62  E-value: 1.84e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   81 VIGRGAFGEVQLVRH---KSTRKVYAMKLLSKFEMIKRSDSAffwE----ERDIM-AFANSPWVVQLFYAFQDDRYLYMV 152
Cdd:cd05583     1 VLGTGAYGKVFLVRKvggHDAGKLYAMKVLKKATIVQKAKTA---EhtmtERQVLeAVRQSPFLVTLHYAFQTDAKLHLI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGGDL-VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRC 231
Cdd:cd05583    78 LDYVNGGELfTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGENDRA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  232 DTAVGTPDYISPEVLKsqGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNH--KNSLTFPddNDISKEA 309
Cdd:cd05583   158 YSFCGTIEYMAPEVVR--GGSDGHDKAVDWWSLGVLTYELLTGASPFTVDGERNSQSEISKRilKSHPPIP--KTFSAEA 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 167887698  310 KNLICAFLT-DREVRLGRN--GVEEIKRHLFFKN 340
Cdd:cd05583   234 KDFILKLLEkDPKKRLGAGprGAHEIKEHPFFKG 267
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
75-399 8.86e-58

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: 202.92  E-value: 8.86e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSP-WVVQLFYAFQDDRYLYMVM 153
Cdd:cd05616     1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALSGKPpFLTQLHSCFQTMDRLYFVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmKMNKEGMVRCD 232
Cdd:cd05616    81 EYVNGGDLMyHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMC-KENIWDGVTTK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  233 TAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHknSLTFPddNDISKEAKNL 312
Cdd:cd05616   160 TFCGTPDYIAPEIIAYQP----YGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEH--NVAYP--KSMSKEAVAI 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  313 ICAFLTD---REVRLGRNGVEEIKRHLFFKndQWAWETL-RDTVAPVVPDLSSDIDTSNFDDlEEDKGEEETFPIPKAFV 388
Cdd:cd05616   232 CKGLMTKhpgKRLGCGPEGERDIKEHAFFR--YIDWEKLeRKEIQPPYKPKACGRNAENFDR-FFTRHPPVLTPPDQEVI 308
                         330
                  ....*....|...
gi 167887698  389 GN--QLPFVGFTY 399
Cdd:cd05616   309 RNidQSEFEGFSF 321
PH_ROCK cd01242
Rho-associated coiled-coil containing protein kinase pleckstrin homology (PH) domain; ROCK is ...
1119-1225 4.10e-57

Rho-associated coiled-coil containing protein kinase pleckstrin homology (PH) domain; ROCK is a serine/threonine kinase that binds GTP-Rho. It consists of a kinase domain, a coiled coil region and a PH domain. The ROCK PH domain is interrupted by a C1 domain. ROCK plays a role in cellular functions, such as contraction, adhesion, migration, and proliferation and in the regulation of apoptosis. There are two ROCK isoforms, ROCK1 and ROCK2. In ROCK2 the Rho Binding Domain (RBD) and the PH domain work together in membrane localization with RBD receiving the RhoA signal and the PH domain receiving the phospholipid signal. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269948  Cd Length: 110  Bit Score: 192.57  E-value: 4.10e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698 1119 SRIEGWLSVPNRGNIKRYGWKKQYVVVSSKKILFYNDEQDKEQSNPSMVLDIDKLFHVRPVTQGDVYRAETEEIPKIFQI 1198
Cdd:cd01242     1 SRLEGWLSLPNKQNIRRHGWKKQYVVVSSKKILFYNSEQDKANSNPILVLDIDKLFHVRSVTQGDVIRADAKEIPRIFQI 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 167887698 1199 LYANEGECRKDVEMEP---VQQAEKTNFQN 1225
Cdd:cd01242    81 LYANEGESSRPAEVTDtlsVSREEKPNTIL 110
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
76-313 6.74e-57

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: 197.81  E-value: 6.74e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLL-SKFEMIKRSDSAFFwEERDIMAFANSPWVVQLFYAFQDDRYLYMVME 154
Cdd:cd14014     2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLrPELAEDEEFRERFL-REARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDT 233
Cdd:cd14014    81 YVEGGSLADLLRERGpLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTGS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  234 AVGTPDYISPEVLKSQGGDGyygrECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLI 313
Cdd:cd14014   161 VLGTPAYMAPEQARGGPVDP----RSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAII 236
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
70-369 8.31e-57

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: 200.15  E-value: 8.31e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   70 RMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFA-NSPWVVQLFYAFQDDRY 148
Cdd:cd05619     1 KLTIEDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAwEHPFLTHLFCTFQTKEN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 LYMVMEYMPGGDL---VNLMSNYDVPEkwARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmKMNK 225
Cdd:cd05619    81 LFFVMEYLNGGDLmfhIQSCHKFDLPR--ATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMC-KENM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  226 EGMVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKImnHKNSLTFPddNDI 305
Cdd:cd05619   158 LGDAKTSTFCGTPDYIAPEILLGQK----YNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSI--RMDNPFYP--RWL 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  306 SKEAKN-LICAFLTDREVRLGRNGveEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFD 369
Cdd:cd05619   230 EKEAKDiLVKLFVREPERRLGVRG--DIRQHPFFREINWEALEEREIEPPFKPKVKSPFDCSNFD 292
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
75-338 1.23e-55

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: 193.96  E-value: 1.23e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLsKFEMIKRSDSAFfwEERDIMAFANSPWVVQLFYAFQDDRYLYMVME 154
Cdd:cd05122     1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKI-NLESKEKKESIL--NEIAILKKCKHPNIVKYYGSYLKKDELWIVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDLVNLMSNYDVP--EKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGmvRCD 232
Cdd:cd05122    78 FCSGGSLKDLLKNTNKTltEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGK--TRN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  233 TAVGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLYEMLVGDTPFYADslvgTYSKIM---NHKNSLTFPDDNDISKEA 309
Cdd:cd05122   156 TFVGTPYWMAPEVIQ----GKPYGFKADIWSLGITAIEMAEGKPPYSEL----PPMKALfliATNGPPGLRNPKKWSKEF 227
                         250       260       270
                  ....*....|....*....|....*....|
gi 167887698  310 KNLICAFLT-DREvrlGRNGVEEIKRHLFF 338
Cdd:cd05122   228 KDFLKKCLQkDPE---KRPTAEQLLKHPFI 254
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
80-369 1.28e-55

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: 196.87  E-value: 1.28e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfEMIKrSDSAFFWEERDIMAF---ANSPWVVQLFYAFQDDRYLYMVMEYM 156
Cdd:cd05588     1 RVIGRGSYAKVLMVELKKTKRIYAMKVIKK-ELVN-DDEDIDWVQTEKHVFetaSNHPFLVGLHSCFQTESRLFFVIEFV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  157 PGGDLVNLMSNY-DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmkmnKEGMVRCDTA- 234
Cdd:cd05588    79 NGGDLMFHMQRQrRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMC----KEGLRPGDTTs 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  235 --VGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFyaDSLVGTYSKIMNHKNSL-------TFPDDNDI 305
Cdd:cd05588   155 tfCGTPNYIAPEILRGED----YGFSVDWWALGVLMFEMLAGRSPF--DIVGSSDNPDQNTEDYLfqvilekPIRIPRSL 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  306 SKEAKNLICAFLT-DREVRLG---RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFD 369
Cdd:cd05588   229 SVKAASVLKGFLNkNPAERLGchpQTGFADIQSHPFFRTIDWEQLEQKQVTPPYKPRIESERDLENFD 296
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
80-369 6.08e-55

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: 194.42  E-value: 6.08e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIM-AFANSPWVVQLFYAFQDDRYLYMVMEYMPG 158
Cdd:cd05603     1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAERNVLlKNLKHPFLVGLHYSFQTSEKLYFVLDYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  159 GDL-VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmkmnKEGMVRCDTA--- 234
Cdd:cd05603    81 GELfFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLC----KEGMEPEETTstf 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  235 VGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnHKnSLTFPDDNDISkeAKNLIC 314
Cdd:cd05603   157 CGTPEYLAPEVLRKEP----YDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNIL-HK-PLHLPGGKTVA--ACDLLQ 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  315 AFL-TDREVRLG-RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFD 369
Cdd:cd05603   229 GLLhKDQRRRLGaKADFLEIKNHVFFSPINWDDLYHKRITPPYNPNVAGPADLRHFD 285
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
75-357 1.63e-54

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: 192.14  E-value: 1.63e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKS---TRKVYAMKLLSKFEMIKRSDSA-FFWEERDIMA-FANSPWVVQLFYAFQDDRYL 149
Cdd:cd05613     1 NFELLKVLGTGAYGKVFLVRKVSghdAGKLYAMKVLKKATIVQKAKTAeHTRTERQVLEhIRQSPFLVTLHYAFQTDTKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 YMVMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGM 228
Cdd:cd05613    81 HLILDYINGGELFTHLSQRErFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLDEN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  229 VRCDTAVGTPDYISPEVLKsqGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNH--KNSLTFPddNDIS 306
Cdd:cd05613   161 ERAYSFCGTIEYMAPEIVR--GGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRilKSEPPYP--QEMS 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 167887698  307 KEAKNLI-CAFLTDREVRL--GRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVP 357
Cdd:cd05613   237 ALAKDIIqRLLMKDPKKRLgcGPNGADEIKKHPFFQKINWDDLAAKKVPAPFKP 290
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
80-369 1.92e-54

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: 192.85  E-value: 1.92e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFA-NSPWVVQLFYAFQDDRYLYMVMEYMPG 158
Cdd:cd05620     1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVECTMVEKRVLALAwENPFLTHLYCTFQTKEHLFFVMEFLNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  159 GDLVnlmsnYDVPEKW------ARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmKMNKEGMVRCD 232
Cdd:cd05620    81 GDLM-----FHIQDKGrfdlyrATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMC-KENVFGDNRAS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  233 TAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKImnHKNSLTFPddNDISKEAKNL 312
Cdd:cd05620   155 TFCGTPDYIAPEILQGLK----YTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESI--RVDTPHYP--RWITKESKDI 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  313 ICAFLT-DREVRLGRNGveEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFD 369
Cdd:cd05620   227 LEKLFErDPTRRLGVVG--NIRGHPFFKTINWTALEKRELDPPFKPKVKSPSDYSNFD 282
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
82-335 4.74e-54

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: 190.07  E-value: 4.74e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAF-----------FWEERDIMAFANSPWVVQLFYAFQDD--RY 148
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRLRKRREGKNdrgkiknalddVRREIAIMKKLDHPNIVRLYEVIDDPesDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 LYMVMEYMPGGDLVNLMSNYDV---PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGtCMKMNK 225
Cdd:cd14008    81 LYLVLEYCEGGPVMELDSGDRVpplPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFG-VSEMFE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  226 EGMVRCDTAVGTPDYISPEVLKSqGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDdnDI 305
Cdd:cd14008   160 DGNDTLQKTAGTPAFLAPELCDG-DSKTYSGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFPIPP--EL 236
                         250       260       270
                  ....*....|....*....|....*....|.
gi 167887698  306 SKEAKNLICAFLT-DREVRLgrnGVEEIKRH 335
Cdd:cd14008   237 SPELKDLLRRMLEkDPEKRI---TLKEIKEH 264
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
70-399 6.14e-54

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: 192.52  E-value: 6.14e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   70 RMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSP-WVVQLFYAFQDDRY 148
Cdd:cd05615     6 RVRLTDFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMVEKRVLALQDKPpFLTQLHSCFQTVDR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 LYMVMEYMPGGDLV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEG 227
Cdd:cd05615    86 LYFVMEYVNGGDLMyHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVEG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  228 mVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHknSLTFPddNDISK 307
Cdd:cd05615   166 -VTTRTFCGTPDYIAPEIIAYQP----YGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEH--NVSYP--KSLSK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  308 EAKNLICAFLTDREVR---LGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDiDTSNFDDLEEdKGEEETFPIP 384
Cdd:cd05615   237 EAVSICKGLMTKHPAKrlgCGPEGERDIREHAFFRRIDWDKLENREIQPPFKPKVCGK-GAENFDKFFT-RGQPVLTPPD 314
                         330
                  ....*....|....*..
gi 167887698  385 KAFVGN--QLPFVGFTY 399
Cdd:cd05615   315 QLVIANidQADFEGFSY 331
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
70-387 8.17e-54

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: 192.22  E-value: 8.17e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   70 RMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYL 149
Cdd:cd05593    11 RKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 YMVMEYMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmkmnKEGM 228
Cdd:cd05593    91 CFVMEYVNGGELFFHLSRERVfSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC----KEGI 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  229 VRCDTA---VGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFPddNDI 305
Cdd:cd05593   167 TDAATMktfCGTPEYLAPEVLE----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL--MEDIKFP--RTL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  306 SKEAKNLICAFL-TDREVRL--GRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDdlEEDKGEEETFP 382
Cdd:cd05593   239 SADAKSLLSGLLiKDPNKRLggGPDDAKEIMRHSFFTGVNWQDVYDKKLVPPFKPQVTSETDTRYFD--EEFTAQTITIT 316

                  ....*
gi 167887698  383 IPKAF 387
Cdd:cd05593   317 PPEKY 321
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
67-374 4.31e-53

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 189.81  E-value: 4.31e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   67 RDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTR-KVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQD 145
Cdd:PTZ00426   23 RKNKMKYEDFNFIRTLGTGSFGRVILATYKNEDfPPVAIKRFEKSKIIKQKQVDHVFSERKILNYINHPFCVNLYGSFKD 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  146 DRYLYMVMEYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMN 224
Cdd:PTZ00426  103 ESYLYLVLEFVIGGEFFTfLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVD 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  225 kegmVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFPD--D 302
Cdd:PTZ00426  183 ----TRTYTLCGTPEYIAPEILLNVG----HGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKIL--EGIIYFPKflD 252
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887698  303 NDISKEAKNLICAFLTDREVRLgRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDDLEED 374
Cdd:PTZ00426  253 NNCKHLMKKLLSHDLTKRYGNL-KKGAQNVKEHPWFGNIDWVSLLHKNVEVPYKPKYKNVFDSSNFERVQED 323
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
70-370 6.66e-53

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: 189.86  E-value: 6.66e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   70 RMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYL 149
Cdd:cd05594    21 KVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 YMVMEYMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHS-MGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEG 227
Cdd:cd05594   101 CFVMEYANGGELFFHLSRERVfSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDG 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  228 MVRcDTAVGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFPddNDISK 307
Cdd:cd05594   181 ATM-KTFCGTPEYLAPEVLE----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL--MEEIRFP--RTLSP 251
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167887698  308 EAKNLICAFL-TDREVRL--GRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDD 370
Cdd:cd05594   252 EAKSLLSGLLkKDPKQRLggGPDDAKEIMQHKFFAGIVWQDVYEKKLVPPFKPQVTSETDTRYFDE 317
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
76-293 8.67e-53

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 193.31  E-value: 8.67e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSK-----FEMIKRsdsafFWEERDIMAFANSPWVVQLFYAFQDDRYLY 150
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPelaadPEARER-----FRREARALARLNHPNIVRVYDVGEEDGRPY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMV 229
Cdd:COG0515    84 LVMEYVEGESLADLLRRRGpLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLT 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167887698  230 RCDTAVGTPDYISPEVLKSQGGDGYYgrecDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNH 293
Cdd:COG0515   164 QTGTVVGTPGYMAPEQARGEPVDPRS----DVYSLGVTLYELLTGRPPFDGDSPAELLRAHLRE 223
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
74-338 1.25e-52

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: 185.45  E-value: 1.25e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd14099     1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLM-SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMvRCD 232
Cdd:cd14099    81 ELCSNGSLMELLkRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGE-RKK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  233 TAVGTPDYISPEVLKSQGGDGYygrECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKImnHKNSLTFPDDNDISKEAKNL 312
Cdd:cd14099   160 TLCGTPNYIAPEVLEKKKGHSF---EVDIWSLGVILYTLLVGKPPFETSDVKETYKRI--KKNEYSFPSHLSISDEAKDL 234
                         250       260
                  ....*....|....*....|....*.
gi 167887698  313 ICAFLTDREVRlgRNGVEEIKRHLFF 338
Cdd:cd14099   235 IRSMLQPDPTK--RPSLDEILSHPFF 258
C1_ROCK1 cd20874
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing ...
1222-1290 1.29e-52

protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing protein kinase 1 (ROCK1) and similar proteins; ROCK1 is a serine/threonine kinase, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1, also called Rho-associated protein kinase 1, renal carcinoma antigen NY-REN-35, Rho-associated, coiled-coil-containing protein kinase I (ROCK-I), p160 ROCK-1, or p160ROCK, 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 proteins contain 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), a pleckstrin homology (PH) domain and a C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410424  Cd Length: 69  Bit Score: 178.29  E-value: 1.29e-52
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167887698 1222 NFQNHKGHEFIPTLYHFPANCDACAKPLWHVFKPPPALECRRCHVKCHRDHLDKKEDLICPCKVSYDVT 1290
Cdd:cd20874     1 NFLPHKGHEFIPTLYHFPANCEACAKPLWHVFKPPPALECRRCHVKCHKDHLDKKEDMITPCKVNYDVT 69
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
82-271 2.27e-51

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: 180.16  E-value: 2.27e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDsaFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLLE--ELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNYD--VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPD 239
Cdd:cd00180    79 KDLLKENKgpLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGGTTPP 158
                         170       180       190
                  ....*....|....*....|....*....|..
gi 167887698  240 YISPEVLKSQggdGYYGRECDWWSVGVFLYEM 271
Cdd:cd00180   159 YYAPPELLGG---RYYGPKVDIWSLGVILYEL 187
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
82-358 9.98e-51

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: 180.80  E-value: 9.98e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNYD---VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMnKEGMvRCDTAVGTP 238
Cdd:cd05577    81 KYHIYNVGtrgFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEF-KGGK-KIKGRVGTH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  239 DYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPF--YADSLVGTYSKIMNHKNSLTFPDDNdiSKEAKNLICAF 316
Cdd:cd05577   159 GYMAPEVLQ---KEVAYDFSVDWFALGCMLYEMIAGRSPFrqRKEKVDKEELKRRTLEMAVEYPDSF--SPEARSLCEGL 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 167887698  317 LT-DREVRLG--RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPD 358
Cdd:cd05577   234 LQkDPERRLGcrGGSADEVKEHPFFRSLNWQRLEAGMLEPPFVPD 278
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
74-369 1.59e-50

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: 183.31  E-value: 1.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfEMIKrSDSAFFWEERDIMAF---ANSPWVVQLFYAFQDDRYLY 150
Cdd:cd05618    20 QDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKK-ELVN-DDEDIDWVQTEKHVFeqaSNHPFLVGLHSCFQTESRLF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGGDLV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmkmnKEGMV 229
Cdd:cd05618    98 FVIEYVNGGDLMfHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMC----KEGLR 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  230 RCDTA---VGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFyadSLVGTYSKIMNHKNSLTFP------ 300
Cdd:cd05618   174 PGDTTstfCGTPNYIAPEILRGED----YGFSVDWWALGVLMFEMMAGRSPF---DIVGSSDNPDQNTEDYLFQvilekq 246
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  301 --DDNDISKEAKNLICAFL-TDREVRLG---RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFD 369
Cdd:cd05618   247 irIPRSLSVKAASVLKSFLnKDPKERLGchpQTGFADIQGHPFFRNVDWDLMEQKQVVPPFKPNISGEFGLDNFD 321
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
74-369 3.60e-50

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: 182.14  E-value: 3.60e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANS-PWVVQLFYAFQDDRYLYMV 152
Cdd:cd05617    15 QDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSnPFLVGLHSCFQTTSRLFLV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGGDLV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmkmnKEGMVRC 231
Cdd:cd05617    95 IEYVNGGDLMfHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMC----KEGLGPG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  232 DTA---VGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYadslVGTYSKIMNHKNSL-------TFPD 301
Cdd:cd05617   171 DTTstfCGTPNYIAPEILRGEE----YGFSVDWWALGVLMFEMMAGRSPFD----IITDNPDMNTEDYLfqvilekPIRI 242
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887698  302 DNDISKEAKNLICAFLT-DREVRLG---RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFD 369
Cdd:cd05617   243 PRFLSVKASHVLKGFLNkDPKERLGcqpQTGFSDIKSHTFFRSIDWDLLEKKQVTPPFKPQITDDYGLENFD 314
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
75-313 9.42e-50

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: 177.33  E-value: 9.42e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLsKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVME 154
Cdd:cd06606     1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKEV-ELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCD- 232
Cdd:cd06606    80 YVPGGSLASLLKKFGkLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIATGEGTk 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  233 TAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYA-DSLVGTYSKIMNHKNSLTFPDdnDISKEAKN 311
Cdd:cd06606   160 SLRGTPYWMAPEVIRGEG----YGRAADIWSLGCTVIEMATGKPPWSElGNPVAALFKIGSSGEPPPIPE--HLSEEAKD 233

                  ..
gi 167887698  312 LI 313
Cdd:cd06606   234 FL 235
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
75-313 2.29e-49

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: 176.11  E-value: 2.29e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRS-DSAFFweERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd08215     1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKErEEALN--EVKLLSKLKHPNIVKYYESFEENGKLCIVM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYDV-----PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTC-MKMNKEG 227
Cdd:cd08215    79 EYADGGDLAQKIKKQKKkgqpfPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISkVLESTTD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  228 MVRcdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNhknsLTFPDDNDI-S 306
Cdd:cd08215   159 LAK--TVVGTPYYLSPELCENKP----YNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVK----GQYPPIPSQyS 228

                  ....*..
gi 167887698  307 KEAKNLI 313
Cdd:cd08215   229 SELRDLV 235
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
80-344 1.09e-48

Catalytic domain of G protein-coupled Receptor Kinase 4-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 GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. 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 GRK4-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: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 175.24  E-value: 1.09e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 159
Cdd:cd05605     6 RVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTIMNGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DL---VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRcdTAVG 236
Cdd:cd05605    86 DLkfhIYNMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGETIR--GRVG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  237 TPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAF 316
Cdd:cd05605   164 TVGYMAPEVVKNE----RYTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKREEVDRRVKEDQEEYSEKFSEEAKSICSQL 239
                         250       260       270
                  ....*....|....*....|....*....|.
gi 167887698  317 LT-DREVRLG--RNGVEEIKRHLFFKNDQWA 344
Cdd:cd05605   240 LQkDPKTRLGcrGEGAEDVKSHPFFKSINFK 270
Pkinase pfam00069
Protein kinase domain;
76-338 1.53e-48

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 172.43  E-value: 1.53e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698    76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFfWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNI-LREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   156 MPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMgfihrdvkpdnmlldksghlkladfgtcmkmnkegmvrcDTA 234
Cdd:pfam00069   80 VEGGSLFDLLSEKGAfSEREAKFIMKQILEGLESGSSL---------------------------------------TTF 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   235 VGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNdISKEAKNLIC 314
Cdd:pfam00069  121 VGTPWYMAPEVLGGNP----YGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSN-LSEEAKDLLK 195
                          250       260
                   ....*....|....*....|....*
gi 167887698   315 AFLT-DREVRLgrnGVEEIKRHLFF 338
Cdd:pfam00069  196 KLLKkDPSKRL---TATQALQHPWF 217
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
75-335 2.97e-48

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: 172.97  E-value: 2.97e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVME 154
Cdd:cd14663     1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGMVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG-TCMKMNKEGMVRCD 232
Cdd:cd14663    81 LVTGGELFSkIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGlSALSEQFRQDGLLH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  233 TAVGTPDYISPEVLKSqggDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFPddNDISKEAKNL 312
Cdd:cd14663   161 TTCGTPNYVAPEVLAR---RGYDGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIM--KGEFEYP--RWFSPGAKSL 233
                         250       260
                  ....*....|....*....|...
gi 167887698  313 ICAFLTDREVRlgRNGVEEIKRH 335
Cdd:cd14663   234 IKRILDPNPST--RITVEQIMAS 254
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
82-335 8.37e-48

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: 172.16  E-value: 8.37e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSdsAFF----------------------WEERDIMAFANSPWVVQL 139
Cdd:cd14118     2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKLLKQA--GFFrrppprrkpgalgkpldpldrvYREIAILKKLDHPNVVKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  140 FYAFQD--DRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADF 217
Cdd:cd14118    80 VEVLDDpnEDNLYMVFELVDKGAVMEVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  218 GTCMKMNKEGMVRCDTAvGTPDYISPEVLkSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNhkNSL 297
Cdd:cd14118   160 GVSNEFEGDDALLSSTA-GTPAFMAPEAL-SESRKKFSGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKT--DPV 235
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 167887698  298 TFPDDNDISKEAKNLICAFLT-DREVRLgrnGVEEIKRH 335
Cdd:cd14118   236 VFPDDPVVSEQLKDLILRMLDkNPSERI---TLPEIKEH 271
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
82-337 1.68e-47

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: 170.48  E-value: 1.68e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFwEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKLQENLE-SEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH---LKLADFGTCMKMNKEGMVrcDTAVGT 237
Cdd:cd14009    80 SQYIRKRGrLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDdpvLKIADFGFARSLQPASMA--ETLCGS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  238 PDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFL 317
Cdd:cd14009   158 PLYMAPEILQFQ----KYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPFPIAAQLSPDCKDLLRRLL 233
                         250       260
                  ....*....|....*....|
gi 167887698  318 TDREVRlgRNGVEEIKRHLF 337
Cdd:cd14009   234 RRDPAE--RISFEEFFAHPF 251
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
76-338 2.94e-47

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: 170.13  E-value: 2.94e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd14081     3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGtcMKMNKEGMVRCDTA 234
Cdd:cd14081    83 VSGGELFDyLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFG--MASLQPEGSLLETS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  235 VGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnsLTFPDdnDISKEAKNLIC 314
Cdd:cd14081   161 CGSPHYACPEVIK---GEKYDGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGV--FHIPH--FISPDAQDLLR 233
                         250       260
                  ....*....|....*....|....*
gi 167887698  315 AFLT-DREVRLgrnGVEEIKRHLFF 338
Cdd:cd14081   234 RMLEvNPEKRI---TIEEIKKHPWF 255
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
74-313 6.02e-47

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: 169.31  E-value: 6.02e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMK---LLSKFEMIKRSDSaffweERDIMAFANSPWVVQLFYAFQDDRYLY 150
Cdd:cd06623     1 SDLERVKVLGQGSSGVVYKVRHKPTGKIYALKkihVDGDEEFRKQLLR-----ELKTLRSCESPYVVKCYGAFYKEGEIS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGGDLVNLM-SNYDVPEKWARFYTAEVVLALDAIHSM-GFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKeGM 228
Cdd:cd06623    76 IVLEYMDGGSLADLLkKVGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGEVKIADFGISKVLEN-TL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  229 VRCDTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFyADSLVGTYSKIMNHKNS--LTFPDDNDIS 306
Cdd:cd06623   155 DQCNTFVGTVTYMSPERIQGE----SYSYAADIWSLGLTLLECALGKFPF-LPPGQPSFFELMQAICDgpPPSLPAEEFS 229

                  ....*..
gi 167887698  307 KEAKNLI 313
Cdd:cd06623   230 PEFRDFI 236
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
74-338 2.45e-46

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: 167.51  E-value: 2.45e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFfWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd14069     1 EDWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPENI-KKEVCIQKMLSHKNVVRFYGHRREGEFQYLFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMS-NYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVR-C 231
Cdd:cd14069    80 EYASGGELFDKIEpDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFRYKGKERlL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  232 DTAVGTPDYISPEVLKSQggdGYYGRECDWWSVGVFLYEMLVGDTPF-YADSLVGTYSKIMNHKNSLTFPdDNDISKEAK 310
Cdd:cd14069   160 NKMCGTLPYVAPELLAKK---KYRAEPVDVWSCGIVLFAMLAGELPWdQPSDSCQEYSDWKENKKTYLTP-WKKIDTAAL 235
                         250       260
                  ....*....|....*....|....*...
gi 167887698  311 NLICAFLTDREVRlgRNGVEEIKRHLFF 338
Cdd:cd14069   236 SLLRKILTENPNK--RITIEDIKKHPWY 261
C1_ROCK2 cd20875
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing ...
1219-1288 2.11e-45

protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing protein kinase 2 (ROCK2) and similar proteins; ROCK2 is a serine/threonine kinase, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2, also called Rho-associated protein kinase 2, Rho kinase 2, Rho-associated, coiled-coil-containing protein kinase II (ROCK-II), or p164 ROCK-2, 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 proteins contain 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), a pleckstrin homology (PH) domain and a C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410425  Cd Length: 71  Bit Score: 157.50  E-value: 2.11e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698 1219 EKTNFQNHKGHEFIPTLYHFPANCDACAKPLWHVFKPPPALECRRCHVKCHRDHLDKKEDLICPCKVSYD 1288
Cdd:cd20875     2 EKSNYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVNYD 71
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
75-318 5.78e-45

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: 163.80  E-value: 5.78e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMI-KRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd14098     1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAgNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSG--HLKLADFGTCmKMNKEGMVr 230
Cdd:cd14098    81 EYVEGGDLMDfIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGLA-KVIHTGTF- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  231 CDTAVGTPDYISPEVLKS--QGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKImnHKNSLTFPDDND--IS 306
Cdd:cd14098   159 LVTFCGTMAYLAPEILMSkeQNLQGGYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRI--RKGRYTQPPLVDfnIS 236
                         250
                  ....*....|..
gi 167887698  307 KEAKNLICAFLT 318
Cdd:cd14098   237 EEAIDFILRLLD 248
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
81-357 3.54e-44

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: 161.84  E-value: 3.54e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   81 VIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFAN----SPWVVQLFYAFQDDRYLYMVMEYM 156
Cdd:cd05606     1 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVStggdCPFIVCMTYAFQTPDKLCFILDLM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  157 PGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEgmvRCDTAV 235
Cdd:cd05606    81 NGGDLHYHLSQHGVfSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDFSKK---KPHASV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  236 GTPDYISPEVLkSQGgdGYYGRECDWWSVGVFLYEMLVGDTPFYADSlvgTYSKIMNHKNSLT----FPDdnDISKEAKN 311
Cdd:cd05606   158 GTHGYMAPEVL-QKG--VAYDSSADWFSLGCMLYKLLKGHSPFRQHK---TKDKHEIDRMTLTmnveLPD--SFSPELKS 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 167887698  312 LICAFLT-DREVRLG--RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVP 357
Cdd:cd05606   230 LLEGLLQrDVSKRLGclGRGATEVKEHPFFKGVDWQQVYLQKYPPPLIP 278
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
67-335 9.50e-44

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: 160.64  E-value: 9.50e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   67 RDLRMKaedYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfEMIKRSDSAFFWEERD------IMAFANSPWVVQLF 140
Cdd:cd14084     2 KELRKK---YIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINK-RKFTIGSRREINKPRNieteieILKKLSHPCIIKIE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  141 YAFQDDRYLYMVMEYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLdkSGH-----LKL 214
Cdd:cd14084    78 DFFDAEDDYYIVLELMEGGELFDrVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLL--SSQeeeclIKI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  215 ADFGTCMKMNKEGMVRcdTAVGTPDYISPEVLKSQGGDGyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSK-IMNH 293
Cdd:cd14084   156 TDFGLSKILGETSLMK--TLCGTPTYLAPEVLRSFGTEG-YTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLKEqILSG 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 167887698  294 KNSLTFPDDNDISKEAKNLICAFLT-DREVRLgrnGVEEIKRH 335
Cdd:cd14084   233 KYTFIPKAWKNVSEEAKDLVKKMLVvDPSRRP---SIEEALEH 272
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
82-318 3.39e-43

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: 158.20  E-value: 3.39e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAffweERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDKKKEAVLR----EISILNQLQHPRIIQLHEAYESPTELVLILELCSGGEL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD--KSGHLKLADFGTCMKMNKEGMVRCDTavGTP 238
Cdd:cd14006    77 LDrLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLAdrPSPQIKIIDFGLARKLNPGEELKEIF--GTP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  239 DYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLT 318
Cdd:cd14006   155 EFVAPEIVNGEP----VSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFSEEYFSSVSQEAKDFIRKLLV 230
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
76-338 7.88e-43

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: 157.46  E-value: 7.88e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQL---VRHKstRKVyAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMV 152
Cdd:cd14162     2 YIVGKTLGHGSYAVVKKaysTKHK--CKV-AIKIVSKKKAPEDYLQKFLPREIEVIKGLKHPNLICFYEAIETTSRVYII 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGGDLVNLM-SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG---TCMKMNKEGM 228
Cdd:cd14162    79 MELAENGDLLDYIrKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGfarGVMKTKDGKP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  229 VRCDTAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVgtysKIMNH-KNSLTFPDDNDISK 307
Cdd:cd14162   159 KLSETYCGSYAYASPEILR---GIPYDPFLSDIWSMGVVLYTMVYGRLPFDDSNLK----VLLKQvQRRVVFPKNPTVSE 231
                         250       260       270
                  ....*....|....*....|....*....|.
gi 167887698  308 EAKNLICAFLTDREVRLgrnGVEEIKRHLFF 338
Cdd:cd14162   232 ECKDLILRMLSPVKKRI---TIEEIKRDPWF 259
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
80-358 2.23e-42

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: 156.97  E-value: 2.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 159
Cdd:cd05608     7 RVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMNGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DLVNLMSNYD-----VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMnKEGMVRCDTA 234
Cdd:cd05608    87 DLRYHIYNVDeenpgFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVEL-KDGQTKTKGY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  235 VGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYADSlvgtySKIMNHK-------NSLTFPDdnDISK 307
Cdd:cd05608   166 AGTPGFMAPELLLGE----EYDYSVDYFTLGVTLYEMIAARGPFRARG-----EKVENKElkqrilnDSVTYSE--KFSP 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  308 EAKNlICAFLTDREV--RLG-RNG-VEEIKRHLFFKNDQWAWETLRDTVAPVVPD 358
Cdd:cd05608   235 ASKS-ICEALLAKDPekRLGfRDGnCDGLRTHPFFRDINWRKLEAGILPPPFVPD 288
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
75-313 5.19e-42

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: 156.25  E-value: 5.19e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfemIKRSDSaffwEERDI-MAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd14091     1 EYEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDK---SKRDPS----EEIEIlLRYGQHPNIITLRDVYDDGNSVYLVT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL-DKSGH---LKLADFGTCMKMNKEG- 227
Cdd:cd14091    74 ELLRGGELLDrILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYaDESGDpesLRICDFGFAKQLRAENg 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  228 --MVRCDTAvgtpDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYA---DSLVGTYSKIMNHKNSLTFPDD 302
Cdd:cd14091   154 llMTPCYTA----NFVAPEVLKKQG----YDAACDIWSLGVLLYTMLAGYTPFASgpnDTPEVILARIGSGKIDLSGGNW 225
                         250
                  ....*....|.
gi 167887698  303 NDISKEAKNLI 313
Cdd:cd14091   226 DHVSDSAKDLV 236
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
74-325 6.90e-42

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: 154.33  E-value: 6.90e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfemIKRSDS--AFFWEERDIMAFANSPWVVQLFYAFQDDRYLYM 151
Cdd:cd14002     1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPK---RGKSEKelRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  152 VMEYMPGgDLVNLMS-NYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNkegmvr 230
Cdd:cd14002    78 VTEYAQG-ELFQILEdDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMS------ 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  231 CDTAV-----GTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFPDdnDI 305
Cdd:cd14002   151 CNTLVltsikGTPLYMAPELVQEQP----YDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIV--KDPVKWPS--NM 222
                         250       260
                  ....*....|....*....|.
gi 167887698  306 SKEAKNLICAFLT-DREVRLG 325
Cdd:cd14002   223 SPEFKSFLQGLLNkDPSKRLS 243
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
76-324 1.03e-41

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: 154.02  E-value: 1.03e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFE------MIKrsdsaffwEERDIMAFANSPWVVQLFYAFQDDRYL 149
Cdd:cd14095     2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKckgkehMIE--------NEVAILRRVKHPNIVQLIEEYDTDTEL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 YMVMEYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL----DKSGHLKLADFGTCMKMN 224
Cdd:cd14095    74 YLVMELVKGGDLFDaITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVveheDGSKSLKLADFGLATEVK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  225 KEGMVRCdtavGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYA-----DSLvgtYSKIMNHKNSLTF 299
Cdd:cd14095   154 EPLFTVC----GTPTYVAPEILAETG----YGLKVDIWAAGVITYILLCGFPPFRSpdrdqEEL---FDLILAGEFEFLS 222
                         250       260
                  ....*....|....*....|....*.
gi 167887698  300 PDDNDISKEAKNLI-CAFLTDREVRL 324
Cdd:cd14095   223 PYWDNISDSAKDLIsRMLVVDPEKRY 248
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
76-294 1.04e-41

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: 154.08  E-value: 1.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEM------IKRsdsaffweERDIMAFANSPWVVQLFYAFQDDRYL 149
Cdd:cd14078     5 YELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKALgddlprVKT--------EIEALKNLSHQHICRLYHVIETDNKI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 YMVMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKmNKEGM 228
Cdd:cd14078    77 FMVLEYCPGGELFDYIVAKDrLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAK-PKGGM 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  229 -VRCDTAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHK 294
Cdd:cd14078   156 dHHLETCCGSPAYAAPELIQ---GKPYIGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGK 219
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
75-291 2.38e-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: 152.93  E-value: 2.38e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKL--LSKFEMIKRSDSAffwEERDIMAFANSPWVVQLFYAFQDDRYLYMV 152
Cdd:cd08530     1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEvnLGSLSQKEREDSV---NEIRLLASVNHPNIIRYKEAFLDGNRLCIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGGDLVNLMSNYD-----VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmKMNKEG 227
Cdd:cd08530    78 MEYAPFGDLSKLISKRKkkrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGIS-KVLKKN 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167887698  228 MVRcdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIM 291
Cdd:cd08530   157 LAK--TQIGTPLYAAPEVWKGRP----YDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVC 214
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
82-278 5.48e-41

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: 151.54  E-value: 5.48e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTrKVyAMKLLsKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd13999     1 IGSGSFGEVYKGKWRGT-DV-AIKKL-KVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNYDVPEKWARFytaeVVLALDA------IHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRcDTAV 235
Cdd:cd13999    78 YDLLHKKKIPLSWSLR----LKIALDIargmnyLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKM-TGVV 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 167887698  236 GTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd13999   153 GTPRWMAPEVLRGEP----YTEKADVYSFGIVLWELLTGEVPF 191
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
76-335 6.81e-41

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: 151.95  E-value: 6.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLV--RHKSTRKVYAMKLLSKF----EMIKRsdsaFFWEERDIMAFANSPWVVQLFYAFQDDRYL 149
Cdd:cd14080     2 YRLGKTIGEGSYSKVKLAeyTKSGLKEKVACKIIDKKkapkDFLEK----FLPRELEILRKLRHPNIIQVYSIFERGSKV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 YMVMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG---TCMKmnK 225
Cdd:cd14080    78 FIFMEYAEHGDLLEYIQKRGaLSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGfarLCPD--D 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  226 EGMVRCDTAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnsLTFP-DDND 304
Cdd:cd14080   156 DGDVLSKTFCGSAAYAAPEILQ---GIPYDPKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRK--VRFPsSVKK 230
                         250       260       270
                  ....*....|....*....|....*....|..
gi 167887698  305 ISKEAKNLICAFLT-DREVRLgrnGVEEIKRH 335
Cdd:cd14080   231 LSPECKDLIDQLLEpDPTKRA---TIEEILNH 259
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
80-358 8.33e-41

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. 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 GRK5 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: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 153.59  E-value: 8.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 159
Cdd:cd05632     8 RVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DL---VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRcdTAVG 236
Cdd:cd05632    88 DLkfhIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGESIR--GRVG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  237 TPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAF 316
Cdd:cd05632   166 TVGYMAPEVLNNQ----RYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETEEVYSAKFSEEAKSICKML 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 167887698  317 LT-DREVRLG--RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPD 358
Cdd:cd05632   242 LTkDPKQRLGcqEEGAGEVKRHPFFRNMNFKRLEAGMLDPPFVPD 286
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
76-339 1.66e-40

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: 150.44  E-value: 1.66e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllsKFEMIKRSDSAFFWEERdIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd06614     2 YKNLEKIGEGASGEVYKATDRATGKEVAIK---KMRLRKQNKELIINEIL-IMKECKHPNIVDYYDSYLVGDELWVVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVNLMSNYDVP--EKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRcDT 233
Cdd:cd06614    78 MDGGSLTDIITQNPVRmnESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKR-NS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  234 AVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNhKNSLTFPDDNDISKEAKNLI 313
Cdd:cd06614   157 VVGTPYWMAPEVIKRKD----YGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITT-KGIPPLKNPEKWSPEFKDFL 231
                         250       260
                  ....*....|....*....|....*.
gi 167887698  314 cAFLTDREVRLgRNGVEEIKRHLFFK 339
Cdd:cd06614   232 -NKCLVKDPEK-RPSAEELLQHPFLK 255
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
80-340 1.71e-40

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. 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 GRK7 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: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 151.60  E-value: 1.71e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 159
Cdd:cd05607     8 RVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALLEKEILEKVNSPFIVSLAYAFETKTHLCLVMSLMNGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DLVNLMsnYDVPEKWAR-----FYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMnKEGMVRCDTA 234
Cdd:cd05607    88 DLKYHI--YNVGERGIEmerviFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEV-KEGKPITQRA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  235 vGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPF--YADSLVGTYSKIMNHKNSLTFPDDNdISKEAKNL 312
Cdd:cd05607   165 -GTNGYMAPEILKEES----YSYPVDWFAMGCSIYEMVAGRTPFrdHKEKVSKEELKRRTLEDEVKFEHQN-FTEEAKDI 238
                         250       260       270
                  ....*....|....*....|....*....|
gi 167887698  313 ICAFLTDR-EVRLG-RNGVEEIKRHLFFKN 340
Cdd:cd05607   239 CRLFLAKKpENRLGsRTNDDDPRKHEFFKS 268
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
80-340 1.72e-40

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: 151.71  E-value: 1.72e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 159
Cdd:cd05630     6 RVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DL---VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRcdTAVG 236
Cdd:cd05630    86 DLkfhIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIK--GRVG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  237 TPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLiCAF 316
Cdd:cd05630   164 TVGYMAPEVVKNE----RYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSEKFSPQARSL-CSM 238
                         250       260
                  ....*....|....*....|....*...
gi 167887698  317 L--TDREVRLGRNG--VEEIKRHLFFKN 340
Cdd:cd05630   239 LlcKDPAERLGCRGggAREVKEHPLFKK 266
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
80-358 5.50e-40

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. 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 GRK4 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: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 150.14  E-value: 5.50e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 159
Cdd:cd05631     6 RVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEKVNSRFVVSLAYAYETKDALCLVLTIMNGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DL---VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRcdTAVG 236
Cdd:cd05631    86 DLkfhIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPEGETVR--GRVG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  237 TPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNlICAF 316
Cdd:cd05631   164 TVGYMAPEVINNEK----YTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEVDRRVKEDQEEYSEKFSEDAKS-ICRM 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 167887698  317 L--TDREVRLG--RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPD 358
Cdd:cd05631   239 LltKNPKERLGcrGNGAAGVKQHPIFKNINFKRLEANMLEPPFCPD 284
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
76-314 1.24e-39

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: 148.29  E-value: 1.24e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd14083     5 YEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKEDS--LENEIAVLRKIKHPNIVQLLDIYESKSHLYLVMEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNML---LDKSGHLKLADFGTCmKMNKEGMVrc 231
Cdd:cd14083    83 VTGGELFDrIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFGLS-KMEDSGVM-- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  232 DTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKN 311
Cdd:cd14083   160 STACGTPGYVAPEVLAQKP----YGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFDSPYWDDISDSAKD 235

                  ...
gi 167887698  312 LIC 314
Cdd:cd14083   236 FIR 238
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
71-376 6.57e-39

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: 149.06  E-value: 6.57e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   71 MKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANS---PWVVQLFYAFQDDR 147
Cdd:cd05633     2 LTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTPD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  148 YLYMVMEYMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKE 226
Cdd:cd05633    82 KLCFILDLMNGGDLHYHLSQHGVfSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSKK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  227 gmvRCDTAVGTPDYISPEVLksQGGDGyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYS-KIMNHKNSLTFPDdnDI 305
Cdd:cd05633   162 ---KPHASVGTHGYMAPEVL--QKGTA-YDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEiDRMTLTVNVELPD--SF 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167887698  306 SKEAKNLICAFLT-DREVRLG--RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVP-----DLSSDIDTSNFDDlEEDKG 376
Cdd:cd05633   234 SPELKSLLEGLLQrDVSKRLGchGRGAQEVKEHSFFKGIDWQQVYLQKYPPPLIPprgevNAADAFDIGSFDE-EDTKG 311
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
75-376 1.20e-38

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: 147.50  E-value: 1.20e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANS---PWVVQLFYAFQDDRYLYM 151
Cdd:cd14223     1 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTgdcPFIVCMSYAFHTPDKLSF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  152 VMEYMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEgmvR 230
Cdd:cd14223    81 ILDLMNGGDLHYHLSQHGVfSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKK---K 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  231 CDTAVGTPDYISPEVLKSQGGdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYS-KIMNHKNSLTFPDdnDISKEA 309
Cdd:cd14223   158 PHASVGTHGYMAPEVLQKGVA---YDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEiDRMTLTMAVELPD--SFSPEL 232
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  310 KNLICAFLT-DREVRLG--RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVP-----DLSSDIDTSNFDDlEEDKG 376
Cdd:cd14223   233 RSLLEGLLQrDVNRRLGcmGRGAQEVKEEPFFRGLDWQMVFLQKYPPPLIPprgevNAADAFDIGSFDE-EDTKG 306
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
74-317 1.30e-38

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: 145.10  E-value: 1.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd14116     5 EDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLIL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDL---VNLMSNYDvpEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEgmvR 230
Cdd:cd14116    85 EYAPLGTVyreLQKLSKFD--EQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSS---R 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  231 CDTAVGTPDYISPEVLKSQGGDgyygRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKImnHKNSLTFPDdnDISKEAK 310
Cdd:cd14116   160 RTTLCGTLDYLPPEMIEGRMHD----EKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRI--SRVEFTFPD--FVTEGAR 231

                  ....*..
gi 167887698  311 NLICAFL 317
Cdd:cd14116   232 DLISRLL 238
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
76-323 1.89e-38

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: 144.71  E-value: 1.89e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDsaFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd14185     2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKED--MIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL----DKSGHLKLADFGTCMKMNKEGMVR 230
Cdd:cd14185    80 VRGGDLFDaIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKYVTGPIFTV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  231 CdtavGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYA-----DSLvgtYSKIMNHKNSLTFPDDNDI 305
Cdd:cd14185   160 C----GTPTYVAPEILSEKG----YGLEVDMWAAGVILYILLCGFPPFRSperdqEEL---FQIIQLGHYEFLPPYWDNI 228
                         250
                  ....*....|....*....
gi 167887698  306 SKEAKNLICAFLT-DREVR 323
Cdd:cd14185   229 SEAAKDLISRLLVvDPEKR 247
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
76-317 2.81e-38

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: 144.20  E-value: 2.81e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERdIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd14072     2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVR-IMKILNHPNIVKLFEVIETEKTLYLVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGmvRCDTA 234
Cdd:cd14072    81 ASGGEVFDyLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPGN--KLDTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  235 VGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPddndISKEAKNLIC 314
Cdd:cd14072   159 CGSPPYAAPELFQ---GKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFY----MSTDCENLLK 231

                  ...
gi 167887698  315 AFL 317
Cdd:cd14072   232 KFL 234
C1_ROCK cd20813
protein kinase C conserved region 1 (C1 domain) found in the Rho-associated coiled-coil ...
1225-1286 5.09e-38

protein kinase C conserved region 1 (C1 domain) found in the Rho-associated coiled-coil containing protein kinase (ROCK) family; ROCK is a serine/threonine protein kinase, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. It 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 C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD), a pleckstrin homology (PH) domain and a C1 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. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410363  Cd Length: 65  Bit Score: 136.25  E-value: 5.09e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887698 1225 NHKGHEFIPTLYHFPANCDACAKPLWHVFKPPPALECRRCHVKCHRDHLDKKEDLICPCKVS 1286
Cdd:cd20813     4 SHKGHEFVEITFHMPTTCDVCHKPLWHLFKPPPALECKRCRMKIHKDHVDKEEYFIPPCKVN 65
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
74-338 8.19e-38

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: 143.26  E-value: 8.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLskfEMIKRSDSAFFWE--------ERDIM-AFANSPWVVQLFYAFQ 144
Cdd:cd14093     3 AKYEPKEILGRGVSSTVRRCIEKETGQEFAVKII---DITGEKSSENEAEelreatrrEIEILrQVSGHPNIIELHDVFE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  145 DDRYLYMVMEYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKM 223
Cdd:cd14093    80 SPTFIFLVFELCRKGELFDyLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  224 NKEGMVRcdTAVGTPDYISPEVLKSQGGDGY--YGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPD 301
Cdd:cd14093   160 DEGEKLR--ELCGTPGYLAPEVLKCSMYDNApgYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFGSPE 237
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 167887698  302 DNDISKEAKNLICAFLT-DREVRLgrnGVEEIKRHLFF 338
Cdd:cd14093   238 WDDISDTAKDLISKLLVvDPKKRL---TAEEALEHPFF 272
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
74-318 9.96e-38

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: 143.73  E-value: 9.96e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEV-QLVRHKSTRKVYAMKLLSKFEM----IKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRY 148
Cdd:cd14096     1 ENYRLINKIGEGAFSNVyKAVPLRNTGKPVAIKVVRKADLssdnLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 LYMVMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD------------KS------ 209
Cdd:cd14096    81 YYIVLELADGGEIFHQIVRLTyFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEpipfipsivklrKAdddetk 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  210 ---------------GHLKLADFGTCMKM-NKEGMVRCdtavGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLYEMLV 273
Cdd:cd14096   161 vdegefipgvggggiGIVKLADFGLSKQVwDSNTKTPC----GTVGYTAPEVVK----DERYSKKVDMWALGCVLYTLLC 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 167887698  274 GDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLT 318
Cdd:cd14096   233 GFPPFYDESIETLTEKISRGDYTFLSPWWDEISKSAKDLISHLLT 277
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
76-278 2.99e-37

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: 140.99  E-value: 2.99e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd14073     3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVNLMSN-YDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRcdTA 234
Cdd:cd14073    83 ASGGELYDYISErRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLYSKDKLLQ--TF 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 167887698  235 VGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd14073   161 CGSPLYASPEIVN---GTPYQGPEVDCWSLGVLLYTLVYGTMPF 201
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
76-335 4.81e-37

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: 141.63  E-value: 4.81e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIK----------RSDSAFFWEERDIMAFANSPW---------- 135
Cdd:cd14200     2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKLLKqygfprrpppRGSKAAQGEQAKPLAPLERVYqeiailkkld 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  136 ---VVQLFYAFQD--DRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSG 210
Cdd:cd14200    82 hvnIVKLIEVLDDpaEDNLYMVFDLLRKGPVMEVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  211 HLKLADFGTCMKMNKEGMVRCDTAvGTPDYISPEVLkSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKI 290
Cdd:cd14200   162 HVKIADFGVSNQFEGNDALLSSTA-GTPAFMAPETL-SDSGQSFSGKALDVWAMGVTLYCFVYGKCPFIDEFILALHNKI 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 167887698  291 MNhkNSLTFPDDNDISKEAKNLICAFLTDR-EVRLgrnGVEEIKRH 335
Cdd:cd14200   240 KN--KPVEFPEEPEISEELKDLILKMLDKNpETRI---TVPEIKVH 280
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
75-290 5.84e-37

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: 140.75  E-value: 5.84e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFwEERDIMAFANSPWVVQLFYAFQD--DRYLYMV 152
Cdd:cd08217     1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEKEKQQLV-SEVNILRELKHPNIVRYYDRIVDraNTTLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGGDLVNLMSNYD-----VPEKWARFYTAEVVLALDAIH-----SMGFIHRDVKPDNMLLDKSGHLKLADFGTCMK 222
Cdd:cd08217    80 MEYCEGGDLAQLIKKCKkenqyIPEEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANIFLDSDNNVKLGDFGLARV 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  223 MNKEGMVrCDTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKI 290
Cdd:cd08217   160 LSHDSSF-AKTYVGTPYYMSPELLNEQ----SYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKI 222
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
74-281 8.27e-37

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: 140.46  E-value: 8.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKL--LSKFEmikrSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYM 151
Cdd:cd06609     1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVidLEEAE----DEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  152 VMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNkEGMVRC 231
Cdd:cd06609    77 IMEYCGGGSVLDLLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLT-STMSKR 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 167887698  232 DTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPfYAD 281
Cdd:cd06609   156 NTFVGTPFWMAPEVIKQSG----YDEKADIWSLGITAIELAKGEPP-LSD 200
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
75-291 1.30e-36

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: 139.47  E-value: 1.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKL--LSKFEMIKRSDSAffwEERDIMAFANSPWVVQLFYAFQDDRYLYMV 152
Cdd:cd08529     1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQidISRMSRKMREEAI---DEARVLSKLNSPYVIKYYDSFVDKGKLNIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGGDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmKMNKEGMV 229
Cdd:cd08529    78 MEYAENGDLHSLIKSQRgrpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVA-KILSDTTN 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887698  230 RCDTAVGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIM 291
Cdd:cd08529   157 FAQTIVGTPYYLSPELCE----DKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIV 214
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
75-335 1.33e-36

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: 139.44  E-value: 1.33e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfemiKRSDSAFFWEERD---------IMAFANS---PWVVQLFYA 142
Cdd:cd14004     1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFK----ERILVDTWVRDRKlgtvpleihILDTLNKrshPNIVKLLDF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  143 FQDDRYLYMVME-YMPGGDLVNLM-SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTC 220
Cdd:cd14004    77 FEDDEFYYLVMEkHGSGMDLFDFIeRKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  221 MKMnKEGmvRCDTAVGTPDYISPEVLksqGGDGYYGRECDWWSVGVFLYEMLVGDTPFYadslvgTYSKIMnhKNSLTFP 300
Cdd:cd14004   157 AYI-KSG--PFDTFVGTIDYAAPEVL---RGNPYGGKEQDIWALGVLLYTLVFKENPFY------NIEEIL--EADLRIP 222
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 167887698  301 ddNDISKEAKNLICAFLtDREVRlGRNGVEEIKRH 335
Cdd:cd14004   223 --YAVSEDLIDLISRML-NRDVG-DRPTIEELLTD 253
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
74-317 1.86e-36

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: 139.74  E-value: 1.86e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDsafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd14166     3 ETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSS---LENEIAVLKRIKHENIVTLEDIYESTTHYYLVM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL---DKSGHLKLADFGTCmKMNKEGMV 229
Cdd:cd14166    80 QLVSGGELFDRILERGVyTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLS-KMEQNGIM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  230 rcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEA 309
Cdd:cd14166   159 --STACGTPGYVAPEVLAQKP----YSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESPFWDDISESA 232

                  ....*...
gi 167887698  310 KNLICAFL 317
Cdd:cd14166   233 KDFIRHLL 240
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
74-356 5.16e-36

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: 138.71  E-value: 5.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRsDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd14086     1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSAR-DHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL---DKSGHLKLADFGTCMKMNKEGMV 229
Cdd:cd14086    80 DLVTGGELFeDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQGDQQA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  230 RCDTAvGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEA 309
Cdd:cd14086   160 WFGFA-GTPGYLSPEVLRKDP----YGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEA 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 167887698  310 KNLICAFLTDREVRlgRNGVEEIKRHLFFKNdqwawetlRDTVAPVV 356
Cdd:cd14086   235 KDLINQMLTVNPAK--RITAAEALKHPWICQ--------RDRVASMV 271
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
82-317 5.78e-36

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: 137.36  E-value: 5.78e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLlskFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKF---IKCRKAKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGEL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VN--LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNML-LDKSGH-LKLADFGTCMKMNKEGMVRcdTAVGT 237
Cdd:cd14103    78 FErvVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNqIKIIDFGLARKYDPDKKLK--VLFGT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  238 PDYISPEVLKsqggdgyY---GRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLIC 314
Cdd:cd14103   156 PEFVAPEVVN-------YepiSYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFDDEAFDDISDEAKDFIS 228

                  ...
gi 167887698  315 AFL 317
Cdd:cd14103   229 KLL 231
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
76-335 7.31e-36

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: 137.14  E-value: 7.31e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKrSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd14071     2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDE-ENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRcdTA 234
Cdd:cd14071    81 ASNGEIFDYLAQHGrMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPGELLK--TW 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  235 VGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFpddnDISKEAKNLIC 314
Cdd:cd14071   159 CGSPPYAAPEVFE---GKEYEGPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPF----FMSTDCEHLIR 231
                         250       260
                  ....*....|....*....|.
gi 167887698  315 AFLTDREVRlgRNGVEEIKRH 335
Cdd:cd14071   232 RMLVLDPSK--RLTIEQIKKH 250
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
74-279 8.09e-36

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: 137.01  E-value: 8.09e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKF----EMIKrsdsaffweERDIMAFANSPWVVQLFYAFQDDRYL 149
Cdd:cd06612     3 EVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEedlqEIIK---------EISILKQCDSPYIVKYYGSYFKNTDL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 YMVMEYMPGGDLVNLM--SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNkEG 227
Cdd:cd06612    74 WIVMEYCGAGSVSDIMkiTNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLT-DT 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 167887698  228 MVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFY 279
Cdd:cd06612   153 MAKRNTVIGTPFWMAPEVIQEIG----YNNKADIWSLGITAIEMAEGKPPYS 200
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
82-318 9.98e-36

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: 137.05  E-value: 9.98e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRK--VYAMKLLSKfemiKRSDS------AFFWEERDIMAFANSPWVVQLFYAFQDDRYLY-MV 152
Cdd:cd13994     1 IGKGATSVVRIVTKKNPRSgvLYAVKEYRR----RDDESkrkdyvKRLTSEYIISSKLHHPNIVKVLDLCQDLHGKWcLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGGDLVNLMSNYDVPEKWARF-YTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKM----NKEG 227
Cdd:cd13994    77 MEYCPGGDLFTLIEKADSLSLEEKDcFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFgmpaEKES 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  228 MVRCDtAVGTPDYISPEVLKSQGGDGYYGrecDWWSVGVFLYEMLVGDTPF----YADSLVGTYSKIMNHKNSLTFPDDN 303
Cdd:cd13994   157 PMSAG-LCGSEPYMAPEVFTSGSYDGRAV---DVWSCGIVLFALFTGRFPWrsakKSDSAYKAYEKSGDFTNGPYEPIEN 232
                         250
                  ....*....|....*
gi 167887698  304 DISKEAKNLICAFLT 318
Cdd:cd13994   233 LLPSECRRLIYRMLH 247
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
82-338 1.27e-35

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: 136.62  E-value: 1.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLsKFEMIKR--SDSAFFWEERDIMAFANSPWVVQLFYAFQDDRY--LYMVMEYMP 157
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAVKIL-KKRKLRRipNGEANVKREIQILRRLNHRNVIKLVDVLYNEEKqkLYMVMEYCV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  158 GGDLVNLMSnydVPEK----W-ARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTC--MKMNKEGMvR 230
Cdd:cd14119    80 GGLQEMLDS---APDKrlpiWqAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAeaLDLFAEDD-T 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  231 CDTAVGTPDYISPEVlkSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKImnHKNSLTFPDdnDISKEAK 310
Cdd:cd14119   156 CTTSQGSPAFQPPEI--ANGQDSFSGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENI--GKGEYTIPD--DVDPDLQ 229
                         250       260
                  ....*....|....*....|....*....
gi 167887698  311 NLICAFL-TDREVRLgrnGVEEIKRHLFF 338
Cdd:cd14119   230 DLLRGMLeKDPEKRF---TIEQIRQHPWF 255
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
80-338 3.88e-35

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: 135.18  E-value: 3.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSkfemIKRSDSAFFWE----ERDIMAFAN--SPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd06625     6 KLLGQGAFGQVYLCYDADTGRELAVKQVE----IDPINTEASKEvkalECEIQLLKNlqHERIVQYYGCLQDEKSLSIFM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMN----KEGM 228
Cdd:cd06625    82 EYMPGGSVKDEIKAYGaLTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRLQticsSTGM 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  229 vrcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDdnDISKE 308
Cdd:cd06625   162 ---KSVTGTPYWMSPEVINGEG----YGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIATQPTNPQLPP--HVSED 232
                         250       260       270
                  ....*....|....*....|....*....|.
gi 167887698  309 AKNLI-CAFltDREVRLgRNGVEEIKRHLFF 338
Cdd:cd06625   233 ARDFLsLIF--VRNKKQ-RPSAEELLSHSFV 260
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
76-338 4.05e-35

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: 135.09  E-value: 4.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd14079     4 YILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRcdTA 234
Cdd:cd14079    84 VSGGELFDYIVQKGrLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIMRDGEFLK--TS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  235 VGTPDYISPEVLksqGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNhkNSLTFPDdnDISKEAKNLIC 314
Cdd:cd14079   162 CGSPNYAAPEVI---SGKLYAGPEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKS--GIYTIPS--HLSPGARDLIK 234
                         250       260
                  ....*....|....*....|....
gi 167887698  315 AFLTDREVRlgRNGVEEIKRHLFF 338
Cdd:cd14079   235 RMLVVDPLK--RITIPEIRQHPWF 256
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
76-335 6.35e-35

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: 134.46  E-value: 6.35e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERdIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd14074     5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDVSKAHLFQEVR-CMKLVQHPNVVRLYEVIDTQTKLYLILEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVNLMSNYD--VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL-DKSGHLKLADFGTCMKMNKEGMVrcD 232
Cdd:cd14074    84 GDGGDMYDYIMKHEngLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGEKL--E 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  233 TAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnsLTFPDdnDISKEAKNL 312
Cdd:cd14074   162 TSCGSLAYSAPEILL---GDEYDAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCK--YTVPA--HVSPECKDL 234
                         250       260
                  ....*....|....*....|...
gi 167887698  313 ICAFLTDREVRlgRNGVEEIKRH 335
Cdd:cd14074   235 IRRMLIRDPKK--RASLEEIENH 255
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
76-335 7.02e-35

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: 135.48  E-value: 7.02e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIK-----------------------RSDSAFFWEERDIMAFAN 132
Cdd:cd14199     4 YKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMRqagfprrppprgaraapegctqpRGPIERVYQEIAILKKLD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  133 SPWVVQLFYAFQD--DRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSG 210
Cdd:cd14199    84 HPNVVKLVEVLDDpsEDHLYMVFELVKQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGEDG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  211 HLKLADFGTCMKMNKEGMVRCDTaVGTPDYISPEVLkSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKI 290
Cdd:cd14199   164 HIKIADFGVSNEFEGSDALLTNT-VGTPAFMAPETL-SETRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERILSLHSKI 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 167887698  291 MNHknSLTFPDDNDISKEAKNLICAFL-TDREVRLgrnGVEEIKRH 335
Cdd:cd14199   242 KTQ--PLEFPDQPDISDDLKDLLFRMLdKNPESRI---SVPEIKLH 282
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
76-291 1.07e-34

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: 133.51  E-value: 1.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDsaffweERDIMA------FANSPWVVQLFYAF--QDDR 147
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKAA------LREIKLlkhlndVEGHPNIVKLLDVFehRGGN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  148 YLYMVMEYMpGGDLVNLMSNYD--VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD-KSGHLKLADFGTCMKMN 224
Cdd:cd05118    75 HLCLVFELM-GMNLYELIKDYPrgLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINlELGQLKLADFGLARSFT 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  225 KEGMvrcDTAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIM 291
Cdd:cd05118   154 SPPY---TPYVATRWYRAPEVLL---GAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIV 214
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
80-337 1.40e-34

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: 133.68  E-value: 1.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFAN--SPWVVQLFYAFQDDRYLYMVMEYMP 157
Cdd:cd06632     6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKKSRESVKQLEQEIALLSKlrHPNIVQYYGTEREEDNLYIFLEYVP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  158 GGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRcdTAVG 236
Cdd:cd06632    86 GGSIHKLLQRYGaFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFSFAK--SFKG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  237 TPDYISPEVLKSQggDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDdnDISKEAKNLICAF 316
Cdd:cd06632   164 SPYWMAPEVIMQK--NSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGELPPIPD--HLSPDAKDFIRLC 239
                         250       260
                  ....*....|....*....|.
gi 167887698  317 LTDREVRlgRNGVEEIKRHLF 337
Cdd:cd06632   240 LQRDPED--RPTASQLLEHPF 258
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
74-335 1.41e-34

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: 133.61  E-value: 1.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd14167     3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETS--IENEIAVLHKIKHPNIVALDDIYESGGHLYLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNML---LDKSGHLKLADFGTCmKMNKEGMV 229
Cdd:cd14167    81 QLVSGGELFDrIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLS-KIEGSGSV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  230 rCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEA 309
Cdd:cd14167   160 -MSTACGTPGYVAPEVLAQKP----YSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSPYWDDISDSA 234
                         250       260
                  ....*....|....*....|....*.
gi 167887698  310 KNLIcAFLTDREVRLgRNGVEEIKRH 335
Cdd:cd14167   235 KDFI-QHLMEKDPEK-RFTCEQALQH 258
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
76-337 1.49e-34

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: 133.23  E-value: 1.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFfweERDI--MAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd14075     4 YRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKTQRLL---SREIssMEKLHHPNIIRLYEVVETLSKLHLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNY-DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVrcD 232
Cdd:cd14075    81 EYASGGELYTKISTEgKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKRGETL--N 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  233 TAVGTPDYISPEVLKSqggDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFPDdnDISKEAKNL 312
Cdd:cd14075   159 TFCGSPPYAAPELFKD---EHYIGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCIL--EGTYTIPS--YVSEPCQEL 231
                         250       260
                  ....*....|....*....|....*
gi 167887698  313 ICAFLtdREVRLGRNGVEEIKRHLF 337
Cdd:cd14075   232 IRGIL--QPVPSDRYSIDEIKNSEW 254
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
70-317 2.17e-34

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: 133.45  E-value: 2.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   70 RMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYL 149
Cdd:cd14117     2 KFTIDDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEHQLRREIEIQSHLRHPNILRLYNYFHDRKRI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 YMVMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKegm 228
Cdd:cd14117    82 YLILEYAPRGELYKELQKHGrFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVHAPS--- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  229 VRCDTAVGTPDYISPEVLKSQGGDgyygRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFPddNDISKE 308
Cdd:cd14117   159 LRRRTMCGTLDYLPPEMIEGRTHD----EKVDLWCIGVLCYELLVGMPPFESASHTETYRRIV--KVDLKFP--PFLSDG 230

                  ....*....
gi 167887698  309 AKNLICAFL 317
Cdd:cd14117   231 SRDLISKLL 239
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
76-279 2.57e-34

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: 132.73  E-value: 2.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSkFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd06627     2 YQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQIS-LEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVNLMSNY-DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGmVRCDTA 234
Cdd:cd06627    81 VENGSLASIIKKFgKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVE-KDENSV 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 167887698  235 VGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFY 279
Cdd:cd06627   160 VGTPYWMAPEVIEMSG----VTTASDIWSVGCTVIELLTGNPPYY 200
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
80-318 3.10e-34

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: 134.35  E-value: 3.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfemikRSDSAFfwEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 159
Cdd:cd14092    12 EALGDGSFSVCRKCVHKKTGQEFAVKIVSR-----RLDTSR--EVQLLRLCQGHPNIVKLHEVFQDELHTYLVMELLRGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DLVnlmsnyDVPEKWARFYTAE-------VVLALDAIHSMGFIHRDVKPDNMLL---DKSGHLKLADFG-TCMKMNKEGM 228
Cdd:cd14092    85 ELL------ERIRKKKRFTESEasrimrqLVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVDFGfARLKPENQPL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  229 vrcDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNH--KNSLTFPDD--ND 304
Cdd:cd14092   159 ---KTPCFTLPYAAPEVLKQALSTQGYDESCDLWSLGVILYTMLSGQVPFQSPSRNESAAEIMKRikSGDFSFDGEewKN 235
                         250
                  ....*....|....
gi 167887698  305 ISKEAKNLICAFLT 318
Cdd:cd14092   236 VSSEAKSLIQGLLT 249
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
80-313 6.59e-34

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: 131.66  E-value: 6.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSkfemIKRSDSAFF---WEERDIMAFANSPWVVQlFYAFQDDR-YLYMVMEY 155
Cdd:cd06626     6 NKIGEGTFGKVYTAVNLDTGELMAMKEIR----FQDNDPKTIkeiADEMKVLEGLDHPNLVR-YYGVEVHReEVYIFMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEG-MVRC-- 231
Cdd:cd06626    81 CQEGTLEELLRHGRIlDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNTtTMAPge 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  232 -DTAVGTPDYISPEVLKSQGGDGyYGRECDWWSVGVFLYEMLVGDTPFYAdsLVGTYSkIMNH---KNSLTFPDDNDISK 307
Cdd:cd06626   161 vNSLVGTPAYMAPEVITGNKGEG-HGRAADIWSLGCVVLEMATGKRPWSE--LDNEWA-IMYHvgmGHKPPIPDSLQLSP 236

                  ....*.
gi 167887698  308 EAKNLI 313
Cdd:cd06626   237 EGKDFL 242
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
76-335 7.66e-34

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: 131.43  E-value: 7.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSdsaffwEERDIMAFA--NSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd14662     2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKIDEN------VQREIINHRslRHPNIIRFKEVVLTPTHLAIVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKS--GHLKLADFGtcmkMNKEGMV- 229
Cdd:cd14662    76 EYAAGGELFERICNAGrFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSpaPRLKICDFG----YSKSSVLh 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  230 -RCDTAVGTPDYISPEVLKSQggdGYYGRECDWWSVGVFLYEMLVGDTPFY----ADSLVGTYSKIMNHKNSLtfPDDND 304
Cdd:cd14662   152 sQPKSTVGTPAYIAPEVLSRK---EYDGKVADVWSCGVTLYVMLVGAYPFEdpddPKNFRKTIQRIMSVQYKI--PDYVR 226
                         250       260       270
                  ....*....|....*....|....*....|..
gi 167887698  305 ISKEAKNLI-CAFLTDREVRLgrnGVEEIKRH 335
Cdd:cd14662   227 VSQDCRHLLsRIFVANPAKRI---TIPEIKNH 255
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
74-352 9.09e-34

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: 132.67  E-value: 9.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKL--LSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYM 151
Cdd:cd14094     3 DVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIvdVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  152 VMEYMPGGDL----VNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL---DKSGHLKLADFGTCMKM 223
Cdd:cd14094    83 VFEFMDGADLcfeiVKRADAGFVySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  224 NKEGMVRCDTaVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYAdSLVGTYSKIMNHKNSLTFPDDN 303
Cdd:cd14094   163 GESGLVAGGR-VGTPHFMAPEVVKRE----PYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWS 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 167887698  304 DISKEAKNLICAFLT-DREVRLgrnGVEEIKRHLFFKN-DQWAWET-LRDTV 352
Cdd:cd14094   237 HISESAKDLVRRMLMlDPAERI---TVYEALNHPWIKErDRYAYRIhLPETV 285
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
76-341 2.75e-33

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: 130.40  E-value: 2.75e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMikRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd14169     5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKAL--RGKEAMVENEIAVLRRINHENIVSLEDIYESPTHLYLAMEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD---KSGHLKLADFGTCmKMNKEGMVrc 231
Cdd:cd14169    83 VTGGELFDrIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGLS-KIEAQGML-- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  232 DTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKN 311
Cdd:cd14169   160 STACGTPGYVAPELLEQKP----YGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFDSPYWDDISESAKD 235
                         250       260       270
                  ....*....|....*....|....*....|.
gi 167887698  312 LICAFLT-DREVRLgrnGVEEIKRHLFFKND 341
Cdd:cd14169   236 FIRHLLErDPEKRF---TCEQALQHPWISGD 263
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
76-324 6.08e-33

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: 129.76  E-value: 6.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfemIKRSDSaffwEERDIM-AFANSPWVVQLFYAFQDDRYLYMVME 154
Cdd:cd14175     3 YVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDK---SKRDPS----EEIEILlRYGQHPNIITLKDVYDDGKHVYLVTE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNML-LDKSGH---LKLADFGTCMKMNKEG-- 227
Cdd:cd14175    76 LMRGGELLDkILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGNpesLRICDFGFAKQLRAENgl 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  228 -MVRCDTAvgtpDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFY---ADSLVGTYSKIMNHKNSLTFPDDN 303
Cdd:cd14175   156 lMTPCYTA----NFVAPEVLKRQG----YDEGCDIWSLGILLYTMLAGYTPFAngpSDTPEEILTRIGSGKFTLSGGNWN 227
                         250       260
                  ....*....|....*....|..
gi 167887698  304 DISKEAKNLICAFL-TDREVRL 324
Cdd:cd14175   228 TVSDAAKDLVSKMLhVDPHQRL 249
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
76-335 6.77e-33

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: 128.56  E-value: 6.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSdsaffwEERDIMAFAN--SPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd14665     2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDEN------VQREIINHRSlrHPNIVRFKEVILTPTHLAIVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSG--HLKLADFGtcmkMNKEGMVR 230
Cdd:cd14665    76 EYAAGGELFERICNAGrFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFG----YSKSSVLH 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  231 CD--TAVGTPDYISPEVLKSQggdGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTF--PDDNDIS 306
Cdd:cd14665   152 SQpkSTVGTPAYIAPEVLLKK---EYDGKIADVWSCGVTLYVMLVGAYPFEDPEEPRNFRKTIQRILSVQYsiPDYVHIS 228
                         250       260       270
                  ....*....|....*....|....*....|
gi 167887698  307 KEAKNLIC-AFLTDREVRLgrnGVEEIKRH 335
Cdd:cd14665   229 PECRHLISrIFVADPATRI---TIPEIRNH 255
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
76-318 7.73e-33

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: 128.42  E-value: 7.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfemiKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd14087     3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIET----KCRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH---LKLADFGTCMKMNKEGMVRC 231
Cdd:cd14087    79 ATGGELFDrIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLASTRKKGPNCLM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  232 DTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKN 311
Cdd:cd14087   159 KTTCGTPEYIAPEILLRKP----YTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEPWPSVSNLAKD 234

                  ....*..
gi 167887698  312 LICAFLT 318
Cdd:cd14087   235 FIDRLLT 241
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
75-282 1.46e-32

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: 127.78  E-value: 1.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMK---LLSKFEMIKRSDsaffwEERDIMAFANSPWVVQLFYAFQDDRYLYM 151
Cdd:cd08219     1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKeirLPKSSSAVEDSR-----KEAVLLAKMKHPNIVAFKESFEADGHLYI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  152 VMEYMPGGDL---VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGM 228
Cdd:cd08219    76 VMEYCDGGDLmqkIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGA 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 167887698  229 VRCdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADS 282
Cdd:cd08219   156 YAC-TYVGTPYYVPPEIWENMP----YNNKSDIWSLGCILYELCTLKHPFQANS 204
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
74-338 1.51e-32

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: 127.86  E-value: 1.51e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllsKFEMIKRSDSA-FFWEERDIMAFANSPWVVQLFYAFQDDRYLYMV 152
Cdd:cd06610     1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIK---RIDLEKCQTSMdELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGGDLVNLMS---NYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGM 228
Cdd:cd06610    78 MPLLSGGSLLDIMKssyPRGGlDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASLATGGD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  229 VRC---DTAVGTPDYISPEVLKSQGGdgyYGRECDWWSVGVFLYEMLVGDTPFY----ADSLVGTyskIMNHKNSL-TFP 300
Cdd:cd06610   158 RTRkvrKTFVGTPCWMAPEVMEQVRG---YDFKADIWSFGITAIELATGAAPYSkyppMKVLMLT---LQNDPPSLeTGA 231
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 167887698  301 DDNDISKEAKNLICAFLTDREVRlgRNGVEEIKRHLFF 338
Cdd:cd06610   232 DYKKYSKSFRKMISLCLQKDPSK--RPTAEELLKHKFF 267
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
75-279 1.82e-32

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: 127.42  E-value: 1.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSkfeMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVME 154
Cdd:cd06613     1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIK---LEPGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDLVNLmsnYDV----PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEgMVR 230
Cdd:cd06613    78 YCGGGSLQDI---YQVtgplSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTAT-IAK 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 167887698  231 CDTAVGTPDYISPEVLKSQGGDGYYGReCDWWSVGVFLYEMLVGDTPFY 279
Cdd:cd06613   154 RKSFIGTPYWMAPEVAAVERKGGYDGK-CDIWALGITAIELAELQPPMF 201
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
76-300 2.02e-32

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: 128.39  E-value: 2.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAmkllskfemIKRS--DSAFFWEERDIMAFANSPWVVQLFYAF------QDDR 147
Cdd:cd14137     6 YTIEKVIGSGSFGVVYQAKLLETGEVVA---------IKKVlqDKRYKNRELQIMRRLKHPNIVKLKYFFyssgekKDEV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  148 YLYMVMEYMPGgDLVNLMSNYD-----VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD-KSGHLKLADFGTCM 221
Cdd:cd14137    77 YLNLVMEYMPE-TLYRVIRHYSknkqtIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDpETGVLKLCDFGSAK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  222 KMNKegmvrcdtavGTPD--YIS------PE-VLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYADS----LV---- 284
Cdd:cd14137   156 RLVP----------GEPNvsYICsryyraPElIFGAT----DYTTAIDIWSAGCVLAELLLGQPLFPGESsvdqLVeiik 221
                         250       260
                  ....*....|....*....|...
gi 167887698  285 --GTYSKI----MNHKNSL-TFP 300
Cdd:cd14137   222 vlGTPTREqikaMNPNYTEfKFP 244
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
74-339 2.17e-32

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: 127.46  E-value: 2.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLlskfeMIKRSDSAFFWE---ERDIMAFANSPWVVQLFYAFQDDRYLY 150
Cdd:cd06605     1 DDLEYLGELGEGNGGVVSKVRHRPSGQIMAVKV-----IRLEIDEALQKQilrELDVLHKCNSPYIVGFYGAFYSEGDIS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHS-MGFIHRDVKPDNMLLDKSGHLKLADFGTCMKM-NKEG 227
Cdd:cd06605    76 ICMEYMDGGSLDKILKEVGrIPERILGKIAVAVVKGLIYLHEkHKIIHRDVKPSNILVNSRGQVKLCDFGVSGQLvDSLA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  228 mvrcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPF------YADSLVGTYSKIMNHKNSLtFPD 301
Cdd:cd06605   156 ----KTFVGTRSYMAPERISGGK----YTVKSDIWSLGLSLVELATGRFPYpppnakPSMMIFELLSYIVDEPPPL-LPS 226
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 167887698  302 DNdISKEAKNLICAFLTDREVRlgRNGVEEIKRHLFFK 339
Cdd:cd06605   227 GK-FSPDFQDFVSQCLQKDPTE--RPSYKELMEHPFIK 261
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
74-292 2.24e-32

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: 128.20  E-value: 2.24e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllsKF------EMIKRSDSaffwEERDIMAFANSPWVVQLFYAFQDDR 147
Cdd:cd07833     1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIK---KFkeseddEDVKKTAL----REVKVLRQLRHENIVNLKEAFRRKG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  148 YLYMVMEYMPGGDLVNL-MSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKE 226
Cdd:cd07833    74 RLYLVFEYVERTLLELLeASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTAR 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167887698  227 GMVRCDTAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMN 292
Cdd:cd07833   154 PASPLTDYVATRWYRAPELLV---GDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIQK 216
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
74-338 3.90e-32

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: 127.01  E-value: 3.90e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLS------KFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDR 147
Cdd:cd14181    10 QKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEvtaerlSPEQLEEVRSSTLKEIHILRQVSGHPSIITLIDSYESST 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  148 YLYMVMEYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKE 226
Cdd:cd14181    90 FIFLVFDLMRRGELFDyLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHLEPG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  227 GMVRcdTAVGTPDYISPEVLKSQGGDGY--YGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDND 304
Cdd:cd14181   170 EKLR--ELCGTPGYLAPEILKCSMDETHpgYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFSSPEWDD 247
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 167887698  305 ISKEAKNLICAFL-TDREVRLgrnGVEEIKRHLFF 338
Cdd:cd14181   248 RSSTVKDLISRLLvVDPEIRL---TAEQALQHPFF 279
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
75-324 3.99e-32

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: 126.63  E-value: 3.99e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVV-KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRsdsaffweERDIMAFANS-PWVVQLF--YA--FQDDRY 148
Cdd:cd14089     1 DYTISkQVLGLGINGKVLECFHKKTGEKFALKVLRDNPKARR--------EVELHWRASGcPHIVRIIdvYEntYQGRKC 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 LYMVMEYMPGGDLVNLMSnydvpEKWARFYT----AEVV----LALDAIHSMGFIHRDVKPDNMLL---DKSGHLKLADF 217
Cdd:cd14089    73 LLVVMECMEGGELFSRIQ-----ERADSAFTereaAEIMrqigSAVAHLHSMNIAHRDLKPENLLYsskGPNAILKLTDF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  218 GtcmkMNKE--GMVRCDTAVGTPDYISPEVLksqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLV----GTYSKIM 291
Cdd:cd14089   148 G----FAKEttTKKSLQTPCYTPYYVAPEVL----GPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLaispGMKKRIR 219
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 167887698  292 NhkNSLTFPDD--NDISKEAKNLI-CAFLTDREVRL 324
Cdd:cd14089   220 N--GQYEFPNPewSNVSEEAKDLIrGLLKTDPSERL 253
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
73-324 5.93e-32

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: 127.05  E-value: 5.93e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   73 AEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfemIKRSDSaffwEERDIM-AFANSPWVVQLFYAFQDDRYLYM 151
Cdd:cd14178     2 TDGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDK---SKRDPS----EEIEILlRYGQHPNIITLKDVYDDGKFVYL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  152 VMEYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNML-LDKSGH---LKLADFGTCMKMNKE 226
Cdd:cd14178    75 VMELMRGGELLDrILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNpesIRICDFGFAKQLRAE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  227 G---MVRCDTAvgtpDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFY---ADSLVGTYSKIMNHKNSLTFP 300
Cdd:cd14178   155 NgllMTPCYTA----NFVAPEVLKRQG----YDAACDIWSLGILLYTMLAGFTPFAngpDDTPEEILARIGSGKYALSGG 226
                         250       260
                  ....*....|....*....|....*
gi 167887698  301 DDNDISKEAKNLICAFL-TDREVRL 324
Cdd:cd14178   227 NWDSISDAAKDIVSKMLhVDPHQRL 251
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
75-301 6.04e-32

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: 126.17  E-value: 6.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRhKSTRKVYAMKllsKFEMIKRSDSA---FFWEERDIMAFANSPWVVQLF-YAFQDDR-YL 149
Cdd:cd14131     2 PYEILKQLGKGGSSKVYKVL-NPKKKIYALK---RVDLEGADEQTlqsYKNEIELLKKLKGSDRIIQLYdYEVTDEDdYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 YMVMEYmPGGDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKsGHLKLADFGTCMKMNKE 226
Cdd:cd14131    78 YMVMEC-GEIDLATILKKKRpkpIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVK-GRLKLIDFGIAKAIQND 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  227 --GMVRcDTAVGTPDYISPEVLKSQGGDGYY------GRECDWWSVGVFLYEMLVGDTPFYadSLVGTYSK---IMNHKN 295
Cdd:cd14131   156 ttSIVR-DSQVGTLNYMSPEAIKDTSASGEGkpkskiGRPSDVWSLGCILYQMVYGKTPFQ--HITNPIAKlqaIIDPNH 232

                  ....*.
gi 167887698  296 SLTFPD 301
Cdd:cd14131   233 EIEFPD 238
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
76-278 8.65e-32

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: 125.45  E-value: 8.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVyAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd14161     5 YEFLETLGKGTYGRVKKARDSSGRLV-AIKSIRKDRIKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRcdTA 234
Cdd:cd14161    84 ASRGDLYDYISERQrLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYNQDKFLQ--TY 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 167887698  235 VGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd14161   162 CGSPLYASPEIVN---GRPYIGPEVDSWSLGVLLYILVHGTMPF 202
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
74-317 1.15e-31

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: 124.97  E-value: 1.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd14186     1 EDFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYDVP--EKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG--TCMKMNKEgmv 229
Cdd:cd14186    81 EMCHNGEMSRYLKNRKKPftEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGlaTQLKMPHE--- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  230 RCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFPDdnDISKEA 309
Cdd:cd14186   158 KHFTMCGTPNYISPEIATRSA----HGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVV--LADYEMPA--FLSREA 229

                  ....*...
gi 167887698  310 KNLICAFL 317
Cdd:cd14186   230 QDLIHQLL 237
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
75-283 1.87e-31

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: 124.69  E-value: 1.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMI---KRSDSAffwEERDIMAFANSPWVVQLFYAFQDDRYLYM 151
Cdd:cd08224     1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEMMdakARQDCL---KEIDLLQQLNHPNIIKYLASFIENNELNI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  152 VMEYMPGGDLVNLMSNYD-----VPEK--WARFYtaEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMN 224
Cdd:cd08224    78 VLELADAGDLSRLIKHFKkqkrlIPERtiWKYFV--QLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRFFS 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 167887698  225 KEGMVrCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSL 283
Cdd:cd08224   156 SKTTA-AHSLVGTPYYMSPERIREQG----YDFKSDIWSLGCLLYEMAALQSPFYGEKM 209
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
75-335 3.63e-31

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: 124.10  E-value: 3.63e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLS-------KFEMIKRSDSAFFWEERDIMAFA-----NSPWVVQLFYA 142
Cdd:cd14077     2 NWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPrasnaglKKEREKRLEKEISRDIRTIREAAlssllNHPHICRLRDF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  143 FQDDRYLYMVMEYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCM 221
Cdd:cd14077    82 LRTPNHYYMLFEYVDGGQLLDyIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLSN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  222 KMNKEGMVRcdTAVGTPDYISPEVLKSQggdGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFPd 301
Cdd:cd14077   162 LYDPRRLLR--TFCGSLYFAAPELLQAQ---PYTGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIK--KGKVEYP- 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 167887698  302 dNDISKEAKNLICAFLTDREVRlgRNGVEEIKRH 335
Cdd:cd14077   234 -SYLSSECKSLISRMLVVDPKK--RATLEQVLNH 264
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
80-338 1.08e-30

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: 122.43  E-value: 1.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 159
Cdd:cd14188     7 KVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRR 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRcDTAVGTP 238
Cdd:cd14188    87 SMAHILKARKVlTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRR-RTICGTP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  239 DYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTfpddNDISKEAKNLICAFLT 318
Cdd:cd14188   166 NYLSPEVLNKQG----HGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLP----SSLLAPAKHLIASMLS 237
                         250       260
                  ....*....|....*....|
gi 167887698  319 DREVrlGRNGVEEIKRHLFF 338
Cdd:cd14188   238 KNPE--DRPSLDEIIRHDFF 255
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
68-282 1.66e-30

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: 121.78  E-value: 1.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   68 DLRMKAEDYevvKVIGRGAFGEVQLVRHKSTRKVYAMKllsKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDR 147
Cdd:cd06648     4 DPRSDLDNF---VKIGEGSTGIVCIATDKSTGRQVAVK---KMDLRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYLVGD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  148 YLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEg 227
Cdd:cd06648    78 ELWVVMEFLEGGALTDIVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKE- 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  228 MVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADS 282
Cdd:cd06648   157 VPRRKSLVGTPYWMAPEVISRLP----YGTEVDIWSLGIMVIEMVDGEPPYFNEP 207
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
73-273 1.87e-30

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: 122.02  E-value: 1.87e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   73 AEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMK-LLSKFEMIKRSDsaffwEERDIMAFA--NSPWVVQLFYAFQDDRYL 149
Cdd:cd13996     5 LNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKkIRLTEKSSASEK-----VLREVKALAklNHPNIVRYYTAWVEEPPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 YMVMEYMPGGDLVNLMSNYDVPEKWARF----YTAEVVLALDAIHSMGFIHRDVKPDNMLLDKS-GHLKLADFG--TCMK 222
Cdd:cd13996    80 YIQMELCEGGTLRDWIDRRNSSSKNDRKlaleLFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDdLQVKIGDFGlaTSIG 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887698  223 MNKEGMVRCD-----------TAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLV 273
Cdd:cd13996   160 NQKRELNNLNnnnngntsnnsVGIGTPLYASPEQLDGE----NYNEKADIYSLGIILFEMLH 217
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
76-317 2.33e-30

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: 123.59  E-value: 2.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfemiKRSDSAffwEERDIM-AFANSPWVVQLFYAFQDDRYLYMVME 154
Cdd:cd14176    21 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDK----SKRDPT---EEIEILlRYGQHPNIITLKDVYDDGKYVYVVTE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNML-LDKSGH---LKLADFGTCMKMNKEG-- 227
Cdd:cd14176    94 LMKGGELLDkILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENgl 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  228 -MVRCDTAvgtpDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFY---ADSLVGTYSKIMNHKNSLTFPDDN 303
Cdd:cd14176   174 lMTPCYTA----NFVAPEVLERQG----YDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGYWN 245
                         250
                  ....*....|....
gi 167887698  304 DISKEAKNLICAFL 317
Cdd:cd14176   246 SVSDTAKDLVSKML 259
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
82-337 4.25e-30

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: 120.86  E-value: 4.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDimafanSPWVVQlFYAFQDDR-YLYMVMEYMPGGD 160
Cdd:cd14010     8 IGRGKHSVVYKGRRKGTIEFVAIKCVDKSKRPEVLNEVRLTHELK------HPNVLK-FYEWYETSnHLWLVVEYCTGGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  161 LVNLMS-NYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG---------------TCMKMN 224
Cdd:cd14010    81 LETLLRqDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGlarregeilkelfgqFSDEGN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  225 KEGMVRCDTAVGTPDYISPEVLksQGGDgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHK-NSLTFPDDN 303
Cdd:cd14010   161 VNKVSKKQAKRGTPYYMAPELF--QGGV--HSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDpPPPPPKVSS 236
                         250       260       270
                  ....*....|....*....|....*....|....
gi 167887698  304 DISKEAKNLICAFLTDREVRlgRNGVEEIKRHLF 337
Cdd:cd14010   237 KPSPDFKSLLKGLLEKDPAK--RLSWDELVKHPF 268
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
76-339 4.76e-30

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: 121.04  E-value: 4.76e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLS----KFEMikrSDsafFWEERDIMA---FANSPWVVQLFYAFQDDRY 148
Cdd:cd06917     3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNldtdDDDV---SD---IQKEVALLSqlkLGQPKNIIKYYGSYLKGPS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 LYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGM 228
Cdd:cd06917    77 LWIIMDYCEGGSIRTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  229 VRcDTAVGTPDYISPEVLKsqggDG-YYGRECDWWSVGVFLYEMLVGDTPfYADSLVGTYSKIMNHKNSLTFPdDNDISK 307
Cdd:cd06917   157 KR-STFVGTPYWMAPEVIT----EGkYYDTKADIWSLGITTYEMATGNPP-YSDVDALRAVMLIPKSKPPRLE-GNGYSP 229
                         250       260       270
                  ....*....|....*....|....*....|..
gi 167887698  308 EAKNLICAFLTDREVRlgRNGVEEIKRHLFFK 339
Cdd:cd06917   230 LLKEFVAACLDEEPKD--RLSADELLKSKWIK 259
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
76-283 6.30e-30

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: 120.06  E-value: 6.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFfWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd08225     2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEAS-KKEVILLAKMKHPNIVTFFASFQENGRLFIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDL---VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHL-KLADFGTCMKMNkEGMVRC 231
Cdd:cd08225    81 CDGGDLmkrINRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLN-DSMELA 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 167887698  232 DTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSL 283
Cdd:cd08225   160 YTCVGTPYYLSPEICQNRP----YNNKTDIWSLGCVLYELCTLKHPFEGNNL 207
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
82-278 1.08e-29

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: 119.48  E-value: 1.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFwEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALL-KEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNYDVPEKWA-RFYTA-EVVLALDAIHSM--GFIHRDVKPDNMLLDKSGHLKLADFG-TCMKMNKEGMVRCDTA-- 234
Cdd:cd13978    80 KSLLEREIQDVPWSlRFRIIhEIALGMNFLHNMdpPLLHHDLKPENILLDNHFHVKISDFGlSKLGMKSISANRRRGTen 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 167887698  235 -VGTPDYISPEVLKsqggDGYY--GRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd13978   160 lGGTPIYMAPEAFD----DFNKkpTSKSDVYSFAIVIWAVLTRKEPF 202
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
74-339 1.10e-29

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: 120.02  E-value: 1.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKL-------LSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDD 146
Cdd:cd14182     3 EKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIiditgggSFSPEEVQELREATLKEIDILRKVSGHPNIIQLKDTYETN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  147 RYLYMVMEYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNK 225
Cdd:cd14182    83 TFFFLVFDLMKKGELFDyLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLDP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  226 EGMVRcdTAVGTPDYISPEVLKSQGGDGY--YGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDN 303
Cdd:cd14182   163 GEKLR--EVCGTPGYLAPEIIECSMDDNHpgYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFGSPEWD 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 167887698  304 DISKEAKNLICAFLTDREVRlgRNGVEEIKRHLFFK 339
Cdd:cd14182   241 DRSDTVKDLISRFLVVQPQK--RYTAEEALAHPFFQ 274
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
81-335 1.21e-29

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: 120.21  E-value: 1.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   81 VIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSdsAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGD 160
Cdd:cd14090     9 LLGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRS--RVFREVETLHQCQGHPNILQLIEYFEDDERFYLVFEKMRGGP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  161 LVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNML---LDKSGHLKLADFGTCMKMnKEGMVRCD---- 232
Cdd:cd14090    87 LLShIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILcesMDKVSPVKICDFDLGSGI-KLSSTSMTpvtt 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  233 ----TAVGTPDYISPEVLKSQGGDG-YYGRECDWWSVGVFLYEMLVGDTPFYA------------------DSLV----- 284
Cdd:cd14090   166 pellTPVGSAEYMAPEVVDAFVGEAlSYDKRCDLWSLGVILYIMLCGYPPFYGrcgedcgwdrgeacqdcqELLFhsiqe 245
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 167887698  285 GTYSkimnhknsltFPDDN--DISKEAKNLICAFLTdREVRLgRNGVEEIKRH 335
Cdd:cd14090   246 GEYE----------FPEKEwsHISAEAKDLISHLLV-RDASQ-RYTAEQVLQH 286
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
69-278 1.23e-29

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: 119.71  E-value: 1.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   69 LRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLL----SKFEMIKrsdsaffwEERDIMA-FANSPWVVQLFYAF 143
Cdd:cd06608     1 LPDPAGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMdiieDEEEEIK--------LEINILRkFSNHPNIATFYGAF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  144 -------QDDRyLYMVMEYMPGG---DLVN--LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH 211
Cdd:cd06608    73 ikkdppgGDDQ-LWLVMEYCGGGsvtDLVKglRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAE 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  212 LKLADFGTCMKMNKEGMVRcDTAVGTPDYISPEVLK-SQGGDGYYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd06608   152 VKLVDFGVSAQLDSTLGRR-NTFIGTPYWMAPEVIAcDQQPDASYDARCDVWSLGITAIELADGKPPL 218
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
82-317 1.51e-29

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: 118.93  E-value: 1.51e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKS-TRKVYAMKLLSKFEMIKRSDSAFFWEERdIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGD 160
Cdd:cd14121     3 LGSGTYATVYKAYRKSgAREVVAVKCVSKSSLNKASTENLLTEIE-LLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGGD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  161 LVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSG--HLKLADFGTCMKMNKEgmVRCDTAVGT 237
Cdd:cd14121    82 LSRFIRSRRtLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYnpVLKLADFGFAQHLKPN--DEAHSLRGS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  238 PDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnSLTFPDDNDISKEAKNLICAFL 317
Cdd:cd14121   160 PLYMAPEMILKK----KYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSK-PIEIPTRPELSADCRDLLLRLL 234
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
76-271 2.26e-29

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: 119.18  E-value: 2.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllskfEMIKRSDSaffWEE-------RDIMAFANSPWVVQLFYAFQDDRY 148
Cdd:cd07830     1 YKVIKQLGDGTFGSVYLARNKETGELVAIK-----KMKKKFYS---WEEcmnlrevKSLRKLNEHPNIVKLKEVFRENDE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 LYMVMEYMPGgDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGtcmkMNK 225
Cdd:cd07830    73 LYFVFEYMEG-NLYQLMKDRKgkpFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFG----LAR 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 167887698  226 EgmVRCD---TA-VGTPDYISPEV-LKSQggdgYYGRECDWWSVGVFLYEM 271
Cdd:cd07830   148 E--IRSRppyTDyVSTRWYRAPEIlLRST----SYSSPVDIWALGCIMAEL 192
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
68-284 3.57e-29

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: 118.93  E-value: 3.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   68 DLRMKAEDYevVKvIGRGAFGEVQLVRHKSTRKVYAMKLLskfEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDR 147
Cdd:cd06659    18 DPRQLLENY--VK-IGEGSTGVVCIAREKHSGRQVAVKMM---DLRKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  148 YLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEG 227
Cdd:cd06659    92 ELWVLMEYLQGGALTDIVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDV 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  228 MVRcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLV 284
Cdd:cd06659   172 PKR-KSLVGTPYWMAPEVISRCP----YGTEVDIWSLGIMVIEMVDGEPPYFSDSPV 223
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
73-313 4.29e-29

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: 117.84  E-value: 4.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   73 AEDYEVV-KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYM 151
Cdd:cd14106     6 NEVYTVEsTPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRNEILHEIAVLELCKDCPRVVNLHEVYETRSELIL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  152 VMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKS---GHLKLADFGTCMKMNKEG 227
Cdd:cd14106    86 ILELAAGGELQTLLDEEEcLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEfplGDIKLCDFGISRVIGEGE 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  228 MVRcdTAVGTPDYISPEVLKsqggdgyY---GRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKImnHKNSLTFPDD-- 302
Cdd:cd14106   166 EIR--EILGTPDYVAPEILS-------YepiSLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNI--SQCNLDFPEElf 234
                         250
                  ....*....|.
gi 167887698  303 NDISKEAKNLI 313
Cdd:cd14106   235 KDVSPLAIDFI 245
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
74-317 4.59e-29

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: 117.83  E-value: 4.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMikRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd14184     1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKC--CGKEHLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL----DKSGHLKLADFGTCMKMnkEGM 228
Cdd:cd14184    79 ELVKGGDLFDaITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATVV--EGP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  229 VRcdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLV--GTYSKIMNHKNSLTFPDDNDIS 306
Cdd:cd14184   157 LY--TVCGTPTYVAPEIIAETG----YGLKVDIWAAGVITYILLCGFPPFRSENNLqeDLFDQILLGKLEFPSPYWDNIT 230
                         250
                  ....*....|.
gi 167887698  307 KEAKNLICAFL 317
Cdd:cd14184   231 DSAKELISHML 241
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
76-305 8.74e-29

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: 117.07  E-value: 8.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAF----FWEERDIMAFA-NSPWVVQLFYAFQDDRYLY 150
Cdd:cd13993     2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKDGNDFqklpQLREIDLHRRVsRHPNIITLHDVFETEVAIY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGGDLV-NLMSNYDVPEK--WARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKS-GHLKLADFG--TCMKMN 224
Cdd:cd13993    82 IVLEYCPNGDLFeAITENRIYVGKteLIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCDFGlaTTEKIS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  225 kegmvrCDTAVGTPDYISPEVLKSQGGD--GYYGRECDWWSVGVFLYEMLVGDTPF-YADSLVGTYSKIMNHKNSL--TF 299
Cdd:cd13993   162 ------MDFGVGSEFYMAPECFDEVGRSlkGYPCAAGDIWSLGIILLNLTFGRNPWkIASESDPIFYDYYLNSPNLfdVI 235

                  ....*.
gi 167887698  300 PDDNDI 305
Cdd:cd13993   236 LPMSDD 241
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
80-293 9.87e-29

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: 116.76  E-value: 9.87e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSkFEMIKRSDSAF----FWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd06630     6 PLLGTGAFSSCYQARDVKTGTLMAVKQVS-FCRNSSSEQEEvveaIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEW 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSG-HLKLADFGTCMKMNKEGMVRCD- 232
Cdd:cd06630    85 MAGGSVASLLSKYGaFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGqRLRIADFGAAARLASKGTGAGEf 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167887698  233 --TAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADslvgtysKIMNH 293
Cdd:cd06630   165 qgQLLGTIAFMAPEVLRGEQ----YGRSCDVWSVGCVIIEMATAKPPWNAE-------KISNH 216
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
76-291 1.08e-28

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: 116.45  E-value: 1.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKL--LSKFEMIKRSDSAffwEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd08218     2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEinISKMSPKEREESR---KEVAVLSKMKHPNIVQYQESFEENGNLYIVM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDL---VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEG-MV 229
Cdd:cd08218    79 DYCDGGDLykrINAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVeLA 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887698  230 RcdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIM 291
Cdd:cd08218   159 R--TCIGTPYYLSPEICENKP----YNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKII 214
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
73-277 1.24e-28

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: 117.15  E-value: 1.24e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   73 AEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDsafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMV 152
Cdd:cd06611     4 NDIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIESEEELED---FMVEIDILSECKHPNIVGLYEAYFYENKLWIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGGDLVNLMSNYDVP--EKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKmNKEGMVR 230
Cdd:cd06611    81 IEFCDGGALDSIMLELERGltEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAK-NKSTLQK 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 167887698  231 CDTAVGTPDYISPEVLKSQG-GDGYYGRECDWWSVGVFLYEMLVGDTP 277
Cdd:cd06611   160 RDTFIGTPYWMAPEVVACETfKDNPYDYKADIWSLGITLIELAQMEPP 207
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
74-340 1.35e-28

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 116.49  E-value: 1.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIG--RGAFGEVQLVRHKSTRKVYAMKLLSKfemikrsdSAFFWEE---RDIMAfaNSPWVVQLFYAFQDDRY 148
Cdd:PHA03390   14 KNCEIVKKLKliDGKFGKVSVLKHKPTQKLFVQKIIKA--------KNFNAIEpmvHQLMK--DNPNFIKLYYSVTTLKG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 LYMVMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKS-GHLKLADFGTCMKMNKE 226
Cdd:PHA03390   84 HVLIMDYIKDGDLFDLLKKEGkLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAkDRIYLCDYGLCKIIGTP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  227 GMVRcdtavGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPF---YADSLvgTYSKIMNH-KNSLTFPdd 302
Cdd:PHA03390  164 SCYD-----GTLDYFSPEKIKGH----NYDVSFDWWAVGVLTYELLTGKHPFkedEDEEL--DLESLLKRqQKKLPFI-- 230
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 167887698  303 NDISKEAKNLICAFLT-DREVRLgrNGVEEIKRHLFFKN 340
Cdd:PHA03390  231 KNVSKNANDFVQSMLKyNINYRL--TNYNEIIKHPFLKI 267
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
76-270 1.36e-28

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: 115.87  E-value: 1.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLlSKFEMIKRSDSAFFWEE-RDIMAFANSPWVVQLFYAFQDDRYLYMVME 154
Cdd:cd14050     3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKR-SRSRFRGEKDRKRKLEEvERHEKLGEHPNCVRFIKAWEEKGILYIQTE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGmvRCDTA 234
Cdd:cd14050    82 LCDTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELDKED--IHDAQ 159
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 167887698  235 VGTPDYISPEVLksqggDGYYGRECDWWSVGVFLYE 270
Cdd:cd14050   160 EGDPRYMAPELL-----QGSFTKAADIFSLGITILE 190
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
67-271 1.66e-28

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: 117.05  E-value: 1.66e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   67 RDLRmKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLskfEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDD 146
Cdd:cd06644     6 RDLD-PNEVWEIIGELGDGAFGKVYKAKNKETGALAAAKVI---ETKSEEELEDYMVEIEILATCNHPYIVKLLGAFYWD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  147 RYLYMVMEYMPGGDLVNLMSNYD--VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKmN 224
Cdd:cd06644    82 GKLWIMIEFCPGGAVDAIMLELDrgLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAK-N 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 167887698  225 KEGMVRCDTAVGTPDYISPEVLKSQG-GDGYYGRECDWWSVGVFLYEM 271
Cdd:cd06644   161 VKTLQRRDSFIGTPYWMAPEVVMCETmKDTPYDYKADIWSLGITLIEM 208
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
82-317 2.83e-28

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: 115.16  E-value: 2.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHK-STRKVYAMKLLSKFEMIKRSDsaFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGD 160
Cdd:cd14120     1 IGHGAFAVVFKGRHRkKPDLPVAIKCITKKNLSKSQN--LLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  161 LVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSG---------HLKLADFGTCMKMNKEGMVR 230
Cdd:cd14120    79 LADyLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRLKIADFGFARFLQDGMMAA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  231 cdTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYADS---LVGTYSKIMNHKNSLTfpddNDISK 307
Cdd:cd14120   159 --TLCGSPMYMAPEVIMSL----QYDAKADLWSIGTIVYQCLTGKAPFQAQTpqeLKAFYEKNANLRPNIP----SGTSP 228
                         250
                  ....*....|
gi 167887698  308 EAKNLICAFL 317
Cdd:cd14120   229 ALKDLLLGLL 238
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
74-335 3.12e-28

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: 116.02  E-value: 3.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVV--KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFemiKRSDSaffwEERDIMAFANSPWVVQLFYAFQDD----- 146
Cdd:cd14171     4 EEYEVNwtQKLGTGISGPVRVCVKKSTGERFALKILLDR---PKART----EVRLHMMCSGHPNIVQIYDVYANSvqfpg 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  147 -----RYLYMVMEYMPGGDLVNLMS-NYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH---LKLADF 217
Cdd:cd14171    77 essprARLLIVMELMEGGELFDRISqHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEdapIKLCDF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  218 GTCmKMNKEGMVrcdTAVGTPDYISPEVLKSQ-------------GGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLV 284
Cdd:cd14171   157 GFA-KVDQGDLM---TPQFTPYYVAPQVLEAQrrhrkersgiptsPTPYTYDKSCDMWSLGVIIYIMLCGYPPFYSEHPS 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  285 GTYSKIMNHK---NSLTFPDD--NDISKEAKNLICAFL-TDREVRLgrnGVEEIKRH 335
Cdd:cd14171   233 RTITKDMKRKimtGSYEFPEEewSQISEMAKDIVRKLLcVDPEERM---TIEEVLHH 286
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
76-335 3.82e-28

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: 115.27  E-value: 3.82e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQL------VRHKSTRKVyAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYL 149
Cdd:cd14076     3 YILGRTLGEGEFGKVKLgwplpkANHRSGVQV-AIKLIRRDTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 YMVMEYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGM 228
Cdd:cd14076    82 GIVLEFVSGGELFDyILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFDHFNG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  229 VRCDTAVGTPDYISPEVLKSQggDGYYGRECDWWSVGVFLYEMLVGDTPF-------YADSLVGTYSKIMNhkNSLTFPD 301
Cdd:cd14076   162 DLMSTSCGSPCYAAPELVVSD--SMYAGRKADIWSCGVILYAMLAGYLPFdddphnpNGDNVPRLYRYICN--TPLIFPE 237
                         250       260       270
                  ....*....|....*....|....*....|....
gi 167887698  302 dnDISKEAKNLICAFLTDREVRlgRNGVEEIKRH 335
Cdd:cd14076   238 --YVTPKARDLLRRILVPNPRK--RIRLSAIMRH 267
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
80-317 3.87e-28

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: 114.82  E-value: 3.87e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFfWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 159
Cdd:cd14082     9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQESQL-RNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLHGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DLVNLMS--NYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSG---HLKLADFGTCMKMNKEGMVRcdTA 234
Cdd:cd14082    88 MLEMILSseKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFARIIGEKSFRR--SV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  235 VGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGtySKIMNhkNSLTFPDD--NDISKEAKNL 312
Cdd:cd14082   166 VGTPAYLAPEVLRNKG----YNRSLDMWSVGVIIYVSLSGTFPFNEDEDIN--DQIQN--AAFMYPPNpwKEISPDAIDL 237

                  ....*
gi 167887698  313 ICAFL 317
Cdd:cd14082   238 INNLL 242
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
76-338 4.30e-28

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: 114.88  E-value: 4.30e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLV-RHKSTRKVyAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQ-DDRYLYMVM 153
Cdd:cd14165     3 YILGINLGEGSYAKVKSAySERLKCNV-AIKIIDKKKAPDDFVEKFLPRELEILARLNHKSIIKTYEIFEtSDGKVYIVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLM-SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEG---MV 229
Cdd:cd14165    82 ELGVQGDLLEFIkLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDEngrIV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  230 RCDTAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPfYADSLVGTYSKImNHKNSLTFPDDNDISKEA 309
Cdd:cd14165   162 LSKTFCGSAAYAAPEVLQ---GIPYDPRIYDIWSLGVILYIMVCGSMP-YDDSNVKKMLKI-QKEHRVRFPRSKNLTSEC 236
                         250       260       270
                  ....*....|....*....|....*....|
gi 167887698  310 KNLICAFLT-DREVRLgrnGVEEIKRHLFF 338
Cdd:cd14165   237 KDLIYRLLQpDVSQRL---CIDEVLSHPWL 263
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
76-324 4.80e-28

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: 115.69  E-value: 4.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfemikRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd14085     5 FEIESELGRGATSVVYRCRQKGTQKPYAVKKLKK-----TVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH---LKLADFGTCMKMNKEGMVRc 231
Cdd:cd14085    80 VTGGELFDrIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLSKIVDQQVTMK- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  232 dTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVG-TYSKIMNHKNSLTFPDDNDISKEAK 310
Cdd:cd14085   159 -TVCGTPGYCAPEILRGCA----YGPEVDMWSVGVITYILLCGFEPFYDERGDQyMFKRILNCDYDFVSPWWDDVSLNAK 233
                         250
                  ....*....|....*
gi 167887698  311 NLICAFLT-DREVRL 324
Cdd:cd14085   234 DLVKKLIVlDPKKRL 248
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
75-317 5.51e-28

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: 114.44  E-value: 5.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFwEERDIMAFANSPWVVQLFYAFQDDRYLYMVME 154
Cdd:cd08220     1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAAL-NEVKVLSMLHHPNIIEYYESFLEDKALMIVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDLVNLMSN----YDVPEKWARFYTaEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHL-KLADFGTCMKMNKEGmv 229
Cdd:cd08220    80 YAPGGTLFEYIQQrkgsLLSEEEILHFFV-QILLALHHVHSKQILHRDLKTQNILLNKKRTVvKIGDFGISKILSSKS-- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  230 RCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSltfPDDNDISKEA 309
Cdd:cd08220   157 KAYTVVGTPCYISPELCEGKP----YNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFA---PISDRYSEEL 229

                  ....*...
gi 167887698  310 KNLICAFL 317
Cdd:cd08220   230 RHLILSML 237
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
75-274 6.47e-28

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: 115.12  E-value: 6.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllsKFEMIKRSDSAFFWEERDIMAFAN---SPWVVQLFYAFQDDRYLYM 151
Cdd:cd07832     1 RYKILGRIGEGAHGIVFKAKDRETGETVALK---KVALRKLEGGIPNQALREIKALQAcqgHPYVVKLRDVFPHGTGFVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  152 VMEYMPGgDLVNLMSNYDVP--EKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMV 229
Cdd:cd07832    78 VFEYMLS-SLSEVLRDEERPltEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFSEEDPR 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 167887698  230 RCDTAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVG 274
Cdd:cd07832   157 LYSHQVATRWYRAPELLY---GSRKYDEGVDLWAVGCIFAELLNG 198
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
73-350 7.05e-28

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: 115.11  E-value: 7.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   73 AEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfemIKRSDSaffwEERDI-MAFANSPWVVQLFYAFQDDRYLYM 151
Cdd:cd14177     3 TDVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDK---SKRDPS----EEIEIlMRYGQHPNIITLKDVYDDGRYVYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  152 VMEYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNML-LDKSGH---LKLADFGTCMKMNKE 226
Cdd:cd14177    76 VTELMKGGELLDrILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILyMDDSANadsIRICDFGFAKQLRGE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  227 G---MVRCDTAvgtpDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFY---ADSLVGTYSKIMNHKNSLTFP 300
Cdd:cd14177   156 NgllLTPCYTA----NFVAPEVLMRQG----YDAACDIWSLGVLLYTMLAGYTPFAngpNDTPEEILLRIGSGKFSLSGG 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 167887698  301 DDNDISKEAKNLICAFL-TDREVRLgrnGVEEIKRHlffkndqwAWETLRD 350
Cdd:cd14177   228 NWDTVSDAAKDLLSHMLhVDPHQRY---TAEQVLKH--------SWIACRD 267
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
77-313 7.20e-28

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: 114.95  E-value: 7.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   77 EVVKVIGRGAFGEVQLVRHKSTRKVYAMKLL------SKFEMIKRsdsaffweERDIMAFANSPWVVQLFYAFQDDRYLY 150
Cdd:cd06622     4 EVLDELGKGNYGSVYKVLHRPTGVTMAMKEIrleldeSKFNQIIM--------ELDILHKAVSPYIVDFYGAFFIEGAVY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGGDLVNL----MSNYDVPEKWARFYTAEVVLALDAI-HSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNK 225
Cdd:cd06622    76 MCMEYMDAGSLDKLyaggVATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLVA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  226 EgmvRCDTAVGTPDYISPEVLKSQG--GDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKI--MNHKNSLTFPD 301
Cdd:cd06622   156 S---LAKTNIGCQSYMAPERIKSGGpnQNPTYTVQSDVWSLGLSILEMALGRYPYPPETYANIFAQLsaIVDGDPPTLPS 232
                         250
                  ....*....|..
gi 167887698  302 dnDISKEAKNLI 313
Cdd:cd06622   233 --GYSDDAQDFV 242
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
75-310 1.16e-27

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: 114.00  E-value: 1.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSkfemIKRSDSAFFWEERDIMAFA--NSPWVVQLFYAFQDDRYLYMV 152
Cdd:cd14046     7 DFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIK----LRSESKNNSRILREVMLLSrlNHQHVVRYYQAWIERANLYIQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGGDLVNLMSNY---DVPEKWARFytAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG--TCMKMNKE- 226
Cdd:cd14046    83 MEYCEKSTLRDLIDSGlfqDTDRLWRLF--RQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGlaTSNKLNVEl 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  227 --GMVRCDTA------------VGTPDYISPEVLksQGGDGYYGRECDWWSVGVFLYEMLvgdtpFYADSLVGTYSKIMN 292
Cdd:cd14046   161 atQDINKSTSaalgssgdltgnVGTALYVAPEVQ--SGTKSTYNEKVDMYSLGIIFFEMC-----YPFSTGMERVQILTA 233
                         250
                  ....*....|....*....
gi 167887698  293 HKN-SLTFPDDNDISKEAK 310
Cdd:cd14046   234 LRSvSIEFPPDFDDNKHSK 252
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
80-313 1.22e-27

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: 113.87  E-value: 1.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 159
Cdd:cd14187    13 RFLGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMvRCDTAVGTP 238
Cdd:cd14187    93 SLLELHKRRKaLTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGE-RKKTLCGTP 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  239 DYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKImnHKNSLTFPddNDISKEAKNLI 313
Cdd:cd14187   172 NYIAPEVLSKKG----HSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRI--KKNEYSIP--KHINPVAASLI 238
HR1_ROCK1 cd11639
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated ...
489-554 1.24e-27

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated coiled-coil containing protein kinase 1; ROCK1 is a serine/threonine kinase and 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. ROCK1 contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a Rho-binding HR1 domain and a pleckstrin homology (PH) domain. It is auto-inhibited by HR1 and PH domains interacting with the catalytic domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212029 [Multi-domain]  Cd Length: 66  Bit Score: 106.63  E-value: 1.24e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167887698  489 MLLQHRINEYQRKAEQENEKRRNVENEVSTLKDQLEDLKKVSQNSQLANEKLSQLQKQLEEANDLL 554
Cdd:cd11639     1 MMLQHRINEYQRKAEQESEKRRNVENEVSTLKDQLEDLKKISQNSQITNEKINQLQKQLEEANDLL 66
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
75-283 1.27e-27

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: 113.58  E-value: 1.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVME 154
Cdd:cd08228     3 NFQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDLVNLMSNYD-----VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEgMV 229
Cdd:cd08228    83 LADAGDLSQMIKYFKkqkrlIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSK-TT 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 167887698  230 RCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSL 283
Cdd:cd08228   162 AAHSLVGTPYYMSPERIHENG----YNFKSDIWSLGCLLYEMAALQSPFYGDKM 211
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
80-337 1.83e-27

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: 113.25  E-value: 1.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKllsKFEMIKRSDSAFFWEERDIMAFANS----------PWVVQLFYAFQDDRYL 149
Cdd:cd06629     7 ELIGKGTYGRVYLAMNATTGEMLAVK---QVELPKTSSDRADSRQKTVVDALKSeidtlkdldhPNIVQYLGFEETEDYF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 YMVMEYMPGGDLVNLMSNY-DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKM----- 223
Cdd:cd06629    84 SIFLEYVPGGSIGSCLRKYgKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKSddiyg 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  224 NKEGMvrcdTAVGTPDYISPEVLKSQGGDgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDN 303
Cdd:cd06629   164 NNGAT----SMQGSVFWMAPEVIHSQGQG--YSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLGNKRSAPPVPEDV 237
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 167887698  304 DISKEAKNLICA-FLTDREVrlgRNGVEEIKRHLF 337
Cdd:cd06629   238 NLSPEALDFLNAcFAIDPRD---RPTAAELLSHPF 269
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
74-353 1.84e-27

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: 114.37  E-value: 1.84e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd14168    10 KIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESS--IENEIAVLRKIKHENIVALEDIYESPNHLYLVM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL---DKSGHLKLADFGTCmKMNKEGMV 229
Cdd:cd14168    88 QLVSGGELFDrIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLS-KMEGKGDV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  230 RcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEA 309
Cdd:cd14168   167 M-STACGTPGYVAPEVLAQKP----YSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSPYWDDISDSA 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 167887698  310 KNLICAFLTDREVRlgRNGVEEIKRHLFFKNDQWAWETLRDTVA 353
Cdd:cd14168   242 KDFIRNLMEKDPNK--RYTCEQALRHPWIAGDTALCKNIHESVS 283
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
76-317 2.00e-27

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: 112.68  E-value: 2.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAmkllSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd14107     4 YEVKEEIGRGTFGFVKRVTHKGNGECCA----AKFIPLRSSTRARAFQERDILARLSHRRLTCLLDQFETRKTLILILEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL--DKSGHLKLADFGTCMKMNKEGMVRcd 232
Cdd:cd14107    80 CSSEELLDrLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvsPTREDIKICDFGFAQEITPSEHQF-- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  233 TAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNL 312
Cdd:cd14107   158 SKYGSPEFVAPEIVHQEP----VSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDTPEITHLSEDAKDF 233

                  ....*
gi 167887698  313 ICAFL 317
Cdd:cd14107   234 IKRVL 238
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
76-338 2.11e-27

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-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: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 113.02  E-value: 2.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRgafgeVQLVRHKSTRKVYAMKLLSKFEMIKRsdsaffweERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd05576     6 FRVLGVIDK-----VLLVMDTRTQETFILKGLRKSSEYSR--------ERKTIIPRCVPNMVCLRKYIISEESVFLVLQH 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVN-----------------------LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHL 212
Cdd:cd05576    73 AEGGKLWSylskflndkeihqlfadlderlaAASRFYIPEECIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  213 KLADFGTCMKMNKEgmvrCDTAVGTPDYISPEVlksqGGDGYYGRECDWWSVGVFLYEMLVGdtpfyaDSLVGTYSKIMN 292
Cdd:cd05576   153 QLTYFSRWSEVEDS----CDSDAIENMYCAPEV----GGISEETEACDWWSLGALLFELLTG------KALVECHPAGIN 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 167887698  293 HKNSLTFPDdnDISKEAKNLICAFLTDREVR---LGRNGVEEIKRHLFF 338
Cdd:cd05576   219 THTTLNIPE--WVSEEARSLLQQLLQFNPTErlgAGVAGVEDIKSHPFF 265
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
76-323 3.28e-27

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: 112.22  E-value: 3.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSD-SAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVME 154
Cdd:cd14070     4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDSYvTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVR-CD 232
Cdd:cd14070    84 LCPGGNLMHrIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGILGYSDpFS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  233 TAVGTPDYISPEVLksqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYAD--SLVGTYSKIMNHKNSltfPDDNDISKEAK 310
Cdd:cd14070   164 TQCGSPAYAAPELL----ARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEpfSLRALHQKMVDKEMN---PLPTDLSPGAI 236
                         250
                  ....*....|...
gi 167887698  311 NLICAFLTDREVR 323
Cdd:cd14070   237 SFLRSLLEPDPLK 249
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
76-292 4.18e-27

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: 112.58  E-value: 4.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllsKFEMIKRSD----SAFfwEERDIMAFANSPWVVQLFYAFQDDRYLYM 151
Cdd:cd07829     1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALK---KIRLDNEEEgipsTAL--REISLLKELKHPNIVKLLDVIHTENKLYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  152 VMEYMPGgDLVNLMSNY--DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFgtcmkmnkeGMV 229
Cdd:cd07829    76 VFEYCDQ-DLKKYLDKRpgPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADF---------GLA 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167887698  230 RcdtAVGTPD-----------YISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMN 292
Cdd:cd07829   146 R---AFGIPLrtythevvtlwYRAPEILL---GSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQ 213
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
76-324 7.89e-27

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: 111.25  E-value: 7.89e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDsafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd14191     4 YDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKEN---IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVNLM--SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDN-MLLDKSG-HLKLADFGTCMKMNKEGMVRc 231
Cdd:cd14191    81 VSGGELFERIidEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENiMCVNKTGtKIKLIDFGLARRLENAGSLK- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  232 dTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNhkNSLTFPDD--NDISKEA 309
Cdd:cd14191   160 -VLFGTPEFVAPEVINYEP----IGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTS--ATWDFDDEafDEISDDA 232
                         250
                  ....*....|....*.
gi 167887698  310 KNLICAFL-TDREVRL 324
Cdd:cd14191   233 KDFISNLLkKDMKARL 248
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
74-324 1.89e-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: 110.46  E-value: 1.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVK-VIGRGAFGEVQLVRHKSTRKVYAMKLLskFEMIK-RSDSAFFWEErdimafANSPWVVQLFYAFQD----DR 147
Cdd:cd14172     3 DDYKLSKqVLGLGVNGKVLECFHRRTGQKCALKLL--YDSPKaRREVEHHWRA------SGGPHIVHILDVYENmhhgKR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  148 YLYMVMEYMPGGDL---VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL---DKSGHLKLADFGTCM 221
Cdd:cd14172    75 CLLIIMECMEGGELfsrIQERGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTDFGFAK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  222 KMNKEGMVRcdTAVGTPDYISPEVLksqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADS----LVGTYSKIMNHKNSL 297
Cdd:cd14172   155 ETTVQNALQ--TPCYTPYYVAPEVL----GPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTgqaiSPGMKRRIRMGQYGF 228
                         250       260
                  ....*....|....*....|....*...
gi 167887698  298 TFPDDNDISKEAKNLICAFL-TDREVRL 324
Cdd:cd14172   229 PNPEWAEVSEEAKQLIRHLLkTDPTERM 256
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
74-337 3.05e-26

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: 109.73  E-value: 3.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLS---KFEMIKRSDSAFFWEERDIMAFANSPwVVQLFYAFQD--DRY 148
Cdd:cd06653     2 VNWRLGKLLGRGAFGEVYLCYDADTGRELAVKQVPfdpDSQETSKEVNALECEIQLLKNLRHDR-IVQYYGCLRDpeEKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 LYMVMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMK----- 222
Cdd:cd06653    81 LSIFVEYMPGGSVKDQLKAYGaLTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRiqtic 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  223 MNKEGMvrcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDd 302
Cdd:cd06653   161 MSGTGI---KSVTGTPYWMSPEVISGEG----YGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIATQPTKPQLPD- 232
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 167887698  303 nDISKEAKNLICAFLTDREVrlgRNGVEEIKRHLF 337
Cdd:cd06653   233 -GVSDACRDFLRQIFVEEKR---RPTAEFLLRHPF 263
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
75-337 3.12e-26

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: 109.75  E-value: 3.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLS----KFEMIKRSDSAffweERDIMAFAN--SPWVVQLFYAFQD--D 146
Cdd:cd06652     3 NWRLGKLLGQGAFGRVYLCYDADTGRELAVKQVQfdpeSPETSKEVNAL----ECEIQLLKNllHERIVQYYGCLRDpqE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  147 RYLYMVMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNK 225
Cdd:cd06652    79 RTLSIFMEYMPGGSIKDQLKSYGaLTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRLQT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  226 -----EGMvrcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFP 300
Cdd:cd06652   159 iclsgTGM---KSVTGTPYWMSPEVISGEG----YGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIATQPTNPQLP 231
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 167887698  301 DdnDISKEAKNLICAFLTDREVrlgRNGVEEIKRHLF 337
Cdd:cd06652   232 A--HVSDHCRDFLKRIFVEAKL---RPSADELLRHTF 263
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
76-338 3.38e-26

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: 109.25  E-value: 3.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEV-QLVRHKSTRKVyAMKLLSK---FEMIKRSDSAFFWEERDIMAFANS---PWVVQLFYAF-QDDR 147
Cdd:cd14005     2 YEVGDLLGKGGFGTVySGVRIRDGLPV-AVKFVPKsrvTEWAMINGPVPVPLEIALLLKASKpgvPGVIRLLDWYeRPDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  148 YLyMVMEY-MPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD-KSGHLKLADFGtCMKMN 224
Cdd:cd14005    81 FL-LIMERpEPCQDLFDFITERGAlSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFG-CGALL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  225 KEGMVRcdTAVGTPDYISPEvLKSQGgdGYYGRECDWWSVGVFLYEMLVGDTPFYADslvgtySKIMnhKNSLTFPddND 304
Cdd:cd14005   159 KDSVYT--DFDGTRVYSPPE-WIRHG--RYHGRPATVWSLGILLYDMLCGDIPFEND------EQIL--RGNVLFR--PR 223
                         250       260       270
                  ....*....|....*....|....*....|....
gi 167887698  305 ISKEAKNLICAFLTDREVRlgRNGVEEIKRHLFF 338
Cdd:cd14005   224 LSKECCDLISRCLQFDPSK--RPSLEQILSHPWF 255
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
80-324 5.14e-26

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: 109.73  E-value: 5.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfeMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 159
Cdd:cd14174     8 ELLGEGAYAKVQGCVSLQNGKEYAVKIIEK--NAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLRGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 D-LVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL---DKSGHLKLADF--GTCMKMNKE----GMV 229
Cdd:cd14174    86 SiLAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCespDKVSPVKICDFdlGSGVKLNSActpiTTP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  230 RCDTAVGTPDYISPEVLKSQGGDG-YYGRECDWWSVGVFLYEMLVGDTPFYADSLV------GTYSKIMNHK-------N 295
Cdd:cd14174   166 ELTTPCGSAEYMAPEVVEVFTDEAtFYDKRCDLWSLGVILYIMLSGYPPFVGHCGTdcgwdrGEVCRVCQNKlfesiqeG 245
                         250       260       270
                  ....*....|....*....|....*....|..
gi 167887698  296 SLTFPDDN--DISKEAKNLICAFLT-DREVRL 324
Cdd:cd14174   246 KYEFPDKDwsHISSEAKDLISKLLVrDAKERL 277
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
74-271 5.47e-26

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: 109.35  E-value: 5.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDY-EVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDsafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMV 152
Cdd:cd06643     4 EDFwEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELED---YMVEIDILASCDHPNIVKLLDAFYYENNLWIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGGDLVNLMSNYDVP--EKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKmNKEGMVR 230
Cdd:cd06643    81 IEFCAGGAVDAVMLELERPltEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAK-NTRTLQR 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 167887698  231 CDTAVGTPDYISPEVLKSQ-GGDGYYGRECDWWSVGVFLYEM 271
Cdd:cd06643   160 RDSFIGTPYWMAPEVVMCEtSKDRPYDYKADVWSLGVTLIEM 201
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
73-317 5.98e-26

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: 108.93  E-value: 5.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   73 AEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMikRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMV 152
Cdd:cd14183     5 SERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKC--RGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL----DKSGHLKLADFGTCMKMNKEG 227
Cdd:cd14183    83 MELVKGGDLFDAITSTNkYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLATVVDGPL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  228 MVRCdtavGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYA--DSLVGTYSKIMNHKNSLTFPDDNDI 305
Cdd:cd14183   163 YTVC----GTPTYVAPEIIAETG----YGLKVDIWAAGVITYILLCGFPPFRGsgDDQEVLFDQILMGQVDFPSPYWDNV 234
                         250
                  ....*....|..
gi 167887698  306 SKEAKNLICAFL 317
Cdd:cd14183   235 SDSAKELITMML 246
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
76-284 7.23e-26

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 114.12  E-value: 7.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVR-HKSTRKVyAMKLLsKFEMikRSDSAF---FweERDIMAFA--NSPWVVQLFYAFQDDRYL 149
Cdd:NF033483    9 YEIGERIGRGGMAEVYLAKdTRLDRDV-AVKVL-RPDL--ARDPEFvarF--RREAQSAAslSHPNIVSVYDVGEDGGIP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 YMVMEYMPGGDLVNLM-SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGM 228
Cdd:NF033483   83 YIVMEYVDGRTLKDYIrEHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARALSSTTM 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167887698  229 VRCDTAVGTPDYISPEvlksQ--GG------DGYygrecdwwSVGVFLYEMLVGDTPFYADSLV 284
Cdd:NF033483  163 TQTNSVLGTVHYLSPE----QarGGtvdarsDIY--------SLGIVLYEMLTGRPPFDGDSPV 214
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
81-282 7.48e-26

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: 108.56  E-value: 7.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   81 VIGRGAFGEVQLVRHKSTRKV-YAMKLLSKFEMIKrsDSAFFWEERDIMAFANSPWVVQLfYAFQD-DRYLYMVMEYMPG 158
Cdd:cd14202     9 LIGHGAFAVVFKGRHKEKHDLeVAVKCINKKNLAK--SQTLLGKEIKILKELKHENIVAL-YDFQEiANSVYLVMEYCNG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  159 GDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSG---------HLKLADFGTCMKMNKEGM 228
Cdd:cd14202    86 GDLADyLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGFARYLQNNMM 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 167887698  229 VRcdTAVGTPDYISPEVLKSQGGDGyygrECDWWSVGVFLYEMLVGDTPFYADS 282
Cdd:cd14202   166 AA--TLCGSPMYMAPEVIMSQHYDA----KADLWSIGTIIYQCLTGKAPFQASS 213
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
76-272 1.04e-25

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: 107.90  E-value: 1.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVR--HKSTRKVYAMKLLSKFEMIKRSDSAffwEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd08221     2 YIPVRVLGRGAFGEAVLYRktEDNSLVVWKEVNLSRLSEKERRDAL---NEIDILSLLNHDNIITYYNHFLDGESLFIEM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDL---VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVr 230
Cdd:cd08221    79 EYCNGGNLhdkIAQQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSM- 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 167887698  231 CDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEML 272
Cdd:cd08221   158 AESIVGTPYYMSPELVQGVK----YNFKSDIWAVGCVLYELL 195
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
76-319 1.50e-25

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: 107.75  E-value: 1.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfEMIKRSDSAffwEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd14113     9 YSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNK-KLMKRDQVT---HELGVLQSLQHPQLVGLLDTFETPTSYILVLEM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVNLMSNY-DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH---LKLADFGTCMKMNKEGMVRc 231
Cdd:cd14113    85 ADQGRLLDYVVRWgNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFGDAVQLNTTYYIH- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  232 dTAVGTPDYISPEVLKsqgGDGyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFPDD--NDISKEA 309
Cdd:cd14113   164 -QLLGSPEFAAPEIIL---GNP-VSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNIC--RLDFSFPDDyfKGVSQKA 236
                         250
                  ....*....|
gi 167887698  310 KNLICAFLTD 319
Cdd:cd14113   237 KDFVCFLLQM 246
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
82-279 2.06e-25

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: 107.80  E-value: 2.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKllsKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd06657    28 IGEGSTGIVCIATVKSSGKLVAVK---KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEgMVRCDTAVGTPDYI 241
Cdd:cd06657   105 TDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKE-VPRRKSLVGTPYWM 183
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 167887698  242 SPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFY 279
Cdd:cd06657   184 APELISRLP----YGPEVDIWSLGIMVIEMVDGEPPYF 217
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
76-278 2.22e-25

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: 107.65  E-value: 2.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllsKFEMikrsdsaffWEERD-----------IMAFANSPWVVQL---FY 141
Cdd:cd07840     1 YEKIAQIGEGTYGQVYKARNKKTGELVALK---KIRM---------ENEKEgfpitaireikLLQKLDHPNVVRLkeiVT 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  142 AFQDDRY---LYMVMEYMPGgDLVNLMSNYDVP--EKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLAD 216
Cdd:cd07840    69 SKGSAKYkgsIYMVFEYMDH-DLTGLLDNPEVKftESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLAD 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887698  217 FGTCMKMNKEGMVRCDTAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd07840   148 FGLARPYTKENNADYTNRVITLWYRPPELLL---GATRYGPEVDMWSVGCILAELFTGKPIF 206
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
75-294 2.34e-25

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: 107.20  E-value: 2.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKST-RKVYAMKLLSKFEMI-----KRSDSAFfweeRDIMAFAN-------SPWVVQLFY 141
Cdd:cd08528     1 EYAVLELLGSGAFGCVYKVRKKSNgQTLLALKEINMTNPAfgrteQERDKSV----GDIISEVNiikeqlrHPNIVRYYK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  142 AFQDDRYLYMVMEYMPG---GDLVNLMS--NYDVPEK--WARFytAEVVLALDAIH-SMGFIHRDVKPDNMLLDKSGHLK 213
Cdd:cd08528    77 TFLENDRLYIVMELIEGaplGEHFSSLKekNEHFTEDriWNIF--VQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  214 LADFGTCmKMNKEGMVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNH 293
Cdd:cd08528   155 ITDFGLA-KQKGPESSKMTSVVGTILYSCPEIVQNEP----YGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEA 229

                  .
gi 167887698  294 K 294
Cdd:cd08528   230 E 230
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
75-274 2.51e-25

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: 106.70  E-value: 2.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAmkllskfemIKRSDSAFfWEERD----------IMAFANSPWVVQLFYAFQ 144
Cdd:cd13997     1 HFHELEQIGSGSFSEVFKVRSKVDGCLYA---------VKKSKKPF-RGPKEraralreveaHAALGQHPNIVRYYSSWE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  145 DDRYLYMVMEYMPGGDLVnlmsnyDVPEKWARF----------YTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKL 214
Cdd:cd13997    71 EGGHLYIQMELCENGSLQ------DALEELSPIsklseaevwdLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKI 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  215 ADFGTCMKMNKEGMVRcdtaVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVG 274
Cdd:cd13997   145 GDFGLATRLETSGDVE----EGDSRYLAPELLN---ENYTHLPKADIFSLGVTVYEAATG 197
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
74-277 2.51e-25

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: 108.29  E-value: 2.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLsKFEmIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd06615     1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMARKLI-HLE-IKPAIRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGG--DLVnLMSNYDVPEKwarfYTAEVVLA-------LDAIHSMgfIHRDVKPDNMLLDKSGHLKLADFGTcmkmn 224
Cdd:cd06615    79 EHMDGGslDQV-LKKAGRIPEN----ILGKISIAvlrgltyLREKHKI--MHRDVKPSNILVNSRGEIKLCDFGV----- 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 167887698  225 kEGMV---RCDTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTP 277
Cdd:cd06615   147 -SGQLidsMANSFVGTRSYMSPERLQGT----HYTVQSDIWSLGLSLVEMAIGRYP 197
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
81-337 2.91e-25

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: 106.72  E-value: 2.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   81 VIGRGAFGEVQLVRHKSTRKVYAMKllskfEMIKRSDSAF--FWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPG 158
Cdd:cd06624    15 VLGKGTFGVVYAARDLSTQVRIAIK-----EIPERDSREVqpLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  159 GDLVNLMSNydvpeKWA---------RFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDK-SGHLKLADFGTCMKMNKEGM 228
Cdd:cd06624    90 GSLSALLRS-----KWGplkdnentiGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTSKRLAGINP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  229 VrCDTAVGTPDYISPEVLkSQGGDGyYGRECDWWSVGVFLYEMLVGDTPFY-------ADSLVGTYsKImnHKNsltFPD 301
Cdd:cd06624   165 C-TETFTGTLQYMAPEVI-DKGQRG-YGPPADIWSLGCTIIEMATGKPPFIelgepqaAMFKVGMF-KI--HPE---IPE 235
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 167887698  302 dnDISKEAKNLI-CAFLTDREvrlGRNGVEEIKRHLF 337
Cdd:cd06624   236 --SLSEEAKSFIlRCFEPDPD---KRATASDLLQDPF 267
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
76-290 3.02e-25

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: 106.74  E-value: 3.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEM--IKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd08222     2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVLKEISVgeLQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIVT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNY-----DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLdKSGHLKLADFGTCMKMnkegM 228
Cdd:cd08222    82 EYCEGGDLDDKISEYkksgtTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL-KNNVIKVGDFGISRIL----M 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  229 VRCDTA---VGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKI 290
Cdd:cd08222   157 GTSDLAttfTGTPYYMSPEVLKHEG----YNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKI 217
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
80-338 3.04e-25

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: 106.55  E-value: 3.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 159
Cdd:cd14189     7 RLLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DLVNL-MSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMvRCDTAVGTP 238
Cdd:cd14189    87 SLAHIwKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQ-RKKTICGTP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  239 DYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTfpddNDISKEAKNLICAFLt 318
Cdd:cd14189   166 NYLAPEVLLRQG----HGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLP----ASLSLPARHLLAGIL- 236
                         250       260
                  ....*....|....*....|
gi 167887698  319 dREVRLGRNGVEEIKRHLFF 338
Cdd:cd14189   237 -KRNPGDRLTLDQILEHEFF 255
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
82-331 3.62e-25

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: 107.65  E-value: 3.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKF--EMIKRSDSAFFWEErdimafaNSPWVVQLFYAFQDDRYLYMVMEYMPGG 159
Cdd:cd14180    14 LGEGSFSVCRKCRHRQSGQEYAVKIISRRmeANTQREVAALRLCQ-------SHPNIVALHEVLHDQYHTYLVMELLRGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DLVnlmsnyDVPEKWARFYTAE-------VVLALDAIHSMGFIHRDVKPDNMLLDKSGH---LKLADFGTCmKMNKEGMV 229
Cdd:cd14180    87 ELL------DRIKKKARFSESEasqlmrsLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFA-RLRPQGSR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  230 RCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYS-------KIMNHKNSLTFPDD 302
Cdd:cd14180   160 PLQTPCFTLQYAAPELFSNQG----YDESCDLWSLGVILYTMLSGQVPFQSKRGKMFHNhaadimhKIKEGDFSLEGEAW 235
                         250       260       270
                  ....*....|....*....|....*....|
gi 167887698  303 NDISKEAKNLICAFLT-DREVRLGRNGVEE 331
Cdd:cd14180   236 KGVSEEAKDLVRGLLTvDPAKRLKLSELRE 265
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
76-272 3.63e-25

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: 106.97  E-value: 3.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllskfEMIKRSDSAffwEE----RDIMA---FANSPWVVQLFYAFQDDRY 148
Cdd:cd07831     1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIK-----CMKKHFKSL---EQvnnlREIQAlrrLSPHPNILRLIEVLFDRKT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 --LYMVMEYMPGgDLVNLMSN--YDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLdKSGHLKLADFGTCmkmn 224
Cdd:cd07831    73 grLALVFELMDM-NLYELIKGrkRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILI-KDDILKLADFGSC---- 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 167887698  225 kegmvrCDTAVGTP--DYIS------PEVLKSqggDGYYGRECDWWSVGVFLYEML 272
Cdd:cd07831   147 ------RGIYSKPPytEYIStrwyraPECLLT---DGYYGPKMDIWAVGCVFFEIL 193
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
80-318 3.89e-25

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: 107.82  E-value: 3.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfemikRSDSAffwEERDIMAFA---NSPWVVQLFYAFQDDRYLYMVMEYM 156
Cdd:cd14179    13 KPLGEGSFSICRKCLHKKTNQEYAVKIVSK-----RMEAN---TQREIAALKlceGHPNIVKLHEVYHDQLHTFLVMELL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  157 PGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL---DKSGHLKLADFGTCmKMNKEGMVRCD 232
Cdd:cd14179    85 KGGELLErIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFA-RLKPPDNQPLK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  233 TAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPF--YADSLVGTYS-KIMN--HKNSLTFPDD--NDI 305
Cdd:cd14179   164 TPCFTLHYAAPELLNYNG----YDESCDLWSLGVILYTMLSGQVPFqcHDKSLTCTSAeEIMKkiKQGDFSFEGEawKNV 239
                         250
                  ....*....|...
gi 167887698  306 SKEAKNLICAFLT 318
Cdd:cd14179   240 SQEAKDLIQGLLT 252
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
76-301 3.91e-25

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: 106.16  E-value: 3.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllsKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd06647     9 YTRFEKIGQGASGTVYTAIDVATGQEVAIK---QMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRcDTAV 235
Cdd:cd06647    86 LAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR-STMV 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  236 GTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADS-LVGTYSKIMNHKNSLTFPD 301
Cdd:cd06647   165 GTPYWMAPEVVTRKA----YGPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGTPELQNPE 227
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
71-339 5.05e-25

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: 106.75  E-value: 5.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   71 MKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLL---SKFEMIKRsdsafFWEERDIMAFANSPWVVQLFYAFQDDR 147
Cdd:cd06620     2 LKNQDLETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIhidAKSSVRKQ-----ILRELQILHECHSPYIVSFYGAFLNEN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  148 -YLYMVMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSM-GFIHRDVKPDNMLLDKSGHLKLADFGTCMKMN 224
Cdd:cd06620    77 nNIIICMEYMDCGSLDKILKKKGpFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKGQIKLCDFGVSGELI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  225 KEgmvRCDTAVGTPDYISPEvlKSQGGDgyYGRECDWWSVGVFLYEMLVGDTPFYA-----DSLVGTYS------KIMNh 293
Cdd:cd06620   157 NS---IADTFVGTSTYMSPE--RIQGGK--YSVKSDVWSLGLSIIELALGEFPFAGsndddDGYNGPMGildllqRIVN- 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 167887698  294 KNSLTFPDDNDISKEAKNLI--CAFLTDREvrlgRNGVEEIKRHLFFK 339
Cdd:cd06620   229 EPPPRLPKDRIFPKDLRDFVdrCLLKDPRE----RPSPQLLLDHDPFI 272
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
56-290 5.25e-25

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: 106.62  E-value: 5.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   56 LSRYKDTINKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLskfEMIKRSDSAFFWEERDIMAFANSPW 135
Cdd:cd06639     4 LFPYNSSMLGLESLADPSDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKIL---DPISDVDEEIEAEYNILRSLPNHPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  136 VVQLFYAF-QDDRY----LYMVMEYMPGGDLVNLMSNY-----DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNML 205
Cdd:cd06639    81 VVKFYGMFyKADQYvggqLWLVLELCNGGSVTELVKGLlkcgqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNIL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  206 LDKSGHLKLADFGTCMKMNKEGMVRcDTAVGTPDYISPEVLK-SQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLV 284
Cdd:cd06639   161 LTTEGGVKLVDFGVSAQLTSARLRR-NTSVGTPFWMAPEVIAcEQQYDYSYDARCDVWSLGITAIELADGDPPLFDMHPV 239

                  ....*.
gi 167887698  285 GTYSKI 290
Cdd:cd06639   240 KALFKI 245
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
82-339 6.27e-25

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: 106.66  E-value: 6.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKllsKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd06658    30 IGEGSTGIVCIATEKHTGKQVAVK---KMDLRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGAL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRcDTAVGTPDYI 241
Cdd:cd06658   107 TDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKR-KSLVGTPYWM 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  242 SPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNhknslTFPDDNDISKEAKNLICAFLTDRE 321
Cdd:cd06658   186 APEVISRLP----YGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRD-----NLPPRVKDSHKVSSVLRGFLDLML 256
                         250       260
                  ....*....|....*....|
gi 167887698  322 VR--LGRNGVEEIKRHLFFK 339
Cdd:cd06658   257 VRepSQRATAQELLQHPFLK 276
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
76-324 8.13e-25

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: 105.36  E-value: 8.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAmkllSKFEMIKRS-DSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVME 154
Cdd:cd14114     4 YDILEELGTGAFGVVHRCTERATGNNFA----AKFIMTPHEsDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDLVNLMS--NYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD--KSGHLKLADFGTCMKMNKEGMVR 230
Cdd:cd14114    80 FLSGGELFERIAaeHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATHLDPKESVK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  231 CDTavGTPDYISPEVLKSQgGDGYYgreCDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAK 310
Cdd:cd14114   160 VTT--GTAEFAAPEIVERE-PVGFY---TDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDSAFSGISEEAK 233
                         250
                  ....*....|....*
gi 167887698  311 NLICAFL-TDREVRL 324
Cdd:cd14114   234 DFIRKLLlADPNKRM 248
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
80-337 9.58e-25

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: 105.55  E-value: 9.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFAN--SPWVVQLFYAFQD--DRYLYMVMEY 155
Cdd:cd06651    13 KLLGQGAFGRVYLCYDVDTGRELAAKQVQFDPESPETSKEVSALECEIQLLKNlqHERIVQYYGCLRDraEKTLTIFMEY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMK-----MNKEGMv 229
Cdd:cd06651    93 MPGGSVKDQLKAYGaLTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRlqticMSGTGI- 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  230 rcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPddNDISKEA 309
Cdd:cd06651   172 --RSVTGTPYWMSPEVISGEG----YGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLP--SHISEHA 243
                         250       260
                  ....*....|....*....|....*....
gi 167887698  310 KNLI-CAFLTDREvrlgRNGVEEIKRHLF 337
Cdd:cd06651   244 RDFLgCIFVEARH----RPSAEELLRHPF 268
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
76-271 1.01e-24

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: 105.82  E-value: 1.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMK--------------LLSKFEMIKRSDSAffweerdimafaNSPWVVQL-- 139
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKkvrvplseegiplsTIREIALLKQLESF------------EHPNVVRLld 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  140 -FYAFQDDRY--LYMVMEYMPGgDLVNLMSNY---DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLK 213
Cdd:cd07838    69 vCHGPRTDRElkLTLVFEHVDQ-DLATYLDKCpkpGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVK 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  214 LADFGTCmKMNKEGMVRCdTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEM 271
Cdd:cd07838   148 LADFGLA-RIYSFEMALT-SVVVTLWYRAPEVLLQS----SYATPVDMWSVGCIFAEL 199
HR1_ROCK cd11626
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated ...
489-554 2.22e-24

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated coiled-coil containing protein kinase; ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It is a serine/threonine protein kinase that is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. ROCKs are the best-described effectors of RhoA. There are 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. ROCK contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a Rho-binding HR1 domain and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by HR1 and PH domains interacting with the catalytic domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212016 [Multi-domain]  Cd Length: 66  Bit Score: 97.43  E-value: 2.22e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167887698  489 MLLQHRINEYQRKAEQENEKRRNVENEVSTLKDQLEDLKKVSQNSQLANEKLSQLQKQLEEANDLL 554
Cdd:cd11626     1 ALLQHRQQEYQRKADMEAEKRRNVENDVAALKDQLEDLKKQKQESQKAEEKARQLQKQLEEANRLL 66
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
76-317 2.23e-24

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: 104.17  E-value: 2.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd14097     3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKINR-EKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSG-------HLKLADFGTCMKMNKEG 227
Cdd:cd14097    82 CEDGELKELLLRKGFfSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIidnndklNIKVTDFGLSVQKYGLG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  228 MVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKImnHKNSLTFPDD--NDI 305
Cdd:cd14097   162 EDMLQETCGTPIYMAPEVISAHG----YSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEI--RKGDLTFTQSvwQSV 235
                         250
                  ....*....|..
gi 167887698  306 SKEAKNLICAFL 317
Cdd:cd14097   236 SDAAKNVLQQLL 247
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
82-277 2.34e-24

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: 103.94  E-value: 2.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKfEMIKRSDsafFWEERDI-MAFANSPWVVQLF-YAFQDDRYLYMVMEYMPGG 159
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFVPK-PSTKLKD---FLREYNIsLELSVHPHIIKTYdVAFETEDYYVFAQEYAPYG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DLV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL-DKS-GHLKLADFGTCMKMnkegmvrcDTAV- 235
Cdd:cd13987    77 DLFsIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfDKDcRRVKLCDFGLTRRV--------GSTVk 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 167887698  236 ---GTPDYISPEVLKSQGGDGYYGREC-DWWSVGVFLYEMLVGDTP 277
Cdd:cd13987   149 rvsGTIPYTAPEVCEAKKNEGFVVDPSiDVWAFGVLLFCCLTGNFP 194
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
76-317 2.47e-24

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: 103.89  E-value: 2.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEV--VKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAffwEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd14192     4 YAVcpHEVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVK---NEINIMNQLNHVNLIQLYDAFESKTNLTLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMS--NYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNML-LDKSGH-LKLADFGTCMKMNKEGMV 229
Cdd:cd14192    81 EYVDGGELFDRITdeSYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILcVNSTGNqIKIIDFGLARRYKPREKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  230 RCDtaVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEA 309
Cdd:cd14192   161 KVN--FGTPEFLAPEVVNYD----FVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDAEAFENLSEEA 234

                  ....*...
gi 167887698  310 KNLICAFL 317
Cdd:cd14192   235 KDFISRLL 242
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
80-279 3.27e-24

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: 103.35  E-value: 3.27e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698    80 KVIGRGAFGEV-----QLVRHKSTRKVyAMKLLSKFEMIKRSDSafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVME 154
Cdd:pfam07714    5 EKLGEGAFGEVykgtlKGEGENTKIKV-AVKTLKEGADEEERED--FLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   155 YMPGGDLVNLM--SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCD 232
Cdd:pfam07714   82 YMPGGDLLDFLrkHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDYYRKR 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 167887698   233 TAVGTP-DYISPEVLKsqggDGYYGRECDWWSVGVFLYEML-VGDTPFY 279
Cdd:pfam07714  162 GGGKLPiKWMAPESLK----DGKFTSKSDVWSFGVLLWEIFtLGEQPYP 206
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
75-294 3.46e-24

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: 103.29  E-value: 3.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERdIMAFANSPWVVQLFYAFQD-DRYLYMVM 153
Cdd:cd08223     1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAK-LLSKLKHPNIVSYKESFEGeDGFLYIVM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEgmvr 230
Cdd:cd08223    80 GFCEGGDLYTRLKEQKgvlLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESS---- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  231 CDTA---VGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHK 294
Cdd:cd08223   156 SDMAttlIGTPYYMSPELFSNKP----YNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGK 218
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
73-278 3.54e-24

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: 104.32  E-value: 3.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   73 AEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAffweERDIM-AFANSPWVVQLFYAF-----QDD 146
Cdd:cd06638    17 SDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEEIEA----EYNILkALSDHPNVVKFYGMYykkdvKNG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  147 RYLYMVMEYMPGGDLVNLMSNY-----DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCM 221
Cdd:cd06638    93 DQLWLVLELCNGGSVTDLVKGFlkrgeRMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSA 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  222 KMNKEGMVRcDTAVGTPDYISPEVLK-SQGGDGYYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd06638   173 QLTSTRLRR-NTSVGTPFWMAPEVIAcEQQLDSTYDARCDVWSLGITAIELGDGDPPL 229
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
76-335 5.36e-24

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: 102.76  E-value: 5.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEV-QLVRHKSTRKVyAMKLLSKF----EMIKRsdsaFFWEERDIMAFANSPWVVQLFYAFQD-DRYL 149
Cdd:cd14163     2 YQLGKTIGEGTYSKVkEAFSKKHQRKV-AIKIIDKSggpeEFIQR----FLPRELQIVERLDHKNIIHVYEMLESaDGKI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 YMVMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLdKSGHLKLADFGTCMKMNKEGM 228
Cdd:cd14163    77 YLVMELAEDGDVFDCVLHGGpLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFGFAKQLPKGGR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  229 VRCDTAVGTPDYISPEVLKSQGGDgyyGRECDWWSVGVFLYEMLVGDTPFYADSLvgtySKIMNHKNS-LTFPDDNDISK 307
Cdd:cd14163   156 ELSQTFCGSTAYAAPEVLQGVPHD---SRKGDIWSMGVVLYVMLCAQLPFDDTDI----PKMLCQQQKgVSLPGHLGVSR 228
                         250       260
                  ....*....|....*....|....*...
gi 167887698  308 EAKNLICAFLTDREVRlgRNGVEEIKRH 335
Cdd:cd14163   229 TCQDLLKRLLEPDMVL--RPSIEEVSWH 254
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
81-313 6.80e-24

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: 103.00  E-value: 6.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   81 VIGRGAFGEVQLVRHKSTRKVYAMKLL------SKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVME 154
Cdd:cd06628     7 LIGSGSFGSVYLGMNASSGELMAVKQVelpsvsAENKDRKKSMLDALQREIALLRELQHENIVQYLGSSSDANHLNIFLE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDLVNLMSNY-DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKM--NKEGMVRC 231
Cdd:cd06628    87 YVPGGSVATLLNNYgAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLeaNSLSTKNN 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  232 DTAV---GTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNhKNSLTFPDdnDISKE 308
Cdd:cd06628   167 GARPslqGSVFWMAPEVVKQTS----YTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIGE-NASPTIPS--NISSE 239

                  ....*
gi 167887698  309 AKNLI 313
Cdd:cd06628   240 ARDFL 244
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
69-278 1.50e-23

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: 102.39  E-value: 1.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   69 LRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFE-----------MIKRsdsafFWEERDIMAFANSpwVV 137
Cdd:cd06636    11 LRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEdeeeeikleinMLKK-----YSHHRNIATYYGA--FI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  138 QLFYAFQDDRyLYMVMEYMPGGDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKL 214
Cdd:cd06636    84 KKSPPGHDDQ-LWLVMEFCGAGSVTDLVKNTKgnaLKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKL 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  215 ADFGTCMKMNKEgMVRCDTAVGTPDYISPEVLK-SQGGDGYYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd06636   163 VDFGVSAQLDRT-VGRRNTFIGTPYWMAPEVIAcDENPDATYDYRSDIWSLGITAIEMAEGAPPL 226
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
74-278 1.81e-23

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 103.75  E-value: 1.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLL--SKFEMIKRSdsafFWEERDIMAFANSPWVVQLFYAFQDDRYLYM 151
Cdd:PLN00034   74 SELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIygNHEDTVRRQ----ICREIEILRDVNHPNVVKCHDMFDHNGEIQV 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  152 VMEYMPGGDLVNLMSNYdvpEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEgMVRC 231
Cdd:PLN00034  150 LLEFMDGGSLEGTHIAD---EQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQT-MDPC 225
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 167887698  232 DTAVGTPDYISPEVLKSQGGDGYY-GRECDWWSVGVFLYEMLVGDTPF 278
Cdd:PLN00034  226 NSSVGTIAYMSPERINTDLNHGAYdGYAGDIWSLGVSILEFYLGRFPF 273
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
74-338 1.88e-23

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: 101.05  E-value: 1.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVV-KVIGRGAFGEVQLVRHKSTRKVYAMKLlskfemikRSDSAFFWEERDIMAFANSPWVVQLFYAFQDD-RYLYM 151
Cdd:cd14109     3 ELYEIGeEDEKRAAQGAPFHVTERSTGRNFLAQL--------RYGDPFLMREVDIHNSLDHPNIVQMHDAYDDEkLAVTV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  152 VMEYMPGGDLV--NLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLdKSGHLKLADFGTCMKMNKEGM 228
Cdd:cd14109    75 IDNLASTIELVrdNLLPGKDYyTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILL-QDDKLKLADFGQSRRLLRGKL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  229 VRCDtaVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKE 308
Cdd:cd14109   154 TTLI--YGSPEFVSPEIVNSYP----VTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDSSPLGNISDD 227
                         250       260       270
                  ....*....|....*....|....*....|
gi 167887698  309 AKNLICAFLTDREVRlgRNGVEEIKRHLFF 338
Cdd:cd14109   228 ARDFIKKLLVYIPES--RLTVDEALNHPWF 255
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
82-318 1.96e-23

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: 102.12  E-value: 1.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKF--EMIKRSdsafFWEERDIMAFANSPWVVQLFYAFQDDR--YLYMVMEYMP 157
Cdd:cd06621     9 LGEGAGGSVTKCRLRNTKTIFALKTITTDpnPDVQKQ----ILRELEINKSCASPYIVKYYGAFLDEQdsSIGIAMEYCE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  158 GGDLVNLMSNydVPEKWARfyTAEVVL---------ALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKM-NKEG 227
Cdd:cd06621    85 GGSLDSIYKK--VKKKGGR--IGEKVLgkiaesvlkGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSGELvNSLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  228 MvrcdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADS-----LVGTYSKIMNHKNsLTFPDD 302
Cdd:cd06621   161 G----TFTGTSYYMAPERIQGGP----YSITSDVWSLGLTLLEVAQNRFPFPPEGepplgPIELLSYIVNMPN-PELKDE 231
                         250       260
                  ....*....|....*....|
gi 167887698  303 --NDI--SKEAKNLICAFLT 318
Cdd:cd06621   232 peNGIkwSESFKDFIEKCLE 251
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
82-317 2.17e-23

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: 100.81  E-value: 2.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKfEMIKRSDSAffwEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKFVSK-KMKKKEQAA---HEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD---KSGHLKLADFGTCMKMNkeGMVRCDTAVGT 237
Cdd:cd14115    77 LDYLMNHDeLMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQIS--GHRHVHHLLGN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  238 PDYISPEVLksQGGDGYYGreCDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFPDD--NDISKEAKNLICA 315
Cdd:cd14115   155 PEFAAPEVI--QGTPVSLA--TDIWSIGVLTYVMLSGVSPFLDESKEETCINVC--RVDFSFPDEyfGDVSQAARDFINV 228

                  ..
gi 167887698  316 FL 317
Cdd:cd14115   229 IL 230
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
75-283 2.33e-23

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: 102.03  E-value: 2.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVME 154
Cdd:cd08229    25 NFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDLVNLMSNYD-----VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmKMNKEGMV 229
Cdd:cd08229   105 LADAGDLSRMIKHFKkqkrlIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLG-RFFSSKTT 183
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 167887698  230 RCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSL 283
Cdd:cd08229   184 AAHSLVGTPYYMSPERIHENG----YNFKSDIWSLGCLLYEMAALQSPFYGDKM 233
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
74-291 2.65e-23

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: 101.73  E-value: 2.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPwVVQLFYAFQDDRYLYMVM 153
Cdd:cd07846     1 EKYENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKKIAMREIKMLKQLRHEN-LVNLIEVFRRKKRWYLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMpGGDLVNLMSNYD--VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVrC 231
Cdd:cd07846    80 EFV-DHTVLDDLEKYPngLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEV-Y 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  232 DTAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIM 291
Cdd:cd07846   158 TDYVATRWYRAPELLV---GDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHII 214
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
83-294 2.71e-23

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: 100.67  E-value: 2.71e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   83 GRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSdsafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLV 162
Cdd:cd14111    12 ARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQG----VLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGKELL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  163 -NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYI 241
Cdd:cd14111    88 hSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLSLRQLGRRTGTLEYM 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 167887698  242 SPEVLKsqgGDgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHK 294
Cdd:cd14111   168 APEMVK---GE-PVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAK 216
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
82-278 2.71e-23

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: 101.29  E-value: 2.71e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd06642    12 IGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEDEIED--IQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGGSA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRcDTAVGTPDYI 241
Cdd:cd06642    90 LDLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKR-NTFVGTPFWM 168
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 167887698  242 SPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd06642   169 APEVIKQSA----YDFKADIWSLGITAIELAKGEPPN 201
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
74-277 2.76e-23

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: 101.30  E-value: 2.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd06641     4 ELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIED--IQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRcDT 233
Cdd:cd06641    82 EYLGGGSALDLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKR-N* 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 167887698  234 AVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTP 277
Cdd:cd06641   161 FVGTPFWMAPEVIKQSA----YDSKADIWSLGITAIELARGEPP 200
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
74-339 5.50e-23

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: 100.95  E-value: 5.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSdsaFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd06656    19 KKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKE---LIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRcDT 233
Cdd:cd06656    96 EYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR-ST 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  234 AVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADS-LVGTYSKIMNHKNSLTFPDD-NDISKEAKN 311
Cdd:cd06656   175 MVGTPYWMAPEVVTRKA----YGPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGTPELQNPERlSAVFRDFLN 250
                         250       260
                  ....*....|....*....|....*...
gi 167887698  312 LICAFLTDRevrlgRNGVEEIKRHLFFK 339
Cdd:cd06656   251 RCLEMDVDR-----RGSAKELLQHPFLK 273
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
75-282 6.31e-23

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: 100.08  E-value: 6.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRH-KSTRKVYAMKLLSKFEMIKrsDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd14201     7 EYSRKDLVGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSK--SQILLGKEIKILKELQHENIVALYDVQEMPNSVFLVM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSG---------HLKLADFGTCMKM 223
Cdd:cd14201    85 EYCNGGDLADyLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIADFGFARYL 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 167887698  224 NKEGMVRcdTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYADS 282
Cdd:cd14201   165 QSNMMAA--TLCGSPMYMAPEVIMSQ----HYDAKADLWSIGTVIYQCLVGKPPFQANS 217
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
80-278 6.52e-23

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: 100.49  E-value: 6.52e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfeMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 159
Cdd:cd14173     8 EVLGEGAYARVQTCINLITNKEYAVKIIEK--RPGHSRSRVFREVEMLYQCQGHRNVLELIEFFEEEDKFYLVFEKMRGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHL---KLADF--GTCMKMNKE----GMV 229
Cdd:cd14173    86 SILShIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVspvKICDFdlGSGIKLNSDcspiSTP 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 167887698  230 RCDTAVGTPDYISPEVLKSQGGDG-YYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd14173   166 ELLTPCGSAEYMAPEVVEAFNEEAsIYDKRCDLWSLGVILYIMLSGYPPF 215
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
75-270 7.41e-23

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: 100.19  E-value: 7.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKS-TRKVYAMKLLsKFEMIKRSDSAFFWEERDI---MAFANSPWVVQLFYAFQDDRYLY 150
Cdd:cd14052     1 RFANVELIGSGEFSQVYKVSERVpTGKVYAVKKL-KPNYAGAKDRLRRLEEVSIlreLTLDGHDNIVQLIDSWEYHGHLY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGGDLVNLMSNY------DVPEKWARFytAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMN 224
Cdd:cd14052    80 IQTELCENGSLDVFLSELgllgrlDEFRVWKIL--VELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVWP 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 167887698  225 KEGMVRCDtavGTPDYISPEVLksqgGDGYYGRECDWWSVGVFLYE 270
Cdd:cd14052   158 LIRGIERE---GDREYIAPEIL----SEHMYDKPADIFSLGLILLE 196
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
80-302 8.47e-23

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: 99.55  E-value: 8.47e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698     80 KVIGRGAFGEVQL-----VRHKSTRKVyAMKllskfeMIKRSDSAF----FWEERDIMAFANSPWVVQLFYAFQDDRYLY 150
Cdd:smart00221    5 KKLGEGAFGEVYKgtlkgKGDGKEVEV-AVK------TLKEDASEQqieeFLREARIMRKLDHPNIVKLLGVCTEEEPLM 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698    151 MVMEYMPGGDLVN-LMSNYDVPEKWARF--YTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEG 227
Cdd:smart00221   78 IVMEYMPGGDLLDyLRKNRPKELSLSDLlsFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDD 157
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167887698    228 MVRCDTAVGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLYEML-VGDTPFYADSLVGTYSKIMNhKNSLTFPDD 302
Cdd:smart00221  158 YYKVKGGKLPIRWMAPESLK----EGKFTSKSDVWSFGVLLWEIFtLGEEPYPGMSNAEVLEYLKK-GYRLPKPPN 228
ROCK_SBD cd22250
Shroom-binding domain found in Rho-associated coiled-coil containing protein kinase; ...
836-913 9.36e-23

Shroom-binding domain found in Rho-associated coiled-coil containing protein kinase; Rho-associated coiled-coil containing protein kinase (ROCK) is a serine/threonine kinase (STK) that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. It is also referred to as Rho-associated protein kinase or simply as Rho kinase. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Rho-associated protein kinase 1 (ROCK1) is also called renal carcinoma antigen NY-REN-35, Rho-associated, coiled-coil-containing protein kinase 1, ROCK-I, p160 ROCK-1, or p160ROCK, 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 in ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. Rho-associated protein kinase 2 (ROCK2), also called Rho kinase 2, Rho-associated, coiled-coil-containing protein kinase 2, ROCK-II, or p164 ROCK-2, is more prominent in brain and skeletal muscle. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK subfamily proteins contain an N-terminal extension, a catalytic kinase domain, a coiled-coil (CC) 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 proteolytic cleavage, binding of lipids to the PH domain, or binding of GTP-bound RhoA to the CC region. More recently, the Shroom family of proteins have been identified as an additional regulator of ROCK. This model corresponds to the Shroom-binding domain (SBD) of ROCK, which forms a parallel coiled coil with the Shroom domain 2 (SD2) of Shroom.


Pssm-ID: 409019 [Multi-domain]  Cd Length: 75  Bit Score: 93.09  E-value: 9.36e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  836 EGQMRELQDQLEAEQYFSTLYKTQVKELKEEIEEKNRENLkkiQELQNEKETLATQLDLAETKAESEQLARGLLEEQY 913
Cdd:cd22250     1 DLQMKELQDQLEAEQYFSTLYKTQVKELKEELEEKTRQIK---QELEDERESLSAQLELALAKADSEQLARSIAEEQI 75
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
76-317 1.51e-22

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: 99.57  E-value: 1.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllsKFEMIKRSD-------SAFfwEERDIMAFANSPWVVQLFYAFQDDRY 148
Cdd:cd07841     2 YEKGKKLGEGTYAVVYKARDKETGRIVAIK---KIKLGERKEakdginfTAL--REIKLLQELKHPNIIGLLDVFGHKSN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 LYMVMEYMPGgDLVNLMSNYDVPEKWA--RFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmKMNKE 226
Cdd:cd07841    77 INLVFEFMET-DLEKVIKDKSIVLTPAdiKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLA-RSFGS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  227 GMVRCDTAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGdTPFyadslvgtyskimnhknsltFPDDNDIS 306
Cdd:cd07841   155 PNRKMTHQVVTRWYRAPELLF---GARHYGVGVDMWSVGCIFAELLLR-VPF--------------------LPGDSDID 210
                         250
                  ....*....|.
gi 167887698  307 KEAKnlICAFL 317
Cdd:cd07841   211 QLGK--IFEAL 219
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
62-278 1.58e-22

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: 99.80  E-value: 1.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   62 TINKIRDLRMKAEDYEVvkvIGRGAFGEVQLVRHKSTRKVYAMKllsKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFY 141
Cdd:cd06655    10 TIVSIGDPKKKYTRYEK---IGQGASGTVFTAIDVATGQEVAIK---QINLQKQPKKELIINEILVMKELKNPNIVNFLD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  142 AFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCM 221
Cdd:cd06655    84 SFLVGDELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCA 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  222 KMNKEGMVRcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd06655   164 QITPEQSKR-STMVGTPYWMAPEVVTRKA----YGPKVDIWSLGIMAIEMVEGEPPY 215
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
76-313 1.73e-22

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: 100.29  E-value: 1.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEmikrsDSAFF----WEERDIMAFANSPWVVQLFYAFQDDRY--- 148
Cdd:cd07834     2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISNVF-----DDLIDakriLREIKILRHLKHENIIGLLDILRPPSPeef 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 --LYMVMEYMPGgDLVNLM-SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNK 225
Cdd:cd07834    77 ndVYIVTELMET-DLHKVIkSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLARGVDP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  226 EGMVRCDTA-VGTPDYISPEVLksqGGDGYYGRECDWWSVGVFLYEMLVGDTPF----YADSLvgtySKIMNHknsLTFP 300
Cdd:cd07834   156 DEDKGFLTEyVVTRWYRAPELL---LSSKKYTKAIDIWSVGCIFAELLTRKPLFpgrdYIDQL----NLIVEV---LGTP 225
                         250
                  ....*....|....*..
gi 167887698  301 DDNDI----SKEAKNLI 313
Cdd:cd07834   226 SEEDLkfisSEKARNYL 242
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
76-313 1.94e-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: 98.93  E-value: 1.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEV----QLVRHK-STRKVY----AMKLLSKFEMIKRSDsaffwEERDIMAFANSPWVVQLFYAFQ-D 145
Cdd:cd13990     2 YLLLNLLGKGGFSEVykafDLVEQRyVACKIHqlnkDWSEEKKQNYIKHAL-----REYEIHKSLDHPRIVKLYDVFEiD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  146 DRYLYMVMEYMPGGDL-VNLMSNYDVPEKWARFYTAEVVLALDAI--HSMGFIHRDVKPDNMLLDK---SGHLKLADFGT 219
Cdd:cd13990    77 TDSFCTVLEYCDGNDLdFYLKQHKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSgnvSGEIKITDFGL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  220 CMKMNKE-----GMVRCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGT--YSKIMN 292
Cdd:cd13990   157 SKIMDDEsynsdGMELTSQGAGTYWYLPPECFVVGKTPPKISSKVDVWSVGVIFYQMLYGRKPFGHNQSQEAilEENTIL 236
                         250       260
                  ....*....|....*....|.
gi 167887698  293 HKNSLTFPDDNDISKEAKNLI 313
Cdd:cd13990   237 KATEVEFPSKPVVSSEAKDFI 257
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
82-291 2.12e-22

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: 98.28  E-value: 2.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKStrKVYAMKLLsKFEMIKRSdsafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd14058     1 VGRGSFGVVCKARWRN--QIVAVKII-ESESEKKA----FEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNYDVpeKWArfYTAEVVL--------ALDAIHSMG---FIHRDVKPDNMLLDKSGH-LKLADFGT-C-----MKM 223
Cdd:cd14058    74 YNVLHGKEP--KPI--YTAAHAMswalqcakGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTvLKICDFGTaCdisthMTN 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  224 NKegmvrcdtavGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFyaDSLVGTYSKIM 291
Cdd:cd14058   150 NK----------GSAAWMAPEVFEGSK----YSEKCDVFSWGIILWEVITRRKPF--DHIGGPAFRIM 201
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
71-277 3.84e-22

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: 98.97  E-value: 3.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   71 MKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLsKFEmIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLY 150
Cdd:cd06650     2 LKDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLI-HLE-IKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGGDLVNLMSNY-DVPEKWARFYTAEVVLALDAIHSM-GFIHRDVKPDNMLLDKSGHLKLADFGTCMKMnKEGM 228
Cdd:cd06650    80 ICMEHMDGGSLDQVLKKAgRIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQL-IDSM 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 167887698  229 VrcDTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTP 277
Cdd:cd06650   159 A--NSFVGTRSYMSPERLQGT----HYSVQSDIWSMGLSLVEMAVGRYP 201
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
80-302 5.10e-22

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 97.22  E-value: 5.10e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698     80 KVIGRGAFGEVQL-----VRHKSTRKVyAMKllskfeMIKRSDSAF----FWEERDIMAFANSPWVVQLFYAFQDDRYLY 150
Cdd:smart00219    5 KKLGEGAFGEVYKgklkgKGGKKKVEV-AVK------TLKEDASEQqieeFLREARIMRKLDHPNVVKLLGVCTEEEPLY 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698    151 MVMEYMPGGDLVNLMSNYDVPEKWARF--YTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGM 228
Cdd:smart00219   78 IVMEYMEGGDLLSYLRKNRPKLSLSDLlsFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDY 157
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887698    229 VRCDTAVGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLYEML-VGDTPFYADSLVGTYSKIMNhKNSLTFPDD 302
Cdd:smart00219  158 YRKRGGKLPIRWMAPESLK----EGKFTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVLEYLKN-GYRLPQPPN 227
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
74-278 5.89e-22

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: 97.87  E-value: 5.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSdsaFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd06654    20 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKE---LIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRcDT 233
Cdd:cd06654    97 EYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR-ST 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 167887698  234 AVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd06654   176 MVGTPYWMAPEVVTRKA----YGPKVDIWSLGIMAIEMIEGEPPY 216
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
80-324 1.33e-21

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: 96.14  E-value: 1.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVqlvrHKSTRKVYAMKLLSKfeMIKR---SDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYM 156
Cdd:cd14190    10 EVLGGGKFGKV----HTCTEKRTGLKLAAK--VINKqnsKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  157 PGGDLVNLMSNYDVP--EKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL-DKSGHL-KLADFGTCMKMNKEGMVRCD 232
Cdd:cd14190    84 EGGELFERIVDEDYHltEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvNRTGHQvKIIDFGLARRYNPREKLKVN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  233 taVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFPDD--NDISKEAK 310
Cdd:cd14190   164 --FGTPEFLSPEVVNYD----QVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVL--MGNWYFDEEtfEHVSDEAK 235
                         250
                  ....*....|....*
gi 167887698  311 NLICAFLT-DREVRL 324
Cdd:cd14190   236 DFVSNLIIkERSARM 250
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
74-279 2.24e-21

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: 96.46  E-value: 2.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLS--KFEMIKRsdsaffweERDIM-AFANSPWVVQLFYAFQDD--RY 148
Cdd:cd14132    18 DDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKpvKKKKIKR--------EIKILqNLRGGPNIVKLLDVVKDPqsKT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 LYMVMEYMPGGDLVNL---MSNYDVpekwaRFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH-LKLADFGTC--MK 222
Cdd:cd14132    90 PSLIFEYVNNTDFKTLyptLTDYDI-----RYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRkLRLIDWGLAefYH 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  223 MNKEGMVRcdtaVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFY 279
Cdd:cd14132   165 PGQEYNVR----VASRYYKGPELLV---DYQYYDYSLDMWSLGCMLASMIFRKEPFF 214
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
70-279 3.83e-21

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: 95.11  E-value: 3.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   70 RMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLsKFEmiKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYL 149
Cdd:cd06645     7 RNPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVI-KLE--PGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 YMVMEYMPGGDLVNLMS-NYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEgM 228
Cdd:cd06645    84 WICMEFCGGGSLQDIYHvTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITAT-I 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 167887698  229 VRCDTAVGTPDYISPEV--LKSQGGdgyYGRECDWWSVGVFLYEMLVGDTPFY 279
Cdd:cd06645   163 AKRKSFIGTPYWMAPEVaaVERKGG---YNQLCDIWAVGITAIELAELQPPMF 212
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
71-277 4.20e-21

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: 96.27  E-value: 4.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   71 MKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfeMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLY 150
Cdd:cd06649     2 LKDDDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHL--EIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSM-GFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEgm 228
Cdd:cd06649    80 ICMEHMDGGSLDQVLKEAKrIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDS-- 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 167887698  229 vRCDTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTP 277
Cdd:cd06649   158 -MANSFVGTRSYMSPERLQGT----HYSVQSDIWSMGLSLVELAIGRYP 201
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
73-278 5.98e-21

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: 94.74  E-value: 5.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   73 AEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMV 152
Cdd:cd06616     5 AEDLKDLGEIGRGAFGTVNKMLHKPSGTIMAVKRIRS-TVDEKEQKRLLMDLDVVMRSSDCPYIVKFYGALFREGDCWIC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGG-----DLVNLMSNYDVPEKWARFYTAEVVLALDAI-HSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMnke 226
Cdd:cd06616    84 MELMDISldkfyKYVYEVLDSVIPEEILGKIAVATVKALNYLkEELKIIHRDVKPSNILLDRNGNIKLCDFGISGQL--- 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  227 gmvrCDTAVGTPD-----YISPE-VLKSQGGDGYYGREcDWWSVGVFLYEMLVGDTPF 278
Cdd:cd06616   161 ----VDSIAKTRDagcrpYMAPErIDPSASRDGYDVRS-DVWSLGITLYEVATGKFPY 213
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
82-313 6.25e-21

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: 94.35  E-value: 6.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd06640    12 IGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDEIED--IQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGSA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRcDTAVGTPDYI 241
Cdd:cd06640    90 LDLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKR-NTFVGTPFWM 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  242 SPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTP---------------FYADSLVGTYSKIMNHKNSLTFPDDNDIS 306
Cdd:cd06640   169 APEVIQQSA----YDSKADIWSLGITAIELAKGEPPnsdmhpmrvlflipkNNPPTLVGDFSKPFKEFIDACLNKDPSFR 244

                  ....*..
gi 167887698  307 KEAKNLI 313
Cdd:cd06640   245 PTAKELL 251
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
80-290 6.36e-21

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: 94.22  E-value: 6.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 159
Cdd:cd14198    14 KELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLELAKSNPRVVNLHEVYETTSEIILILEYAAGG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DLVNLMsnydVPEKWARFYTAEVVLALDAI-------HSMGFIHRDVKPDNMLLDKS---GHLKLADFGTCMKMNKEGMV 229
Cdd:cd14198    94 EIFNLC----VPDLAEMVSENDIIRLIRQIlegvyylHQNNIVHLDLKPQNILLSSIyplGDIKIVDFGMSRKIGHACEL 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167887698  230 RcdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKI 290
Cdd:cd14198   170 R--EIMGTPEYLAPEILNYDP----ITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNI 224
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
76-324 7.52e-21

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: 95.70  E-value: 7.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllsK-FEMIKRSDSA---FfweeRDIM---AFANSPWVVQLF--YAFQDD 146
Cdd:cd07852     9 YEILKKLGKGAYGIVWKAIDKKTGEVVALK---KiFDAFRNATDAqrtF----REIMflqELNDHPNIIKLLnvIRAEND 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  147 RYLYMVMEYMPGgDL-----VNLMSNYDVpekwaRFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG--- 218
Cdd:cd07852    82 KDIYLVFEYMET-DLhavirANILEDIHK-----QYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGlar 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  219 --TCMKMNKEGMVRCDTaVGTPDYISPEVL-KSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhkN 295
Cdd:cd07852   156 slSQLEEDDENPVLTDY-VATRWYRAPEILlGST----RYTKGVDMWSVGCILGEMLLGKPLFPGTSTLNQLEKII---E 227
                         250       260       270
                  ....*....|....*....|....*....|...
gi 167887698  296 SLTFPDDNDI----SKEAKNLICAFLTDREVRL 324
Cdd:cd07852   228 VIGRPSAEDIesiqSPFAATMLESLPPSRPKSL 260
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
74-290 7.89e-21

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: 93.93  E-value: 7.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfemiKRSDSAFFWEERD-------IMAFANSPWVVQLFYAFQDD 146
Cdd:cd14194     5 DYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKK----RRTKSSRRGVSREdierevsILKEIQHPNVITLHEVYENK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  147 RYLYMVMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDN-MLLDKSG---HLKLADFGTCM 221
Cdd:cd14194    81 TDVILILELVAGGELFDFLAEKEsLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENiMLLDRNVpkpRIKIIDFGLAH 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167887698  222 KMNKEGMVRcdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKI 290
Cdd:cd14194   161 KIDFGNEFK--NIFGTPEFVAPEIVNYEP----LGLEADMWSIGVITYILLSGASPFLGDTKQETLANV 223
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
74-278 8.09e-21

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: 94.36  E-value: 8.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllskfeMIKRSDSAffwEER-------DIMAFAN-SPWVVQLFYAFQD 145
Cdd:cd06618    15 NDLENLGEIGSGTCGQVYKMRHKKTGHVMAVK------QMRRSGNK---EENkrilmdlDVVLKSHdCPYIVKCYGYFIT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  146 DRYLYMVMEYMPG-GDLVNLMSNYDVPEKWARFYTAEVVLALDAI-HSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKM 223
Cdd:cd06618    86 DSDVFICMELMSTcLDKLLKRIQGPIPEDILGKMTVSIVKALHYLkEKHGVIHRDVKPSNILLDESGNVKLCDFGISGRL 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  224 nKEGMVRCDTAvGTPDYISPEVLKSQGGDGYYGReCDWWSVGVFLYEMLVGDTPF 278
Cdd:cd06618   166 -VDSKAKTRSA-GCAAYMAPERIDPPDNPKYDIR-ADVWSLGISLVELATGQFPY 217
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
72-335 9.87e-21

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: 93.48  E-value: 9.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   72 KAED-YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWE---ERDIMAFANSPWVVQLFYAFQDDR 147
Cdd:cd14196     2 KVEDfYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEierEVSILRQVLHPNIITLHDVYENRT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  148 YLYMVMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDN-MLLDKSG---HLKLADFGTCMK 222
Cdd:cd14196    82 DVVLILELVSGGELFDFLAQKEsLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIpipHIKLIDFGLAHE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  223 MnkEGMVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKI--MNHKnsltFP 300
Cdd:cd14196   162 I--EDGVEFKNIFGTPEFVAPEIVNYEP----LGLEADMWSIGVITYILLSGASPFLGDTKQETLANItaVSYD----FD 231
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 167887698  301 DD--NDISKEAKNLICAFLTdREVRlGRNGVEEIKRH 335
Cdd:cd14196   232 EEffSHTSELAKDFIRKLLV-KETR-KRLTIQEALRH 266
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
76-324 1.32e-20

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin 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: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 93.39  E-value: 1.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAmkllSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd14104     2 YMIAEELGRGQFGIVHRCVETSSKKTYM----AKFVKVKGADQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVNLMS--NYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL--DKSGHLKLADFGTCMKMNKEGMVRc 231
Cdd:cd14104    78 ISGVDIFERITtaRFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYctRRGSYIKIIEFGQSRQLKPGDKFR- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  232 dTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKN 311
Cdd:cd14104   157 -LQYTSAEFYAPEVHQHE----SVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDEAFKNISIEALD 231
                         250
                  ....*....|....
gi 167887698  312 LICAFLT-DREVRL 324
Cdd:cd14104   232 FVDRLLVkERKSRM 245
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
76-323 1.35e-20

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: 93.04  E-value: 1.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfeMIKRSDSAFfwEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd14108     4 YDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPV--RAKKKTSAR--RELALLAELDHKSIVRFHDAFEKRRVVIIVTEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL--DKSGHLKLADFGTCMKMNKEGMVRCDt 233
Cdd:cd14108    80 CHEELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMadQKTDQVRICDFGNAQELTPNEPQYCK- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  234 aVGTPDYISPEVLKSQGGDGYygreCDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLI 313
Cdd:cd14108   159 -YGTPEFVAPEIVNQSPVSKV----TDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEESMFKDLCREAKGFI 233
                         250
                  ....*....|
gi 167887698  314 CAFLTDREVR 323
Cdd:cd14108   234 IKVLVSDRLR 243
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
80-278 1.37e-20

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: 92.99  E-value: 1.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEV---QLVRHKSTRKVYAMKLLSKFEMIK-RSDsafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd00192     1 KKLGEGAFGEVykgKLKGGDGKTVDVAVKTLKEDASESeRKD---FLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVNLMSNYDVPEKWARF----------YTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNK 225
Cdd:cd00192    78 MEGGDLLDFLRKSRPVFPSPEPstlslkdllsFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIYD 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  226 EGMVRCDTavGTPDYI---SPEVLKsqggDGYYGRECDWWSVGVFLYEMLV-GDTPF 278
Cdd:cd00192   158 DDYYRKKT--GGKLPIrwmAPESLK----DGIFTSKSDVWSFGVLLWEIFTlGATPY 208
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
72-274 2.00e-20

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: 93.53  E-value: 2.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   72 KAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllsKFEMIKRSD----SAFfwEERDIMAFANSPWVVQL---FYAFQ 144
Cdd:cd07866     6 KLRDYEILGKLGEGTFGEVYKARQIKTGRVVALK---KILMHNEKDgfpiTAL--REIKILKKLKHPNVVPLidmAVERP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  145 DDRY-----LYMVMEYMpGGDLVNLMSNYDV--PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADF 217
Cdd:cd07866    81 DKSKrkrgsVYMVTPYM-DHDLSGLLENPSVklTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADF 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887698  218 G------TCMKMNKEGmvrcdTAVGTPDYIS---------PEVLKsqgGDGYYGRECDWWSVGVFLYEMLVG 274
Cdd:cd07866   160 GlarpydGPPPNPKGG-----GGGGTRKYTNlvvtrwyrpPELLL---GERRYTTAVDIWGIGCVFAEMFTR 223
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
70-279 2.09e-20

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: 92.78  E-value: 2.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   70 RMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLsKFEmiKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYL 149
Cdd:cd06646     5 RNPQHDYELIQRVGSGTYGDVYKARNLHTGELAAVKII-KLE--PGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 YMVMEYMPGGDLVNLmsnYDVPEKWARFYTA----EVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNK 225
Cdd:cd06646    82 WICMEYCGGGSLQDI---YHVTGPLSELQIAyvcrETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITA 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 167887698  226 EgMVRCDTAVGTPDYISPEVLKSQGGDGyYGRECDWWSVGVFLYEMLVGDTPFY 279
Cdd:cd06646   159 T-IAKRKSFIGTPYWMAPEVAAVEKNGG-YNQLCDIWAVGITAIELAELQPPMF 210
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
69-278 2.74e-20

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: 92.86  E-value: 2.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   69 LRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLS----KFEMIKRSDSAF--FWEERDIMAFANSpwVVQLFYA 142
Cdd:cd06637     1 LRDPAGIFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDvtgdEEEEIKQEINMLkkYSHHRNIATYYGA--FIKKNPP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  143 FQDDRyLYMVMEYMPGGDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGT 219
Cdd:cd06637    79 GMDDQ-LWLVMEFCGAGSVTDLIKNTKgntLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGV 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  220 CMKMNKEgMVRCDTAVGTPDYISPEVLK-SQGGDGYYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd06637   158 SAQLDRT-VGRRNTFIGTPYWMAPEVIAcDENPDATYDFKSDLWSLGITAIEMAEGAPPL 216
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
80-317 3.93e-20

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: 91.51  E-value: 3.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAffwEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 159
Cdd:cd14193    10 EILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVK---NEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DLVNLM--SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL--DKSGHLKLADFGTCMKMNKEGMVRCDtaV 235
Cdd:cd14193    87 ELFDRIidENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCvsREANQVKIIDFGLARRYKPREKLRVN--F 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  236 GTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICA 315
Cdd:cd14193   165 GTPEFLAPEVVNYE----FVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEDEEFADISEEAKDFISK 240

                  ..
gi 167887698  316 FL 317
Cdd:cd14193   241 LL 242
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
77-278 4.29e-20

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: 92.74  E-value: 4.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   77 EVVKVIGRGAFGE--VQLVRHKSTRKVYAMKllsKFEMIKRS--DSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMV 152
Cdd:cd08216     1 ELLYEIGKCFKGGgvVHLAKHKPTNTLVAVK---KINLESDSkeDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYVV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGGDLVNLMSNY---DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMv 229
Cdd:cd08216    78 TPLMAYGSCRDLLKTHfpeGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVKHGK- 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 167887698  230 RCDTAVGTPDYI-------SPEVLKsQGGDGyYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd08216   157 RQRVVHDFPKSSeknlpwlSPEVLQ-QNLLG-YNEKSDIYSVGITACELANGVVPF 210
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
72-290 4.43e-20

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: 91.78  E-value: 4.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   72 KAED-YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfemiKRSDSAFFWEERD-------IMAFANSPWVVQLFYAF 143
Cdd:cd14105     2 NVEDfYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKK----RRSKASRRGVSREdierevsILRQVLHPNIITLHDVF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  144 QDDRYLYMVMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDN-MLLDKS---GHLKLADFG 218
Cdd:cd14105    78 ENKTDVVLILELVAGGELFDFLAEKEsLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENiMLLDKNvpiPRIKLIDFG 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887698  219 TCMKMnkEGMVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKI 290
Cdd:cd14105   158 LAHKI--EDGNEFKNIFGTPEFVAPEIVNYEP----LGLEADMWSIGVITYILLSGASPFLGDTKQETLANI 223
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
76-222 4.48e-20

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: 91.75  E-value: 4.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLlskfEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd14016     2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKI----EKKDSKHPQLEYEAKVYKLLQGGPGIPRLYWFGQEGDYNVMVMDL 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  156 MpGGDLVNLMSNYDvpekwaRFYTAEVVL--------ALDAIHSMGFIHRDVKPDNMLL---DKSGHLKLADFGTCMK 222
Cdd:cd14016    78 L-GPSLEDLFNKCG------RKFSLKTVLmladqmisRLEYLHSKGYIHRDIKPENFLMglgKNSNKVYLIDFGLAKK 148
HR1_ROCK2 cd11638
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated ...
488-554 5.34e-20

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated coiled-coil containing protein kinase 2; ROCK2 is a serine/threonine protein kinase and was the first identified target of activated RhoA. It plays a role in stress fiber and focal adhesion formation, and 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. ROCK2 contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a Rho-binding HR1 domain and a pleckstrin homology (PH) domain. ROCK2 is auto-inhibited by HR1 and PH domains interacting with the catalytic domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212028 [Multi-domain]  Cd Length: 67  Bit Score: 84.98  E-value: 5.34e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  488 KMLLQHRINEYQRKAEQENEKRRNVENEVSTLKDQLEDLKKVSQNSQLANEKLSQLQKQLEEANDLL 554
Cdd:cd11638     1 KALLQHKNTEYQRKAEHEADRKRNLENEVNSLKDQLEDLKKKNQNSQISNEKNIQLQRQLDEANALL 67
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
82-272 6.26e-20

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: 91.01  E-value: 6.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFemikrSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMKELKRF-----DEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNYDVPEKWA-RFYTA-EVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLK---LADFGTCMKMNKEGMVRCD---- 232
Cdd:cd14065    76 EELLKSMDEQLPWSqRVSLAkDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRnavVADFGLAREMPDEKTKKPDrkkr 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 167887698  233 -TAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEML 272
Cdd:cd14065   156 lTVVGSPYWMAPEMLRGE----SYDEKVDVFSFGIVLCEII 192
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
81-337 7.41e-20

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: 90.96  E-value: 7.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   81 VIGRGAFGEV--------QLVRHKSTRKVYAMKLLSKFEMIKrsdsafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMV 152
Cdd:cd06631     8 VLGKGAYGTVycgltstgQLIAVKQVELDTSDKEKAEKEYEK------LQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGtCMK--------M 223
Cdd:cd06631    82 MEFVPGGSIASILARFGAlEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFG-CAKrlcinlssG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  224 NKEGMVRcdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTP----------FYadslVGTYSKIMNh 293
Cdd:cd06631   161 SQSQLLK--SMRGTPYWMAPEVINETG----HGRKSDIWSIGCTVFEMATGKPPwadmnpmaaiFA----IGSGRKPVP- 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 167887698  294 knslTFPDdnDISKEAKNLICAFLT-DREVRLgrnGVEEIKRHLF 337
Cdd:cd06631   230 ----RLPD--KFSPEARDFVHACLTrDQDERP---SAEQLLKHPF 265
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
74-380 8.13e-20

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: 91.63  E-value: 8.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVV-KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRsDSAFFWEErdimafANSPWVVQLFYAF----QDDRY 148
Cdd:cd14170     1 DDYKVTsQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARR-EVELHWRA------SQCPHIVRIVDVYenlyAGRKC 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 LYMVMEYMPGGDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDK---SGHLKLADFGTCMK 222
Cdd:cd14170    74 LLIVMECLDGGELFSRIQDRGdqaFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAKE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  223 MNKEGMVRcdTAVGTPDYISPEVLksqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLV----GTYSKIMNHKNSLT 298
Cdd:cd14170   154 TTSHNSLT--TPCYTPYYVAPEVL----GPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLaispGMKTRIRMGQYEFP 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  299 FPDDNDISKEAKNLICAFLTDREVRlgRNGVEEikrhlfFKNDQWAWETLRdtvAPVVPDLSSDIDTSNfDDLEEDKGEE 378
Cdd:cd14170   228 NPEWSEVSEEVKMLIRNLLKTEPTQ--RMTITE------FMNHPWIMQSTK---VPQTPLHTSRVLKED-KERWEDVKEE 295

                  ..
gi 167887698  379 ET 380
Cdd:cd14170   296 MT 297
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
103-282 1.20e-19

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 93.93  E-value: 1.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  103 AMKLLSKFEMIK-RSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL-----VNLMSNYDVPEKWAR 176
Cdd:PTZ00267   93 KEKVVAKFVMLNdERQAAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLnkqikQRLKEHLPFQEYEVG 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  177 FYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEgmVRCDTA---VGTPDYISPEVLKSQggdg 253
Cdd:PTZ00267  173 LLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDS--VSLDVAssfCGTPYYLAPELWERK---- 246
                         170       180
                  ....*....|....*....|....*....
gi 167887698  254 YYGRECDWWSVGVFLYEMLVGDTPFYADS 282
Cdd:PTZ00267  247 RYSKKADMWSLGVILYELLTLHRPFKGPS 275
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
518-1090 1.29e-19

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 95.39  E-value: 1.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  518 TLKDQLEDLKKVSQNSQL--ANEKLSQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSISQLESLNRELQERnrilens 595
Cdd:COG1196   217 ELKEELKELEAELLLLKLreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE------- 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  596 ksqtdkdYYQLQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVEGERKEAQDMLNHSEKEKNNLEIDLNy 675
Cdd:COG1196   290 -------EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA- 361
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  676 KLKSLQQRLEQEVNEHKVTKARLTDKHQSIEEAKSVAmcemEKKLKEEREAREKAENRVVQIEKQCSMLDVDLKQSQQKL 755
Cdd:COG1196   362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL----AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  756 EHLTGNKERMEDEVKNLTLQLEQESNKRLLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLEFELA--QLTKQYR 833
Cdd:COG1196   438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEgvKAALLLA 517
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  834 GNEGQMRELQDQLEAEQYFSTLYKTQVKELKEEIEEKNRENLKK-IQELQNEKETLAT--QLDLAETKAESEQLARGLLE 910
Cdd:COG1196   518 GLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAaIEYLKAAKAGRATflPLDKIRARAALAAALARGAI 597
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  911 EQYFELTQESKKAASRNRQEITDKDHTVSRLEEANSMLTKDIEILRRENEELTEKMKKAEEEYKLEKEEEISNLKAAFEK 990
Cdd:COG1196   598 GAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEA 677
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  991 NINTERTLKTQAVNKLAEIMNRKDFKIDRKKANTQDLRKKEKENRKLQLE--LNQEREKFNQMVVKHQKELNDMQAQLVE 1068
Cdd:COG1196   678 EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEeqLEAEREELLEELLEEEELLEEEALEELP 757
                         570       580
                  ....*....|....*....|..
gi 167887698 1069 ECAHRNELQMQLASKESDIEQL 1090
Cdd:COG1196   758 EPPDLEELERELERLEREIEAL 779
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
76-318 1.76e-19

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: 90.09  E-value: 1.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMiKRSDSAFfwEERDIM-AFANSPWVVQL----FYAFQDDRYLY 150
Cdd:cd13985     2 YQVTKQLGEGGFSYVYLAHDVNTGRRYALKRMYFNDE-EQLRVAI--KEIEIMkRLCGHPNIVQYydsaILSSEGRKEVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGgDLVNLMSN-----YDVPEKWARFYtaEVVLALDAIHSMG--FIHRDVKPDNMLLDKSGHLKLADFGTCMKM 223
Cdd:cd13985    79 LLMEYCPG-SLVDILEKsppspLSEEEVLRIFY--QICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGSATTE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  224 NKEGMVRCDTAV--------GTPDYISPEVLKSQGGDgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVgtysKIMNHKN 295
Cdd:cd13985   156 HYPLERAEEVNIieeeiqknTTPMYRAPEMIDLYSKK-PIGEKADIWALGCLLYKLCFFKLPFDESSKL----AIVAGKY 230
                         250       260
                  ....*....|....*....|...
gi 167887698  296 SLtfPDDNDISKEAKNLICAFLT 318
Cdd:cd13985   231 SI--PEQPRYSPELHDLIRHMLT 251
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
76-317 2.05e-19

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: 89.53  E-value: 2.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQ-DDRYLYMVME 154
Cdd:cd14164     2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDFVQKFLPRELSILRRVNHPNIVQMFECIEvANGRLYIVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSG-HLKLADFGTCMKMNKEGMVRcDT 233
Cdd:cd14164    82 AAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVEDYPELS-TT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  234 AVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYaDSLVGtysKIMNHKNSLTFPDDNDISKEAKNLI 313
Cdd:cd14164   161 FCGSRAYTPPEVIL---GTPYDPKKYDVWSLGVVLYVMVTGTMPFD-ETNVR---RLRLQQRGVLYPSGVALEEPCRALI 233

                  ....
gi 167887698  314 CAFL 317
Cdd:cd14164   234 RTLL 237
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
426-1097 2.06e-19

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 95.12  E-value: 2.06e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   426 ESLQKTIYKLE-EQLHNEM----QLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKEKMLLQHRINEYQR 500
Cdd:TIGR02168  223 RELELALLVLRlEELREELeelqEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   501 KAEQENEKRRNVENEVSTLKDQLEDLKkvsQNSQLANEKLSQLQKQLEEANdllrtesdtavrlrkshtemsksiSQLES 580
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEELE---SKLDELAEELAELEEKLEELK------------------------EELES 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   581 LNRELQERNRILENSKSQTDkdyyQLQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVEGERKEAQDMLN 660
Cdd:TIGR02168  356 LEAELEELEAELEELESRLE----ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   661 HSEKEKNNLEID-LNYKLKSLQQRLEQEVNEHKVTKARLTDKHQSI-----EEAKSVAMCEMEKKLKEEREAREKAENRV 734
Cdd:TIGR02168  432 EAELKELQAELEeLEEELEELQEELERLEEALEELREELEEAEQALdaaerELAQLQARLDSLERLQENLEGFSEGVKAL 511
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   735 VQIEKQCSMLDVDLKQS-------QQKLEHLTGnkERMED-EVKNLTLQ------LEQESNKRL--LLQNELKTQAFEAD 798
Cdd:TIGR02168  512 LKNQSGLSGILGVLSELisvdegyEAAIEAALG--GRLQAvVVENLNAAkkaiafLKQNELGRVtfLPLDSIKGTEIQGN 589
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   799 NLKGLEKQ------MKQEINTLLEAKRLLEFELAQLTKQYRGNEGQmrELQDQLEAEQYFSTLYKTQVKELKEEIEEKNR 872
Cdd:TIGR02168  590 DREILKNIegflgvAKDLVKFDPKLRKALSYLLGGVLVVDDLDNAL--ELAKKLRPGYRIVTLDGDLVRPGGVITGGSAK 667
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   873 ENLkKIQELQNEKETLATQLDLAETKAESEQLARGLLEEQYFELTQESKKAASR---NRQEITDKDHTVSRLEEANSMLT 949
Cdd:TIGR02168  668 TNS-SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEleeLSRQISALRKDLARLEAEVEQLE 746
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   950 KDIEILRRENEELTEKMKKAEEEYKLEKEE-------------EISNLKAAFEKNI------NTERTLKTQAVNKLAEIM 1010
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEElaeaeaeieeleaQIEQLKEELKALRealdelRAELTLLNEEAANLRERL 826
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  1011 NRKDFKIDRKKANTQDLRKKEKENRKLQLELNQEREKFNQMVVKHQKELNDMQAQLVEECAHRNELQMQLASKESDIEQL 1090
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906

                   ....*..
gi 167887698  1091 RAKLLDL 1097
Cdd:TIGR02168  907 ESKRSEL 913
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
74-278 2.40e-19

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: 89.94  E-value: 2.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLS---KFEMIKRSDSaffweERDIMAFANSPWVVQLFYAFQDDRYLY 150
Cdd:cd06619     1 QDIQYQEILGHGNGGTVYKAYHLLTRRILAVKVIPldiTVELQKQIMS-----ELEILYKCDSPYIIGFYGAFFVENRIS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGGDLVNLMSnydVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEgmvR 230
Cdd:cd06619    76 ICTEFMDGGSLDVYRK---IPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNS---I 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 167887698  231 CDTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd06619   150 AKTYVGTNAYMAPERISGE----QYGIHSDVWSLGISFMELALGRFPY 193
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
74-274 3.15e-19

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: 89.74  E-value: 3.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFE---MIKRSdsAFfweeRDIMAFAN--SPWVVQLFYAFQDDRY 148
Cdd:cd07847     1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIKKFVESEddpVIKKI--AL----REIRMLKQlkHPNLVNLIEVFRRKRK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 LYMVMEYMPGGDLVNLMSN-YDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEG 227
Cdd:cd07847    75 LHLVFEYCDHTVLNELEKNpRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPG 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 167887698  228 MVRCDTaVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVG 274
Cdd:cd07847   155 DDYTDY-VATRWYRAPELLV---GDTQYGPPVDVWAIGCVFAELLTG 197
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
76-282 3.48e-19

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. 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 CDKL5 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: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 89.67  E-value: 3.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPwVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd07848     3 FEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQEN-IVELKEAFRRRGKLYLVFEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGG--DLVNLMSNYDVPEKwARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDT 233
Cdd:cd07848    82 VEKNmlELLEEMPNGVPPEK-VRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSNANYTE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 167887698  234 AVGTPDYISPEVLKSqggdGYYGRECDWWSVGVFLYEMLVGDTPFYADS 282
Cdd:cd07848   161 YVATRWYRSPELLLG----APYGKAVDMWSVGCILGELSDGQPLFPGES 205
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
82-278 3.70e-19

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: 89.43  E-value: 3.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLlSKFEMIKRSDSAFFWE-ERDIMAFANSPWVVQL------FYAFQDDRYLYMVME 154
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGEYVAIKK-CRQELSPSDKNRERWClEVQIMKKLNHPNVVSArdvppeLEKLSPNDLPLLAME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDL---VNLMSNY-DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH---LKLADFGTCMKMNKEG 227
Cdd:cd13989    80 YCSGGDLrkvLNQPENCcGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGrviYKLIDLGYAKELDQGS 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 167887698  228 MvrCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd13989   160 L--CTSFVGTLQYLAPELFESKK----YTCTVDYWSFGTLAFECITGYRPF 204
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
80-317 4.81e-19

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: 88.84  E-value: 4.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 159
Cdd:cd14197    15 RELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAQANPWVINLHEVYETASEMILVLEYAAGG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DLVN-LMSNYD--VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKS---GHLKLADFGTCMKMNKEGMVRcdT 233
Cdd:cd14197    95 EIFNqCVADREeaFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGLSRILKNSEELR--E 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  234 AVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLI 313
Cdd:cd14197   173 IMGTPEYVAPEILSYEP----ISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEEEFEHLSESAIDFI 248

                  ....
gi 167887698  314 CAFL 317
Cdd:cd14197   249 KTLL 252
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
412-1097 7.16e-19

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 93.20  E-value: 7.16e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   412 NDNRTSSNADKSLQESLQKTIYKLEEQLHNEMQLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKEKMLL 491
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   492 QHRINEYQRKAEQENEKRRNVENEVSTLKDQLEDLKK----VSQNSQLANEKLSQLQKQLEEANDLL--RTESDTAVRLR 565
Cdd:TIGR02168  350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaqLELQIASLNNEIERLEARLERLEDRRerLQQEIEELLKK 429
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   566 KSHTEMSKSISQLESLNRE---LQERNRILENSKSQTDKDYYQLQAILEAERRDRGHDS---EMIGDLQARITSLQEEVK 639
Cdd:TIGR02168  430 LEEAELKELQAELEELEEEleeLQEELERLEEALEELREELEEAEQALDAAERELAQLQarlDSLERLQENLEGFSEGVK 509
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   640 HLKHNLEKVEGERKEAQDMLNHSEKEKNNLEIDlnyklksLQQRLEQEVNEhKVTKARLTDKHQSIEEAKSVAMCEM--- 716
Cdd:TIGR02168  510 ALLKNQSGLSGILGVLSELISVDEGYEAAIEAA-------LGGRLQAVVVE-NLNAAKKAIAFLKQNELGRVTFLPLdsi 581
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   717 -EKKLKEEREAREKAENRVVQIEKQCSMLDVDLK----------------QSQQKLEHLTGNKERM---EDEVKN----L 772
Cdd:TIGR02168  582 kGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvddlDNALELAKKLRPGYRIvtlDGDLVRpggvI 661
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   773 TLQLEQESNKRLLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMRELQDQLEAEQyf 852
Cdd:TIGR02168  662 TGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE-- 739
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   853 stlyktqvkELKEEIEEKNRENLKKIQELQNEKETLATQLD-----LAETKAESEQLARGLleEQYFELTQESKKAASRN 927
Cdd:TIGR02168  740 ---------AEVEQLEERIAQLSKELTELEAEIEELEERLEeaeeeLAEAEAEIEELEAQI--EQLKEELKALREALDEL 808
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   928 RQEITDKDHTVSRLEEANSMLTKDIEILRRENEELTEKmKKAEEEYKLEKEEEISNLKAAFEKnINTERTLKTQAVNKLA 1007
Cdd:TIGR02168  809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ-IEELSEDIESLAAEIEELEELIEE-LESELEALLNERASLE 886
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  1008 EIMNRKDfkiDRKKANTQDLRKKEKENRKLQLELNQEREKFNQMVVKHQK---ELNDMQAQLVEEcaHRNELQMQLA--- 1081
Cdd:TIGR02168  887 EALALLR---SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGlevRIDNLQERLSEE--YSLTLEEAEAlen 961
                          730
                   ....*....|....*.
gi 167887698  1082 SKESDIEQLRAKLLDL 1097
Cdd:TIGR02168  962 KIEDDEEEARRRLKRL 977
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
76-313 7.29e-19

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: 89.66  E-value: 7.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSK-FEMI---KRSdsaffWEERDIMAFANSPWVVQLFYAFQDDRYL-- 149
Cdd:cd07851    17 YQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRpFQSAihaKRT-----YRELRLLKHMKHENVIGLLDVFTPASSLed 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 ----YMVMEYMpGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNK 225
Cdd:cd07851    92 fqdvYLVTHLM-GADLNNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHTDD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  226 EgMVrcdTAVGTPDYISPEVLKSQggdGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSltfPDDNDI 305
Cdd:cd07851   171 E-MT---GYVATRWYRAPEIMLNW---MHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNLVGT---PDEELL 240
                         250
                  ....*....|..
gi 167887698  306 ----SKEAKNLI 313
Cdd:cd07851   241 kkisSESARNYI 252
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
73-272 1.13e-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: 88.01  E-value: 1.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   73 AEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLskfeMIKRSDSAFFWEERDIMAFA--NSPWVVQLFYAF------- 143
Cdd:cd14048     5 LTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRI----RLPNNELAREKVLREVRALAklDHPGIVRYFNAWlerppeg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  144 ----QDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYT----AEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLA 215
Cdd:cd14048    81 wqekMDEVYLYIQMQLCRKENLKDWMNRRCTMESRELFVClnifKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVG 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  216 DFGTCMKMNK---EGMVRCDTA--------VGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEML 272
Cdd:cd14048   161 DFGLVTAMDQgepEQTVLTPMPayakhtgqVGTRLYMSPEQIHGNQ----YSEKVDIFALGLILFELI 224
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
76-318 1.97e-18

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: 87.35  E-value: 1.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllsKFEMIKRSDSAFFWEERDIMAFANSPWVV-----QLFYAFQDDRYLY 150
Cdd:cd13986     2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALK---KILCHSKEDVKEAMREIENYRLFNHPNILrlldsQIVKEAGGKKEVY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGGDLVNLMSNYDV-----PEKWARFYTAEVVLALDAIHSM---GFIHRDVKPDNMLLDKSGHLKLADFGTC-- 220
Cdd:cd13986    79 LLLPYYKRGSLQDEIERRLVkgtffPEDRILHIFLGICRGLKAMHEPelvPYAHRDIKPGNVLLSEDDEPILMDLGSMnp 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  221 ----MKMNKEGMVRCDTAV--GTPDYISPEVLKSQGGDGYYGReCDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHK 294
Cdd:cd13986   159 arieIEGRREALALQDWAAehCTMPYRAPELFDVKSHCTIDEK-TDIWSLGCTLYALMYGESPFERIFQKGDSLALAVLS 237
                         250       260
                  ....*....|....*....|....
gi 167887698  295 NSLTFPDDNDISKEAKNLICAFLT 318
Cdd:cd13986   238 GNYSFPDNSRYSEELHQLVKSMLV 261
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
73-272 2.56e-18

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: 87.81  E-value: 2.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   73 AEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSK-FEMI---KRSdsaffWEERDIMAFANSPWVVQLFYAFQ---- 144
Cdd:cd07855     4 GDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNaFDVVttaKRT-----LRELKILRHFKHDNIIAIRDILRpkvp 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  145 --DDRYLYMVMEYMPGgDLVNLM-SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGT-- 219
Cdd:cd07855    79 yaDFKDVYVVLDLMES-DLHHIIhSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMar 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 167887698  220 CMKMNKEGMVRCDTA-VGTPDYISPEVLKSQGGdgyYGRECDWWSVGVFLYEML 272
Cdd:cd07855   158 GLCTSPEEHKYFMTEyVATRWYRAPELMLSLPE---YTQAIDMWSVGCIFAEML 208
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
76-282 3.81e-18

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: 86.40  E-value: 3.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllsKFEMIKRSDSAFFWEERDIMAFA--NSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd07860     2 FQKVEKIGEGTYGVVYKARNKLTGEVVALK---KIRLDTETEGVPSTAIREISLLKelNHPNIVKLLDVIHTENKLYLVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMpGGDLVNLM---SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEgmVR 230
Cdd:cd07860    79 EFL-HQDLKKFMdasALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVP--VR 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 167887698  231 CDT-AVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADS 282
Cdd:cd07860   156 TYThEVVTLWYRAPEILL---GCKYYSTAVDIWSLGCIFAEMVTRRALFPGDS 205
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
74-284 3.84e-18

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: 85.74  E-value: 3.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllSKFEMIKR-----SDSAFFWEERDIMAFANSPWVVQLFYAFQDDRY 148
Cdd:cd14019     1 NKYRIIEKIGEGTFSSVYKAEDKLHDLYDRNK--GRLVALKHiyptsSPSRILNELECLERLGGSNNVSGLITAFRNEDQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 LYMVMEYMPGG---DLVNLMSNYDVpekwaRFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD-KSGHLKLADFG----TC 220
Cdd:cd14019    79 VVAVLPYIEHDdfrDFYRKMSLTDI-----RIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNrETGKGVLVDFGlaqrEE 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  221 MKMNKEGmvrcdTAVGTPDYISPEVL-KSQggdgYYGRECDWWSVGVFLYEMLVGDTPFY-----ADSLV 284
Cdd:cd14019   154 DRPEQRA-----PRAGTRGFRAPEVLfKCP----HQTTAIDIWSAGVILLSILSGRFPFFfssddIDALA 214
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
82-272 4.11e-18

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: 85.78  E-value: 4.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKF-EMIKRSdsafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGD 160
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGEVMVMKELIRFdEETQRT----FLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  161 LVNLMSNYDVPEKWAR--FYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKE--------GMVR 230
Cdd:cd14221    77 LRGIIKSMDSHYPWSQrvSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDEktqpeglrSLKK 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 167887698  231 CD-----TAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEML 272
Cdd:cd14221   157 PDrkkryTVVGNPYWMAPEMINGRS----YDEKVDVFSFGIVLCEII 199
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
76-290 4.52e-18

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: 85.83  E-value: 4.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWE---ERDIMAFANSPWVVQLFYAFQDDRYLYMV 152
Cdd:cd14195     7 YEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRRGVSREEierEVNILREIQHPNIITLHDIFENKTDVVLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDN-MLLDKSG---HLKLADFGTCMKMNKEG 227
Cdd:cd14195    87 LELVSGGELFDFLAEKEsLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENiMLLDKNVpnpRIKLIDFGIAHKIEAGN 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167887698  228 MVRcdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKI 290
Cdd:cd14195   167 EFK--NIFGTPEFVAPEIVNYEP----LGLEADMWSIGVITYILLSGASPFLGETKQETLTNI 223
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
76-324 5.65e-18

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-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 uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized 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: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 85.46  E-value: 5.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAffWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd14088     3 YDLGQVIKTEEFCEIFRAKDKTTGKLYTCKKFLKRDGRKVRKAA--KNEINILKMVKHPNILQLVDVFETRKEYFIFLEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD---KSGHLKLADFGTCMKMNkeGMVRc 231
Cdd:cd14088    81 ATGREVFDwILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYnrlKNSKIVISDFHLAKLEN--GLIK- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  232 dTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYS--------KIMNHKNSLTFPDDN 303
Cdd:cd14088   158 -EPCGTPEYLAPEVVGRQ----RYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDDYEnhdknlfrKILAGDYEFDSPYWD 232
                         250       260
                  ....*....|....*....|..
gi 167887698  304 DISKEAKNLICAFL-TDREVRL 324
Cdd:cd14088   233 DISQAAKDLVTRLMeVEQDQRI 254
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
82-292 9.15e-18

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: 84.87  E-value: 9.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKllsKFEMikrsdSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd13991    14 IGRGSFGEVHRMEDKQTGFQCAVK---KVRL-----EVFRAEELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGGSL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSG-HLKLADFGTCMKMNKEGMVRC----DTAV 235
Cdd:cd13991    86 GQLIKEQGcLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGsDAFLCDFGHAECLDPDGLGKSlftgDYIP 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167887698  236 GTPDYISPEVLKsqggdgyyGREC----DWWSVGVFLYEMLVGDTP---FYADSLvgtYSKIMN 292
Cdd:cd13991   166 GTETHMAPEVVL--------GKPCdakvDVWSSCCMMLHMLNGCHPwtqYYSGPL---CLKIAN 218
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
76-282 1.04e-17

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: 85.03  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLsKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd07835     1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKI-RLETEDEGVPSTAIREISLLKELNHPNIVRLLDVVHSENKLYLVFEF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MpGGDLVNLM---SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFgtcmkmnkeGMVRcd 232
Cdd:cd07835    80 L-DLDLKKYMdssPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADF---------GLAR-- 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167887698  233 tAVGTPD-----------YISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADS 282
Cdd:cd07835   148 -AFGVPVrtythevvtlwYRAPEILL---GSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDS 204
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
76-271 1.09e-17

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: 84.42  E-value: 1.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfeMIKRSDSAffWEerDIM---AFANS---PWVVQLFYAFQDDRYL 149
Cdd:cd06607     3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSY--SGKQSTEK--WQ--DIIkevKFLRQlrhPNTIEYKGCYLREHTA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 YMVMEYMPG--GDLVnlmsnyDVPEKWAR-----FYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMK 222
Cdd:cd06607    77 WLVMEYCLGsaSDIV------EVHKKPLQeveiaAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASL 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 167887698  223 MNKegmvrCDTAVGTPDYISPEVLKSQgGDGYYGRECDWWSVGVFLYEM 271
Cdd:cd06607   151 VCP-----ANSFVGTPYWMAPEVILAM-DEGQYDGKVDVWSLGITCIEL 193
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
64-279 1.56e-17

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 88.64  E-value: 1.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   64 NKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSkFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAF 143
Cdd:PTZ00266    3 GKYDDGESRLNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAIS-YRGLKEREKSQLVIEVNVMRELKHKNIVRYIDRF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  144 --QDDRYLYMVMEYMPGGDLV-NLMSNY----DVPEKWARFYTAEVVLALDAIHSMG-------FIHRDVKPDNMLLD-- 207
Cdd:PTZ00266   82 lnKANQKLYILMEFCDAGDLSrNIQKCYkmfgKIEEHAIVDITRQLLHALAYCHNLKdgpngerVLHRDLKPQNIFLStg 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  208 ---------KSGHL------KLADFGTCMKMNKEGMVRcdTAVGTPDYISPEVLKSQGGDgyYGRECDWWSVGVFLYEML 272
Cdd:PTZ00266  162 irhigkitaQANNLngrpiaKIGDFGLSKNIGIESMAH--SCVGTPYYWSPELLLHETKS--YDDKSDMWALGCIIYELC 237

                  ....*..
gi 167887698  273 VGDTPFY 279
Cdd:PTZ00266  238 SGKTPFH 244
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
493-1100 1.69e-17

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 88.64  E-value: 1.69e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   493 HRINEYQRKAEQENEKRrnvENEVSTLKDQLEDLKKVSQNSQLANEKLSQLQKQLEEANDLLRTESDTAVR--------- 563
Cdd:pfam15921   85 HQVKDLQRRLNESNELH---EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHeleaakclk 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   564 ---LRKSHTEMSKSISQLESLNRELQERNRILENSKSQTDKDYYQLQAILEAERRDRGHD-SEMIGDLQARITSLQEEVK 639
Cdd:pfam15921  162 edmLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAiSKILRELDTEISYLKGRIF 241
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   640 HLKHNLEKVEGERKEAQDMLnhsekeknnleidlnykLKSLQQRLEQEVNEHKVTKARLTDKHQSI-------------- 705
Cdd:pfam15921  242 PVEDQLEALKSESQNKIELL-----------------LQQHQDRIEQLISEHEVEITGLTEKASSArsqansiqsqleii 304
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   706 -EEAK---SVAMC---EMEKKLKEEREA----REKAENRVVQIEKQCSMLDVDLKQSQQKLEHLTGNKERMEDEVKNL-- 772
Cdd:pfam15921  305 qEQARnqnSMYMRqlsDLESTVSQLRSElreaKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLla 384
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   773 -------TLQLEQESNKRLL------------LQNELKTQAFEADNLKGLEKQMKQEINTLLEAK--------RLLEfEL 825
Cdd:pfam15921  385 dlhkrekELSLEKEQNKRLWdrdtgnsitidhLRRELDDRNMEVQRLEALLKAMKSECQGQMERQmaaiqgknESLE-KV 463
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   826 AQLTKQYRGNEGQMRELQDQLEAEQYfsTLYKTQVKELKEEIEEKNREnlKKIQELQNEKETLATQLDLaetkaESEQLA 905
Cdd:pfam15921  464 SSLTAQLESTKEMLRKVVEELTAKKM--TLESSERTVSDLTASLQEKE--RAIEATNAEITKLRSRVDL-----KLQELQ 534
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   906 RGLLEEQYFELTQESKKAAsrnRQEITDKDhtvsrleeansmltKDIEILRRENEELTEKMKKAEEEYKLEKEEeisnlK 985
Cdd:pfam15921  535 HLKNEGDHLRNVQTECEAL---KLQMAEKD--------------KVIEILRQQIENMTQLVGQHGRTAGAMQVE-----K 592
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   986 AAFEKNINtERTLKTQAVNKLAEimnRKDFKIDRKKANTQDLRKKE-------KENRKLQLELNQEREKFNQMVVKHQKE 1058
Cdd:pfam15921  593 AQLEKEIN-DRRLELQEFKILKD---KKDAKIRELEARVSDLELEKvklvnagSERLRAVKDIKQERDQLLNEVKTSRNE 668
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  1059 LNDMQAQLveECAHR-------------NELQMQLASKESDIEQLRAKLLDLSDS 1100
Cdd:pfam15921  669 LNSLSEDY--EVLKRnfrnkseemetttNKLKMQLKSAQSELEQTRNTLKSMEGS 721
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
82-278 2.47e-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: 84.47  E-value: 2.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFfwEERDIMAFANSPWVVQLFyAFQDD---RYLYMVMEYMPG 158
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMRPLDVQM--REFEVLKKLNHKNIVKLF-AIEEElttRHKVLVMELCPC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  159 GDLVNLM---SN-YDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL----DKSGHLKLADFGTCMK-MNKEGMV 229
Cdd:cd13988    78 GSLYTVLeepSNaYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRvigeDGQSVYKLTDFGAARElEDDEQFV 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 167887698  230 rcdTAVGTPDYISPE-----VLKSQGGDGyYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd13988   158 ---SLYGTEEYLHPDmyeraVLRKDHQKK-YGATVDLWSIGVTFYHAATGSLPF 207
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
82-278 2.49e-17

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: 83.26  E-value: 2.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKllSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd05041     3 IGRGNFGDVYRGVLKPDNTEVAVK--TCRETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNydvpeKWARFYTAEVV-LALDAIHSMGF------IHRDVKPDNMLLDKSGHLKLADFGtcMKMNKEGMVR--CD 232
Cdd:cd05041    81 LTFLRK-----KGARLTVKQLLqMCLDAAAGMEYleskncIHRDLAARNCLVGENNVLKISDFG--MSREEEDGEYtvSD 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 167887698  233 TAVGTP-DYISPEVLKSqggdGYYGRECDWWSVGVFLYEML-VGDTPF 278
Cdd:cd05041   154 GLKQIPiKWTAPEALNY----GRYTSESDVWSFGILLWEIFsLGATPY 197
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
82-278 3.00e-17

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-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: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 83.31  E-value: 3.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLlSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDryLYMVMEYMPGGDL 161
Cdd:cd14025     4 VGSGGFGQVYKVRHKHWKTWLAIKC-PPSLHVDDSERMELLEEAKKMEMAKFRHILPVYGICSEP--VGLVMEYMETGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNYDVPekWA-RFYTA-EVVLALDAIHSMG--FIHRDVKPDNMLLDKSGHLKLADFG--TCMKMNKEGMVRCDTAV 235
Cdd:cd14025    81 EKLLASEPLP--WElRFRIIhETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGlaKWNGLSHSHDLSRDGLR 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 167887698  236 GTPDYISPEVLKSQggDGYYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd14025   159 GTIAYLPPERFKEK--NRCPDTKHDVYSFAIVIWGILTQKKPF 199
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
81-281 4.43e-17

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: 82.82  E-value: 4.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   81 VIGRGAFGEVQLVRHKStRKVyAMKLLSKfEMIKRSDSAFFWEERDImAFANSPWVVQLFYAFQ---DDRYLYMVMEYMP 157
Cdd:cd13979    10 PLGSGGFGSVYKATYKG-ETV-AVKIVRR-RRKNRASRQSFWAELNA-ARLRHENIVRVLAAETgtdFASLGLIIMEYCG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  158 GGDLVNLMSNYDVP---EKWARfYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNK--EGMVRCD 232
Cdd:cd13979    86 NGTLQQLIYEGSEPlplAHRIL-ISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLGEgnEVGTPRS 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 167887698  233 TAVGTPDYISPEVLKSQGGdgyyGRECDWWSVGVFLYEMLVGDTPFYAD 281
Cdd:cd13979   165 HIGGTYTYRAPELLKGERV----TPKADIYSFGITLWQMLTRELPYAGL 209
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
82-272 5.05e-17

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: 82.94  E-value: 5.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKF-EMIKRSdsafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGD 160
Cdd:cd14154     1 LGKGFFGQAIKVTHRETGEVMVMKELIRFdEEAQRN----FLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  161 LVNLMSNYDVPEKWAR--FYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKE----GMVRCD-- 232
Cdd:cd14154    77 LKDVLKDMARPLPWAQrvRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLIVEErlpsGNMSPSet 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 167887698  233 -------------TAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEML 272
Cdd:cd14154   157 lrhlkspdrkkryTVVGNPYWMAPEMLNGRS----YDEKVDIFSFGIVLCEII 205
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
82-281 5.97e-17

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: 82.27  E-value: 5.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSkfemIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd14110    11 INRGRFSVVRQCEEKRSGQMLAAKIIP----YKPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPEL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 V-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDY 240
Cdd:cd14110    87 LyNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQGKVLMTDKKGDYVET 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 167887698  241 ISPEVLKSQGGdgyyGRECDWWSVGVFLYEMLVGDTPFYAD 281
Cdd:cd14110   167 MAPELLEGQGA----GPQTDIWAIGVTAFIMLSADYPVSSD 203
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
136-281 6.58e-17

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; 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 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 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: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 81.94  E-value: 6.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  136 VVQLFYAFQDDRYLYMVMEY-MPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD-KSGHL 212
Cdd:cd14100    67 VIRLLDWFERPDSFVLVLERpEPVQDLFDFITERGaLPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGEL 146
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167887698  213 KLADFGTcmkmnkeGMVRCDTAV----GTPDYISPEVLKSQGgdgYYGRECDWWSVGVFLYEMLVGDTPFYAD 281
Cdd:cd14100   147 KLIDFGS-------GALLKDTVYtdfdGTRVYSPPEWIRFHR---YHGRSAAVWSLGILLYDMVCGDIPFEHD 209
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
76-318 9.13e-17

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; 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 three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 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: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 81.82  E-value: 9.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSK---FEMIKRSDS-------AFFWEerdIMAFANSPWVVQLFYAFQD 145
Cdd:cd14101     2 YTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISRnrvQQWSKLPGVnpvpnevALLQS---VGGGPGHRGVIRLLDWFEI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  146 DRYLYMVMEY-MPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD-KSGHLKLADFGTCMK 222
Cdd:cd14101    79 PEGFLLVLERpQHCQDLFDYITERGaLDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDlRTGDIKLIDFGSGAT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  223 MNKEGMVRCDtavGTPDYISPEVLKSQggdGYYGRECDWWSVGVFLYEMLVGDTPFYADslvgtySKIMnhKNSLTFPdd 302
Cdd:cd14101   159 LKDSMYTDFD---GTRVYSPPEWILYH---QYHALPATVWSLGILLYDMVCGDIPFERD------TDIL--KAKPSFN-- 222
                         250
                  ....*....|....*.
gi 167887698  303 NDISKEAKNLICAFLT 318
Cdd:cd14101   223 KRVSNDCRSLIRSCLA 238
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
74-292 1.02e-16

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: 82.27  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLsKFEmikRSDSAF---FWEERDIMAFANSPWVVQL----FYAFQDD 146
Cdd:cd07843     5 DEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKL-KME---KEKEGFpitSLREINILLKLQHPNIVTVkevvVGSNLDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  147 ryLYMVMEYMPGgDLVNLMSNYDVPekwarFYTAEV-------VLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGT 219
Cdd:cd07843    81 --IYMVMEYVEH-DLKSLMETMKQP-----FLQSEVkclmlqlLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGL 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  220 CMKM--NKEGMVRcdtAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMN 292
Cdd:cd07843   153 AREYgsPLKPYTQ---LVVTLWYRAPELLL---GAKEYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFK 221
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
81-313 1.11e-16

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: 81.29  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   81 VIGRGAFGEVQLVRHK-STRKVYAMKLLSKFEMIKRSDSafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 159
Cdd:cd14061     1 VIGVGGFGKVYRGIWRgEEVAVKAARQDPDEDISVTLEN--VRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DLVNLMSNYDVPEK----WArfytAEVVLALDAIHS---MGFIHRDVKPDNMLLD-KSGH-------LKLADFGTCMKMN 224
Cdd:cd14061    79 ALNRVLAGRKIPPHvlvdWA----IQIARGMNYLHNeapVPIIHRDLKSSNILILeAIENedlenktLKITDFGLAREWH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  225 KegMVRCDTAvGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYA-DSLVGTYSKIMnhkNSLTFPDDN 303
Cdd:cd14061   155 K--TTRMSAA-GTYAWMAPEVIKSS----TFSKASDVWSYGVLLWELLTGEVPYKGiDGLAVAYGVAV---NKLTLPIPS 224
                         250
                  ....*....|
gi 167887698  304 DISKEAKNLI 313
Cdd:cd14061   225 TCPEPFAQLM 234
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
76-277 1.17e-16

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: 81.54  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEmikrSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd14017     2 WKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQ----PKQVLKMEVAVLKKLQGKPHFCRLIGCGRTERYNYIVMTL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MpGGDLVNLMSNYdvPEkwaRFYTAEVVL--------ALDAIHSMGFIHRDVKPDNMLLDKSGH----LKLADFGTCMK- 222
Cdd:cd14017    78 L-GPNLAELRRSQ--PR---GKFSVSTTLrlgiqilkAIEDIHEVGFLHRDVKPSNFAIGRGPSdertVYILDFGLARQy 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  223 MNKEGMV-RCDTAV----GTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTP 277
Cdd:cd14017   152 TNKDGEVeRPPRNAagfrGTVRYASVNAHRNKE----QGRRDDLWSWFYMLIEFVTGQLP 207
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
73-274 1.59e-16

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: 82.74  E-value: 1.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   73 AEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFE-------------MIKRsdsafFWEErDIMAFANspwvVQL 139
Cdd:cd07849     4 GPRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISPFEhqtyclrtlreikILLR-----FKHE-NIIGILD----IQR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  140 FYAFQDDRYLYMVMEYMPGgDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFgt 219
Cdd:cd07849    74 PPTFESFKDVYIVQELMET-DLYKLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDF-- 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167887698  220 cmkmnkeGMVRCDTA-----------VGTPDYISPEVLKSQGGdgyYGRECDWWSVGVFLYEMLVG 274
Cdd:cd07849   151 -------GLARIADPehdhtgflteyVATRWYRAPEIMLNSKG---YTKAIDIWSVGCILAEMLSN 206
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
159-318 2.60e-16

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK 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: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 80.91  E-value: 2.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  159 GDLVNL----MSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH-LKLADFGTCMKMNKEGMVRCDT 233
Cdd:cd13974   114 ADLINLqhyvIREKRLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTRkITITNFCLGKHLVSEDDLLKDQ 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  234 AvGTPDYISPEVLksqGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKImnHKNSLTFPDDNDISKEAKNLI 313
Cdd:cd13974   194 R-GSPAYISPDVL---SGKPYLGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKI--KAAEYTIPEDGRVSENTVCLI 267

                  ....*
gi 167887698  314 CAFLT 318
Cdd:cd13974   268 RKLLV 272
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
74-272 2.64e-16

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: 80.61  E-value: 2.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllsKFEMIKRSdsaffwEERDIMAFAN--SPWVVQLFYAFQDD----- 146
Cdd:cd14047     6 QDFKEIELIGSGGFGQVFKAKHRIDGKTYAIK---RVKLNNEK------AEREVKALAKldHPNIVRYNGCWDGFdydpe 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  147 -----------RYLYMVMEYMPGGDLVNLMS--NYDVPEKWA---RFYtaEVVLALDAIHSMGFIHRDVKPDNMLLDKSG 210
Cdd:cd14047    77 tsssnssrsktKCLFIQMEFCEKGTLESWIEkrNGEKLDKVLaleIFE--QITKGVEYIHSKKLIHRDLKPSNIFLVDTG 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887698  211 HLKLADFGTCMKMNKEGmvRCDTAVGTPDYISPEvlksQGGDGYYGRECDWWSVGVFLYEML 272
Cdd:cd14047   155 KVKIGDFGLVTSLKNDG--KRTKSKGTLSYMSPE----QISSQDYGKEVDIYALGLILFELL 210
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
76-281 2.90e-16

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; 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). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 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: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 80.00  E-value: 2.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSP----WVVQLFYAFQDDRYLYM 151
Cdd:cd14102     2 YQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGTLNGVMVPLEIVLLKKVGsgfrGVIKLLDWYERPDGFLI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  152 VMEY-MPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD-KSGHLKLADFGTcmkmnkeGM 228
Cdd:cd14102    82 VMERpEPVKDLFDFITEKGaLDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlRTGELKLIDFGS-------GA 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  229 VRCDTAV----GTPDYISPEVLKSQGgdgYYGRECDWWSVGVFLYEMLVGDTPFYAD 281
Cdd:cd14102   155 LLKDTVYtdfdGTRVYSPPEWIRYHR---YHGRSATVWSLGVLLYDMVCGDIPFEQD 208
Rho_Binding pfam08912
Rho Binding; Rho Binding Domain is responsible for the recognition and binding of Rho binding ...
949-1014 3.18e-16

Rho Binding; Rho Binding Domain is responsible for the recognition and binding of Rho binding domain-containing proteins (such as ROCK) to Rho, resulting in activation of the GTPase which in turn modulates the phosphorylation of various signalling proteins. This domain is within an amphipathic alpha-helical coiled-coil and interacts with Rho through predominantly hydrophobic interactions.


Pssm-ID: 462630 [Multi-domain]  Cd Length: 68  Bit Score: 74.23  E-value: 3.18e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698   949 TKDIEILRRENEELTEKMKKAEE--EYKLEKEEEISNLKAAFEKNINTERTLKTQAVNKLAEIMNRKD 1014
Cdd:pfam08912    1 TKDVENLAKEKEELNNKLKEQQEelEKAKEEEEEIEKLKASYEKQLNTERTLKTQAVNKLAEIMNRKD 68
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
59-291 4.67e-16

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: 81.15  E-value: 4.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   59 YKDTINK-IRDLRmkaEDYEVVKVIGRGAFGEV-QLVRHKSTRKVYAMKLLSKFE---MIKRSdsaffWEERDIMAFANS 133
Cdd:cd07880     2 YRQEVNKtIWEVP---DRYRDLKQVGSGAYGTVcSALDRRTGAKVAIKKLYRPFQselFAKRA-----YRELRLLKHMKH 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  134 PWVVQLFYAFQDDRYL------YMVMEYMpGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD 207
Cdd:cd07880    74 ENVIGLLDVFTPDLSLdrfhdfYLVMPFM-GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  208 KSGHLKLADFGTCMKMNKEgmvrCDTAVGTPDYISPEVLKSQggdGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTY 287
Cdd:cd07880   153 EDCELKILDFGLARQTDSE----MTGYVVTRWYRAPEVILNW---MHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQL 225

                  ....
gi 167887698  288 SKIM 291
Cdd:cd07880   226 MEIM 229
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
59-291 4.78e-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: 81.25  E-value: 4.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   59 YKDTINKIrdLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSK-FEMIKRSDSAFfwEERDIMAFANSPWVV 137
Cdd:cd07878     2 YRQELNKT--VWEVPERYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRpFQSLIHARRTY--RELRLLKHMKHENVI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  138 QLFYAF------QDDRYLYMVMEYMpGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH 211
Cdd:cd07878    78 GLLDVFtpatsiENFNEVYLVTNLM-GADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  212 LKLADFGTCMKMNKEgmvrCDTAVGTPDYISPEVLKSQggdGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIM 291
Cdd:cd07878   157 LRILDFGLARQADDE----MTGYVATRWYRAPEIMLNW---MHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIM 229
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
494-1099 5.03e-16

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 83.95  E-value: 5.03e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   494 RINEYQRKAEQENEKRRnvenevstLKDQLEDLKKVSQNSQL--ANEKLSQLQKQLEEANDLLRTESDTAV-------RL 564
Cdd:TIGR02168  201 QLKSLERQAEKAERYKE--------LKAELRELELALLVLRLeeLREELEELQEELKEAEEELEELTAELQeleekleEL 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   565 RKSHTEMSKSISQLESLN-------RELQERNRILENSKSQTDKDYYQLQAILEAERRDRGHDSEMIGDLQARITSLQEE 637
Cdd:TIGR02168  273 RLEVSELEEEIEELQKELyalaneiSRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   638 VKHLKhnlEKVEGERKEAQDMLNHSEKEKNNLEiDLNYKLKSLQQRLEQEVNEHKVTKARLTDKHQSIEEAKSVAMCEME 717
Cdd:TIGR02168  353 LESLE---AELEELEAELEELESRLEELEEQLE-TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   718 KKLkeerearekaenrvvqiEKQCSMLDVDLKQSQQKLEHLTGNKERMEDEVKNLTLQLEQESNKRLLLQNELKTQAFEA 797
Cdd:TIGR02168  429 KLE-----------------EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   798 DNLKGLEKQMK---QEINTLLEAKRLLEFELAQLTKQYRGNEG-------------QMRELQDQLEAEQYFSTLYKTQVK 861
Cdd:TIGR02168  492 DSLERLQENLEgfsEGVKALLKNQSGLSGILGVLSELISVDEGyeaaieaalggrlQAVVVENLNAAKKAIAFLKQNELG 571
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   862 ELKEEIEEKNRENLKKI---QELQNEKETLATQLDLAETKAESEQLARGLLEEQYF--ELTQESKKAASRNRQE--ITDK 934
Cdd:TIGR02168  572 RVTFLPLDSIKGTEIQGndrEILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVvdDLDNALELAKKLRPGYriVTLD 651
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   935 DHTVSR--------LEEANSMLTKDIEIlrRENEELTEKMkkaeeeyklekEEEISNLKAAFEKnINTERTLKTQAVNKL 1006
Cdd:TIGR02168  652 GDLVRPggvitggsAKTNSSILERRREI--EELEEKIEEL-----------EEKIAELEKALAE-LRKELEELEEELEQL 717
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  1007 AEIMNRKDFKIDRKKANTQDLRKKEKENRKLQLELNQEREKFNQMVVKHQKELNDMQAQLVEECAHRNELQMQLASKESD 1086
Cdd:TIGR02168  718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
                          650
                   ....*....|...
gi 167887698  1087 IEQLRAKLLDLSD 1099
Cdd:TIGR02168  798 LKALREALDELRA 810
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
74-278 8.42e-16

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: 79.39  E-value: 8.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfeMIKRSDSAFFWEERDI-MAFANSPWVVQLFYAFQDDRYLYMV 152
Cdd:cd06617     1 DDLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRA--TVNSQEQKRLLMDLDIsMRSVDCPYTVTFYGALFREGDVWIC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMpGGDLVNLMSN-YD----VPEKWARFYTAEVVLALDAIHS-MGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMnKE 226
Cdd:cd06617    79 MEVM-DTSLDKFYKKvYDkgltIPEDILGKIAVSIVKALEYLHSkLSVIHRDVKPSNVLINRNGQVKLCDFGISGYL-VD 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 167887698  227 GMVRCDTAvGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd06617   157 SVAKTIDA-GCKPYMAPERINPELNQKGYDVKSDVWSLGITMIELATGRFPY 207
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
81-300 1.29e-15

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: 78.49  E-value: 1.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   81 VIGRGAFGEV-------QLVRHKSTRKVYAMKLLSKFEMIkRSDSAFFWEERdimafanSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd14148     1 IIGVGGFGKVykglwrgEEVAVKAARQDPDEDIAVTAENV-RQEARLFWMLQ-------HPNIIALRGVCLNPPHLCLVM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGF---IHRDVKPDNMLL-------DKSGH-LKLADFGTCMK 222
Cdd:cd14148    73 EYARGGALNRALAGKKVPPHVLVNWAVQIARGMNYLHNEAIvpiIHRDLKSSNILIlepiendDLSGKtLKITDFGLARE 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167887698  223 MNKEGMVrcdTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYA-DSLVGTYSKIMnhkNSLTFP 300
Cdd:cd14148   153 WHKTTKM---SAAGTYAWMAPEVIRLS----LFSKSSDVWSFGVLLWELLTGEVPYREiDALAVAYGVAM---NKLTLP 221
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
76-301 1.47e-15

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: 79.08  E-value: 1.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLsKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDD--------- 146
Cdd:cd07864     9 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKV-RLDNEKEGFPITAIREIKILRQLNHRSVVNLKEIVTDKqdaldfkkd 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  147 -RYLYMVMEYMpGGDLVNLMSN--YDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKM 223
Cdd:cd07864    88 kGAFYLVFEYM-DHDLMGLLESglVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLARLY 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  224 NKEGMVRCDTAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVG---TYSKIMNHKNSLTFP 300
Cdd:cd07864   167 NSEESRPYTNKVITLWYRPPELLL---GEERYGPAIDVWSCGCILGELFTKKPIFQANQELAqleLISRLCGSPCPAVWP 243

                  .
gi 167887698  301 D 301
Cdd:cd07864   244 D 244
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
59-278 1.49e-15

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: 79.70  E-value: 1.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   59 YKDTINKIrdLRMKAEDYEVVKVIGRGAFGEV-QLVRHKSTRKVYAMKLLSKFEMI---KRSdsaffWEERDIMAFANSP 134
Cdd:cd07877     4 YRQELNKT--IWEVPERYQNLSPVGSGAYGSVcAAFDTKTGLRVAVKKLSRPFQSIihaKRT-----YRELRLLKHMKHE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  135 WVVQLFYAFQDDRYL------YMVMEYMpGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDK 208
Cdd:cd07877    77 NVIGLLDVFTPARSLeefndvYLVTHLM-GADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNE 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  209 SGHLKLADFGTCMKMNKEgmvrCDTAVGTPDYISPEVLKSQggdGYYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd07877   156 DCELKILDFGLARHTDDE----MTGYVATRWYRAPEIMLNW---MHYNQTVDIWSVGCIMAELLTGRTLF 218
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
82-278 1.57e-15

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: 78.81  E-value: 1.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSaffW-EERDIMAFANSPWVV-------QLFYAFQDDRYLymVM 153
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELSVKNKDR---WcHEIQIMKKLNHPNVVkacdvpeEMNFLVNDVPLL--AM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNydvPEKWARFYTAEVVLALDAI-------HSMGFIHRDVKPDNMLL-DKSGHL--KLADFGTCMKM 223
Cdd:cd14039    76 EYCSGGDLRKLLNK---PENCCGLKESQVLSLLSDIgsgiqylHENKIIHRDLKPENIVLqEINGKIvhKIIDLGYAKDL 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  224 NKEGMvrCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd14039   153 DQGSL--CTSFVGTLQYLAPELFENKS----YTVTVDYWSFGTMVFECIAGFRPF 201
pknD PRK13184
serine/threonine-protein kinase PknD;
76-278 2.07e-15

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 81.74  E-value: 2.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKS-TRKVYAMKL---LSKFEMIKRSdsafFWEERDIMAFANSPWVVQLFYAFQDDRYLYM 151
Cdd:PRK13184    4 YDIIRLIGKGGMGEVYLAYDPVcSRRVALKKIredLSENPLLKKR----FLREAKIAADLIHPGIVPVYSICSDGDPVYY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  152 VMEYMPGGDLVNLMSNY--------------DVPEKWARFYTaeVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADF 217
Cdd:PRK13184   80 TMPYIEGYTLKSLLKSVwqkeslskelaektSVGAFLSIFHK--ICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDW 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  218 GTC------------MKMNKEG-----MVRCDTAVGTPDYISPEVLKSQGGDgyygRECDWWSVGVFLYEMLVGDTPF 278
Cdd:PRK13184  158 GAAifkkleeedlldIDVDERNicyssMTIPGKIVGTPDYMAPERLLGVPAS----ESTDIYALGVILYQMLTLSFPY 231
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
82-278 2.10e-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: 77.57  E-value: 2.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVqlVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDD-RYLYMVMEYMPGGD 160
Cdd:cd14064     1 IGSGSFGKV--YKGRCRNKIVAIKRYRANTYCSKSDVDMFCREVSILCRLNHPCVIQFVGACLDDpSQFAIVTQYVSGGS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  161 LVNLMSNydvpEKWARFYTAEVVLALDAIHSMGF--------IHRDVKPDNMLLDKSGHLKLADFGTC---MKMNKEGMV 229
Cdd:cd14064    79 LFSLLHE----QKRVIDLQSKLIIAVDVAKGMEYlhnltqpiIHRDLNSHNILLYEDGHAVVADFGESrflQSLDEDNMT 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 167887698  230 RcdtAVGTPDYISPEVLkSQGGDgyYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd14064   155 K---QPGNLRWMAPEVF-TQCTR--YSIKADVFSYALCLWELLTGEIPF 197
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
80-300 2.12e-15

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: 78.16  E-value: 2.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEV-------QLVRHKSTRKVYAMKLLSKFEMIKrsdsaffwEERDIMAFANSPWVVQLFYAFQDDRYLYMV 152
Cdd:cd14145    12 EIIGIGGFGKVyraiwigDEVAVKAARHDPDEDISQTIENVR--------QEAKLFAMLKHPNIIALRGVCLKEPNLCLV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGF---IHRDVKPDNMLL-------DKSGH-LKLADFGTCM 221
Cdd:cd14145    84 MEFARGGPLNRVLSGKRIPPDILVNWAVQIARGMNYLHCEAIvpvIHRDLKSSNILIlekvengDLSNKiLKITDFGLAR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  222 KMNKEGMVrcdTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYA-DSLVGTYSKIMNhKNSLTFP 300
Cdd:cd14145   164 EWHRTTKM---SAAGTYAWMAPEVIRSS----MFSKGSDVWSYGVLLWELLTGEVPFRGiDGLAVAYGVAMN-KLSLPIP 235
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
82-317 2.31e-15

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: 77.74  E-value: 2.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSkFEMIKRSDSaffweerDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd13995    12 IPRGAFGKVYLAQDTKTKKRMACKLIP-VEQFKPSDV-------EIQACFRHENIAELYGALLWEETVHLFMEAGEGGSV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 V-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLdKSGHLKLADFGTCMKMNKEGMVRCDTAvGTPDY 240
Cdd:cd13995    84 LeKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVF-MSTKAVLVDFGLSVQMTEDVYVPKDLR-GTEIY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  241 ISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPF---YADSLVGTYSKIMnHKNSLTFPD-DNDISKEAKNLICAF 316
Cdd:cd13995   162 MSPEVILCRG----HNTKADIYSLGATIIHMQTGSPPWvrrYPRSAYPSYLYII-HKQAPPLEDiAQDCSPAMRELLEAA 236

                  .
gi 167887698  317 L 317
Cdd:cd13995   237 L 237
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
75-282 2.52e-15

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: 78.23  E-value: 2.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMK---LLSKFEMIKRSDSaffwEERDIMAFANSPWVVQLFYAFQDDRYLYM 151
Cdd:cd07861     1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKkirLESEEEGVPSTAI----REISLLKELQHPNIVCLEDVLMQENRLYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  152 VMEYMpGGDLVNLM----SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMnkeG 227
Cdd:cd07861    77 VFEFL-SMDLKKYLdslpKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAF---G 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  228 M-VRCDT-AVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADS 282
Cdd:cd07861   153 IpVRVYThEVVTLWYRAPEVLL---GSPRYSTPVDIWSIGTIFAEMATKKPLFHGDS 206
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
70-317 2.64e-15

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 80.30  E-value: 2.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   70 RMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSkFEMIKRSDSAFFWEERDIMAFANSPWVVQLF--YAFQDDR 147
Cdd:PTZ00283   28 KEQAKKYWISRVLGSGATGTVLCAKRVSDGEPFAVKVVD-MEGMSEADKNRAQAEVCCLLNCDFFSIVKCHedFAKKDPR 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  148 ------YLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTA-----EVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLAD 216
Cdd:PTZ00283  107 npenvlMIALVLDYANAGDLRQEIKSRAKTNRTFREHEAgllfiQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGD 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  217 FG-TCMKMNKEGMVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLvgtySKIMNHKN 295
Cdd:PTZ00283  187 FGfSKMYAATVSDDVGRTFCGTPYYVAPEIWRRKP----YSKKADMFSLGVLLYELLTLKRPFDGENM----EEVMHKTL 258
                         250       260
                  ....*....|....*....|...
gi 167887698  296 SLTF-PDDNDISKEAKNLICAFL 317
Cdd:PTZ00283  259 AGRYdPLPPSISPEMQEIVTALL 281
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
67-300 2.67e-15

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: 77.76  E-value: 2.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   67 RDLRMKaedyevvKVIGRGAFGEV-------QLVRHKSTRKVYAMKLLSKFEMIKrsdsaffwEERDIMAFANSPWVVQL 139
Cdd:cd14147     3 QELRLE-------EVIGIGGFGKVyrgswrgELVAVKAARQDPDEDISVTAESVR--------QEARLFAMLAHPNIIAL 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  140 FYAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGF---IHRDVKPDNMLLDKSGH----- 211
Cdd:cd14147    68 KAVCLEEPNLCLVMEYAAGGPLSRALAGRRVPPHVLVNWAVQIARGMHYLHCEALvpvIHRDLKSNNILLLQPIEnddme 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  212 ---LKLADFGTCMKMNKEGMVrcdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYA-DSLVGTY 287
Cdd:cd14147   148 hktLKITDFGLAREWHKTTQM---SAAGTYAWMAPEVIKAST----FSKGSDVWSFGVLLWELLTGEVPYRGiDCLAVAY 220
                         250
                  ....*....|...
gi 167887698  288 SKIMnhkNSLTFP 300
Cdd:cd14147   221 GVAV---NKLTLP 230
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
65-342 2.68e-15

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: 78.54  E-value: 2.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   65 KIRDLRMKAEDYEV---VKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFY 141
Cdd:cd06633     9 EIADLFYKDDPEEIfvdLHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKWQDIIKEVKFLQQLKHPNTIEYKG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  142 AFQDDRYLYMVMEYMPGG--DLVNLMSNyDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGT 219
Cdd:cd06633    89 CYLKDHTAWLVMEYCLGSasDLLEVHKK-PLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  220 CMKMNKegmvrCDTAVGTPDYISPEVLKSQgGDGYYGRECDWWSVGVFLYEMLVGDTP-FYADSLVGTYSKIMNHKNSLt 298
Cdd:cd06633   168 ASIASP-----ANSFVGTPYWMAPEVILAM-DEGQYDGKVDIWSLGITCIELAERKPPlFNMNAMSALYHIAQNDSPTL- 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 167887698  299 fpDDNDISKEAKNLICAFLtdREVRLGRNGVEEIKRHLFFKNDQ 342
Cdd:cd06633   241 --QSNEWTDSFRGFVDYCL--QKIPQERPSSAELLRHDFVRRER 280
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
425-953 2.97e-15

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 81.52  E-value: 2.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  425 QESLQKTIYKLEEQLHNEMQLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKEKMLLQHRINEYQRKAEQ 504
Cdd:COG1196   241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  505 ENEKRRNVENEVSTLKDQLEDLKKVSQNSQ----LANEKLSQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSISQLES 580
Cdd:COG1196   321 LEEELAELEEELEELEEELEELEEELEEAEeeleEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  581 LNRELQERNRILENSKSQTDKDYYQLQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVEGERKEAQDMLN 660
Cdd:COG1196   401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  661 hsekEKNNLEIDLNYKLKSLQQRLEQEVNEHKVTKARLTDKHQS--IEEAKSVAMCEMEKKLKEEREAREKAENRVVQIE 738
Cdd:COG1196   481 ----ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDD 556
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  739 KQCSMLDVDLKQ--------------SQQKLEHLTGNKERMEDEVKNLTLQLEQESNKRLLLQNELKTQAFEADNLKGLE 804
Cdd:COG1196   557 EVAAAAIEYLKAakagratflpldkiRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  805 KQMKqeinTLLEAKRLLEFELAQLTKQYRGNEGQMRELQDQLEAEQYFSTLYKTQVKELKEEIEEKNRENLKKIQELQNE 884
Cdd:COG1196   637 RRAV----TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167887698  885 KETLATQLDLAETKAESEQLARGLLEEQYFELTQESKKAASRNRQEITDKDHTVSRLEEansmLTKDIE 953
Cdd:COG1196   713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER----LEREIE 777
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
85-278 3.11e-15

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 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: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 77.54  E-value: 3.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   85 GAFGEVQLVRHKsTRKVYAMKLLSKFEMIKRSDSAFFwEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNL 164
Cdd:cd14027     4 GGFGKVSLCFHR-TQGLVVLKTVYTGPNCIEHNEALL-EEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMHV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  165 MSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCM-----KMNKEGMVR-------CD 232
Cdd:cd14027    82 LKKVSVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsKLTKEEHNEqrevdgtAK 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 167887698  233 TAVGTPDYISPEVLKSQGGDGyyGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd14027   162 KNAGTLYYMAPEHLNDVNAKP--TEKSDVYSFAIVLWAIFANKEPY 205
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
450-1100 3.97e-15

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 80.87  E-value: 3.97e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   450 EQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKEKMLLQHRINEYQRKAEQENEKRRNVENEV----STLKDQLED 525
Cdd:TIGR02168  217 ELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIeelqKELYALANE 296
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   526 LKKVSQNSQLANEKLSQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSISQL----ESLNRELQERNRILENSKSQTDk 601
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELkeelESLEAELEELEAELEELESRLE- 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   602 dyyQLQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVEGERKEAQDMLNHSEKEKNNLEID-LNYKLKSL 680
Cdd:TIGR02168  376 ---ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEeLEEELEEL 452
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   681 QQRLEQEVNEHKVTKARLTDKHQSIEEAKSvamcemekklkeerearekaenrvvqiekqcsmldvDLKQSQQKLEHLTG 760
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQALDAAER------------------------------------ELAQLQARLDSLER 496
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   761 NKERMEDE---VKNLTLQLEQESNKRLLLQNELKT-----QAFEA---DNLKGL----EKQMKQEINTLLEAK--RLLEF 823
Cdd:TIGR02168  497 LQENLEGFsegVKALLKNQSGLSGILGVLSELISVdegyeAAIEAalgGRLQAVvvenLNAAKKAIAFLKQNElgRVTFL 576
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   824 ELAQLTKQY-RGNEGQMRELQDQleAEQYFSTLYKTQVKELKEEIEEKNR----ENLKKIQELQNE---KETLATQldla 895
Cdd:TIGR02168  577 PLDSIKGTEiQGNDREILKNIEG--FLGVAKDLVKFDPKLRKALSYLLGGvlvvDDLDNALELAKKlrpGYRIVTL---- 650
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   896 etkaESEQLARGlleeqyFELTQESKKAAS---RNRQEITDKDHTVSRLEEANSMLTKDIEILRRENEELtEKMKKAEEE 972
Cdd:TIGR02168  651 ----DGDLVRPG------GVITGGSAKTNSsilERRREIEELEEKIEELEEKIAELEKALAELRKELEEL-EEELEQLRK 719
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   973 YKLEKEEEISNLKAAFEKnintertlKTQAVNKLAEIMNRKDFKIDRKKANTQDLRKKEKENRKLQLELNQEREKFNQMV 1052
Cdd:TIGR02168  720 ELEELSRQISALRKDLAR--------LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI 791
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*...
gi 167887698  1053 VKHQKELNDMQAQLVEECAHRNELQMQLASKESDIEQLRAKLLDLSDS 1100
Cdd:TIGR02168  792 EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
82-279 4.02e-15

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: 77.31  E-value: 4.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVqlvrHKSTR---KVYAMKLLskFEMIKRSDSAFFWEERDIMAFANSPWVVQLF-YAFQDDRYLyMVMEYMP 157
Cdd:cd14066     1 IGSGGFGTV----YKGVLengTVVAVKRL--NEMNCAASKKEFLTELEMLGRLRHPNLVRLLgYCLESDEKL-LVYEYMP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  158 GGDLVNLMSNYD--VPEKW-ARFYTA-EVVLALDAIHSMGF---IHRDVKPDNMLLDKSGHLKLADFGTCMKMN-KEGMV 229
Cdd:cd14066    74 NGSLEDRLHCHKgsPPLPWpQRLKIAkGIARGLEYLHEECPppiIHGDIKSSNILLDEDFEPKLTDFGLARLIPpSESVS 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 167887698  230 RCDTAVGTPDYISPEVLKSqggdGYYGRECDWWSVGVFLYEMLVGDTPFY 279
Cdd:cd14066   154 KTSAVKGTIGYLAPEYIRT----GRVSTKSDVYSFGVVLLELLTGKPAVD 199
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
419-965 4.02e-15

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 80.88  E-value: 4.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  419 NADKSLQEsLQKTIYKLEEQLHNEMQLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKEKMLLQ---HRI 495
Cdd:PRK03918  162 NAYKNLGE-VIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEelkEEI 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  496 NEYQRKAEQENEKRRNVENEVSTLKDQLEDLKKVSQNSQLANEKLSQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSI 575
Cdd:PRK03918  241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  576 SQLESLNRELQERN------RILENSKSQTDKDYYQLQAILEAERRDRGHDSEMIGdLQARITSLqeEVKHLKHNLEKVE 649
Cdd:PRK03918  321 EEINGIEERIKELEekeerlEELKKKLKELEKRLEELEERHELYEEAKAKKEELER-LKKRLTGL--TPEKLEKELEELE 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  650 GERKEAQDMLNHSEKEKNNLEIDLNYKLKSLqQRLEQEVNEHKVTKARLTDKHQ-SIEEAKSVAMCEMEKKLKEEREARE 728
Cdd:PRK03918  398 KAKEEIEEEISKITARIGELKKEIKELKKAI-EELKKAKGKCPVCGRELTEEHRkELLEEYTAELKRIEKELKEIEEKER 476
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  729 KAENRVVQIEKQCSmldvdlkqsqqKLEHLTGNKErMEDEVKNLTLQLEQESNKrlllqnELKTQAFEADNLKGLEKQMK 808
Cdd:PRK03918  477 KLRKELRELEKVLK-----------KESELIKLKE-LAEQLKELEEKLKKYNLE------ELEKKAEEYEKLKEKLIKLK 538
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  809 QEINTL---LEAKRLLEFELAQLTKQYRGNEGQMRELQDQLEaEQYFSTLykTQVKELKEEIEEKNRENL------KKIQ 879
Cdd:PRK03918  539 GEIKSLkkeLEKLEELKKKLAELEKKLDELEEELAELLKELE-ELGFESV--EELEERLKELEPFYNEYLelkdaeKELE 615
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  880 ELQNEKETLATQLD-----LAETKAESEQLaRGLLEEQYFELTQESKKAASRN----RQEITDKDHTVSRLEEANSMLTK 950
Cdd:PRK03918  616 REEKELKKLEEELDkafeeLAETEKRLEEL-RKELEELEKKYSEEEYEELREEylelSRELAGLRAELEELEKRREEIKK 694
                         570
                  ....*....|....*
gi 167887698  951 DIEILRRENEELTEK 965
Cdd:PRK03918  695 TLEKLKEELEEREKA 709
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
76-271 6.24e-15

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: 77.41  E-value: 6.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllsKFEMIKRSD----SAFfwEERDIMAFANSPWVVQLF-----YAFQDD 146
Cdd:cd07865    14 YEKLAKIGQGTFGEVFKARHRKTGQIVALK---KVLMENEKEgfpiTAL--REIKILQLLKHENVVNLIeicrtKATPYN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  147 RY---LYMVMEYMPGgDLVNLMSNYDVpekwaRFYTAEV-------VLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLAD 216
Cdd:cd07865    89 RYkgsIYLVFEFCEH-DLAGLLSNKNV-----KFTLSEIkkvmkmlLNGLYYIHRNKILHRDMKAANILITKDGVLKLAD 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  217 FGTC--MKMNKEGMVRCDTA-VGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEM 271
Cdd:cd07865   163 FGLAraFSLAKNSQPNRYTNrVVTLWYRPPELLL---GERDYGPPIDMWGAGCIMAEM 217
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
74-278 9.22e-15

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: 76.23  E-value: 9.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVyAMKLLSKFEMikrSDSAFFwEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd05072     7 ESIKLVKKLGAGQFGEVWMGYYNNSTKV-AVKTLKPGTM---SVQAFL-EEANLMKTLQHDKLVRLYAVVTKEEPIYIIT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLM-----SNYDVPEKWArfYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGM 228
Cdd:cd05072    82 EYMAKGSLLDFLksdegGKVLLPKLID--FSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEY 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 167887698  229 VRCDTAVGTPDYISPEVLKSqggdGYYGRECDWWSVGVFLYEMLV-GDTPF 278
Cdd:cd05072   160 TAREGAKFPIKWTAPEAINF----GSFTIKSDVWSFGILLYEIVTyGKIPY 206
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
79-278 1.00e-14

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 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: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 76.11  E-value: 1.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   79 VKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPG 158
Cdd:cd14026     2 LRYLSRGAFGTVSRARHADWRVTVAIKCLKLDSPVGDSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  159 GDLVNLMSNYDV------PEKWARFYtaEVVLALDAIHSMG--FIHRDVKPDNMLLDKSGHLKLADFGTC----MKMNKE 226
Cdd:cd14026    82 GSLNELLHEKDIypdvawPLRLRILY--EIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSkwrqLSISQS 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 167887698  227 GMVRCDTAVGTPDYISPEVL----KSQGGDGYygrecDWWSVGVFLYEMLVGDTPF 278
Cdd:cd14026   160 RSSKSAPEGGTIIYMPPEEYepsqKRRASVKH-----DIYSYAIIMWEVLSRKIPF 210
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
74-282 1.11e-14

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: 76.41  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLlSKFEMIKRS-DSAFFWEERDIMAFANSPWVVQLF---YAFQDDR-Y 148
Cdd:cd07837     1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKK-TRLEMEEEGvPSTALREVSLLQMLSQSIYIVRLLdveHVEENGKpL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 LYMVMEYMpGGDLVNLMSNY------DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKS-GHLKLADFG--- 218
Cdd:cd07837    80 LYLVFEYL-DTDLKKFIDSYgrgphnPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQkGLLKIADLGlgr 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  219 ---TCMKMNKEGMVrcdtavgTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADS 282
Cdd:cd07837   159 aftIPIKSYTHEIV-------TLWYRAPEVLL---GSTHYSTPVDMWSVGCIFAEMSRKQPLFPGDS 215
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
77-313 1.14e-14

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: 75.78  E-value: 1.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   77 EVVKVIGRGAFGEVQLVRHKSTRKVYAMKllskfEMIKRSDSAF--FWEERDIMA-FANSPWVVQLF--YAFQ--DDRY- 148
Cdd:cd14037     6 TIEKYLAEGGFAHVYLVKTSNGGNRAALK-----RVYVNDEHDLnvCKREIEIMKrLSGHKNIVGYIdsSANRsgNGVYe 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 LYMVMEYMPGGDLVNLM----SNydvpekwaRFYTAEVV-------LALDAIHSMG--FIHRDVKPDNMLLDKSGHLKLA 215
Cdd:cd14037    81 VLLLMEYCKGGGVIDLMnqrlQT--------GLTESEILkifcdvcEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLC 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  216 DFG-TCMKM----NKEGMvrcdTAV-------GTPDYISPEVLksqggDGYYGRE----CDWWSVGVFLYEMLVGDTPFY 279
Cdd:cd14037   153 DFGsATTKIlppqTKQGV----TYVeedikkyTTLQYRAPEMI-----DLYRGKPitekSDIWALGCLLYKLCFYTTPFE 223
                         250       260       270
                  ....*....|....*....|....*....|....
gi 167887698  280 ADSLVGtyskIMNHKnsLTFPDDNDISKEAKNLI 313
Cdd:cd14037   224 ESGQLA----ILNGN--FTFPDNSRYSKRLHKLI 251
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
140-285 1.20e-14

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: 75.47  E-value: 1.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  140 FYAFQDDRY-------LYMVMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH 211
Cdd:cd14012    63 YLAFSIERRgrsdgwkVYLLTEYAPGGSLSELLDSVGsVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAG 142
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  212 ---LKLADFGTCMKMNKEGMVRCDTAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVG-DTPFYADSLVG 285
Cdd:cd14012   143 tgiVKLTDYSLGKTLLDMCSRGSLDEFKQTYWLPPELAQ---GSKSPTRKTDVWDLGLLFLQMLFGlDVLEKYTSPNP 217
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
75-282 1.43e-14

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: 76.25  E-value: 1.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllsKFEMIKRSDSAFFWEERDIMAFAN--SPWVVQLFYAFQDDRY--LY 150
Cdd:cd07845     8 EFEKLNRIGEGTYGIVYRARDTTSGEIVALK---KVRMDNERDGIPISSLREITLLLNlrHPNIVELKEVVVGKHLdsIF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGgDLVNLMSNYDVPekwarFYTAEV------VL-ALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGtcMKM 223
Cdd:cd07845    85 LVMEYCEQ-DLASLLDNMPTP-----FSESQVkclmlqLLrGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFG--LAR 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  224 NKEGMVRCDT-AVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADS 282
Cdd:cd07845   157 TYGLPAKPMTpKVVTLWYRAPELLL---GCTTYTTAIDMWAVGCILAELLAHKPLLPGKS 213
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
82-278 1.73e-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: 75.77  E-value: 1.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSaffWE-ERDIMAFANSPWVV-------QLFYAFQDDRYLyMVM 153
Cdd:cd14038     2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRER---WClEIQIMKRLNHPNVVaardvpeGLQKLAPNDLPL-LAM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDL---VNLMSNY-DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHL---KLADFGTCMKMNKE 226
Cdd:cd14038    78 EYCQGGDLrkyLNQFENCcGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRlihKIIDLGYAKELDQG 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 167887698  227 GMvrCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd14038   158 SL--CTSFVGTLQYLAPELLEQQK----YTVTVDYWSFGTLAFECITGFRPF 203
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
425-1080 2.84e-14

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 78.29  E-value: 2.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   425 QESLQKTIYKLEEQLHNEMQLKDEMEQKCrtsnIKLDKIMKELD-----------EEGNQRRNLESTVSQIEKEKMLLQH 493
Cdd:pfam01576  428 RAELAEKLSKLQSELESVSSLLNEAEGKN----IKLSKDVSSLEsqlqdtqellqEETRQKLNLSTRLRQLEDERNSLQE 503
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   494 RIneyqrkaEQENEKRRNVENEVSTLKDQLEDLKK----VSQNSQLANEKLSQLQKQLEEANDLLRTESDTAVRLRKSHT 569
Cdd:pfam01576  504 QL-------EEEEEAKRNVERQLSTLQAQLSDMKKkleeDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKN 576
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   570 EMSKsisQLESLNRELQERNRI---LENSKSQTDKDYYQLQAILE--AERRDRGHDSEMIGDLQA-RITSLQEEVKHLKH 643
Cdd:pfam01576  577 RLQQ---ELDDLLVDLDHQRQLvsnLEKKQKKFDQMLAEEKAISAryAEERDRAEAEAREKETRAlSLARALEEALEAKE 653
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   644 NLEKV-EGERKEAQDMLNHSEKEKNNLeidlnYKLKSLQQRLEQEVNEHKVTKARLTDKHQSIEEAK---SVAMCEMEKK 719
Cdd:pfam01576  654 ELERTnKQLRAEMEDLVSSKDDVGKNV-----HELERSKRALEQQVEEMKTQLEELEDELQATEDAKlrlEVNMQALKAQ 728
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   720 LKEE-REAREKAENRVVQIEKQCSMLDVDLKQSQQKLEHLTGNKERMEDEVKNLTLQLEQESNKRlllqNELKTQafead 798
Cdd:pfam01576  729 FERDlQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGR----EEAVKQ----- 799
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   799 nLKGLEKQMKQEINTLLEAKRLLEFELAQLT---KQYRGNEGQMRELQDQLEAeqyfSTLYKTQVKELKEEIEEKNRENL 875
Cdd:pfam01576  800 -LKKLQAQMKDLQRELEEARASRDEILAQSKeseKKLKNLEAELLQLQEDLAA----SERARRQAQQERDELADEIASGA 874
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   876 KKIQELQNEKETLATQLDLAETKAESEQLARGLLEEQYFELTQESKKAASrnrqEITDKDHTVSRLEEANSMltkdieiL 955
Cdd:pfam01576  875 SGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTT----ELAAERSTSQKSESARQQ-------L 943
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   956 RRENEELTEKMKKAEEEYKLEKEEEISNLKAafeknintertlktqavnKLAEIMNRKDFKIDRKKANTQDLRKKEKENR 1035
Cdd:pfam01576  944 ERQNKELKAKLQEMEGTVKSKFKSSIAALEA------------------KIAQLEEQLEQESRERQAANKLVRRTEKKLK 1005
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  1036 KLQLELNQER----------EKFNQMVVKHQKELNDMQAQLVEECAHRNELQMQL 1080
Cdd:pfam01576 1006 EVLLQVEDERrhadqykdqaEKGNSRMKQLKRQLEEAEEEASRANAARRKLQREL 1060
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
74-278 3.88e-14

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: 74.30  E-value: 3.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEV------QLVRHKSTRKVyAMKLLSKFEMIkrSDSAFFWEERDIMAFANSPWVVQLFYAFQDDR 147
Cdd:cd05032     6 EKITLIRELGQGSFGMVyeglakGVVKGEPETRV-AIKTVNENASM--RERIEFLNEASVMKEFNCHHVVRLLGVVSTGQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  148 YLYMVMEYMPGGDLVNLM----------SNYDVPE-----KWArfytAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHL 212
Cdd:cd05032    83 PTLVVMELMAKGDLKSYLrsrrpeaennPGLGPPTlqkfiQMA----AEIADGMAYLAAKKFVHRDLAARNCMVAEDLTV 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  213 KLADFGTCMKMNKEGMVRCDTAVGTP-DYISPEVLKsqggDGYYGRECDWWSVGVFLYEML-VGDTPF 278
Cdd:cd05032   159 KIGDFGMTRDIYETDYYRKGGKGLLPvRWMAPESLK----DGVFTTKSDVWSFGVVLWEMAtLAEQPY 222
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
70-317 5.87e-14

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 75.84  E-value: 5.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   70 RMKAEDYEVVKVIGRGAFGEV-QLVRHKSTRKVYAMKLLSKFEmikrsdsaffWEERDIMAFAN----------SPWVVQ 138
Cdd:PTZ00036   62 RSPNKSYKLGNIIGNGSFGVVyEAICIDTSEKVAIKKVLQDPQ----------YKNRELLIMKNlnhiniiflkDYYYTE 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  139 LFYAFQDDRYLYMVMEYMPGgDLVNLM-----SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH-L 212
Cdd:PTZ00036  132 CFKKNEKNIFLNVVMEFIPQ-TVHKYMkhyarNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHtL 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  213 KLADFGTCmkMNKEGMVRCDTAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLV-------- 284
Cdd:PTZ00036  211 KLCDFGSA--KNLLAGQRSVSYICSRFYRAPELML---GATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVdqlvriiq 285
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 167887698  285 --GTYS----KIMN-HKNSLTFPD--DNDISK--------EAKNLICAFL 317
Cdd:PTZ00036  286 vlGTPTedqlKEMNpNYADIKFPDvkPKDLKKvfpkgtpdDAINFISQFL 335
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
83-278 6.44e-14

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: 73.07  E-value: 6.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   83 GRGAFGEVQLVRHKSTRKVYAMKLLSKFEmikrsdsaffwEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLV 162
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDKEVAVKKLLKIE-----------KEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLF 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  163 NLMSNYDVPE-------KWARfytaEVVLALDAIHS---MGFIHRDVKPDNMLLDKSGHLKLADFGTCmKMNKEGMVRcd 232
Cdd:cd14060    71 DYLNSNESEEmdmdqimTWAT----DIAKGMHYLHMeapVKVIHRDLKSRNVVIAADGVLKICDFGAS-RFHSHTTHM-- 143
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 167887698  233 TAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd14060   144 SLVGTFPWMAPEVIQSLP----VSETCDTYSYGVVLWEMLTREVPF 185
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
76-307 7.56e-14

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: 74.37  E-value: 7.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSK-FEMIKRSDSAFfwEERDIMAFANSPWVVQLFYAFQDDRYL----- 149
Cdd:cd07850     2 YQNLKPIGSGAQGIVCAAYDTVTGQNVAIKKLSRpFQNVTHAKRAY--RELVLMKLVNHKNIIGLLNVFTPQKSLeefqd 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 -YMVMEYMPGgdlvNLMS--NYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKE 226
Cdd:cd07850    80 vYLVMELMDA----NLCQviQMDLDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  227 GMVrcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHknsLTFPDDNDIS 306
Cdd:cd07850   156 FMM--TPYVVTRYYRAPEVILGMG----YKENVDIWSVGCIMGEMIRGTVLFPGTDHIDQWNKIIEQ---LGTPSDEFMS 226

                  .
gi 167887698  307 K 307
Cdd:cd07850   227 R 227
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
71-278 8.71e-14

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: 73.09  E-value: 8.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   71 MKAEDYEVVKVIGRGAFGEVQLVRHKSTRkvYAMKLlskfemIKRSDSA-FFWEERDIMAFANSPWVVQLFYAFQDDR-Y 148
Cdd:cd05082     3 LNMKELKLLQTIGKGEFGDVMLGDYRGNK--VAVKC------IKNDATAqAFLAEASVMTQLRHSNLVQLLGVIVEEKgG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 LYMVMEYMPGGDLVNLMSNYDVP----EKWARFyTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGtcmkMN 224
Cdd:cd05082    75 LYIVTEYMAKGSLVDYLRSRGRSvlggDCLLKF-SLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFG----LT 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  225 KEGMVRCDTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEML-VGDTPF 278
Cdd:cd05082   150 KEASSTQDTGKLPVKWTAPEALREK----KFSTKSDVWSFGILLWEIYsFGRVPY 200
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
72-284 8.87e-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: 73.51  E-value: 8.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   72 KAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSkfemIKRSDSAFFWEERDIMAFAN--SPWVVQLFYAFQDDRYL 149
Cdd:cd07871     3 KLETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIR----LEHEEGAPCTAIREVSLLKNlkHANIVTLHDIIHTERCL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 YMVMEYMPGgDLV-------NLMSNYDVpekwaRFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMK 222
Cdd:cd07871    79 TLVFEYLDS-DLKqyldncgNLMSMHNV-----KIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARA 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887698  223 MNKEGMVRCDTAVgTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGdTPFYADSLV 284
Cdd:cd07871   153 KSVPTKTYSNEVV-TLWYRPPDVLL---GSTEYSTPIDMWGVGCILYEMATG-RPMFPGSTV 209
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
80-338 9.79e-14

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: 73.08  E-value: 9.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVqlvrhkstrkVYAMKLLSKFEMIKRSDSAFF-WEERDIMAFANS---PWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd13982     7 KVLGYGSEGTI----------VFRGTFDGRPVAVKRLLPEFFdFADREVQLLRESdehPNVIRYFCTEKDRQFLYIALEL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPggdlVNLMSNYDVPEKWARF-------YTA--EVVLALDAIHSMGFIHRDVKPDNMLLDKS---GHLK--LADFGTCM 221
Cdd:cd13982    77 CA----ASLQDLVESPRESKLFlrpglepVRLlrQIASGLAHLHSLNIVHRDLKPQNILISTPnahGNVRamISDFGLCK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  222 KMN-KEGMVRCDTAV-GTPDYISPEVLkSQGGDGYYGRECDWWSVG-VFLYEMLVGDTPFyADSLVGTYSkIMNHKNSLT 298
Cdd:cd13982   153 KLDvGRSSFSRRSGVaGTSGWIAPEML-SGSTKRRQTRAVDIFSLGcVFYYVLSGGSHPF-GDKLEREAN-ILKGKYSLD 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 167887698  299 FPDDnDISK--EAKNLICAFL-TDREVrlgRNGVEEIKRHLFF 338
Cdd:cd13982   230 KLLS-LGEHgpEAQDLIERMIdFDPEK---RPSAEEVLNHPFF 268
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
81-300 1.12e-13

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: 72.76  E-value: 1.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   81 VIGRGAFGEV-------QLVRHKSTRKVYAMKLLSKFEMIKRsdsaffweERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd14146     1 IIGVGGFGKVyratwkgQEVAVKAARQDPDEDIKATAESVRQ--------EAKLFSMLRHPNIIKLEGVCLEEPNLCLVM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYD----------VPEKWARFYTAEVVLALDAIHSMGF---IHRDVKPDN-MLLDKSGH-------L 212
Cdd:cd14146    73 EFARGGTLNRALAAANaapgprrarrIPPHILVNWAVQIARGMLYLHEEAVvpiLHRDLKSSNiLLLEKIEHddicnktL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  213 KLADFGTCMKMNKEGMVrcdTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYA-DSLVGTYSKIM 291
Cdd:cd14146   153 KITDFGLAREWHRTTKM---SAAGTYAWMAPEVIKSS----LFSKGSDIWSYGVLLWELLTGEVPYRGiDGLAVAYGVAV 225

                  ....*....
gi 167887698  292 nhkNSLTFP 300
Cdd:cd14146   226 ---NKLTLP 231
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
151-278 1.16e-13

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: 72.14  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGGDLVNLM--SNYDVPE---KWARfytaEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNK 225
Cdd:cd14059    58 ILMEYCPYGQLYEVLraGREITPSllvDWSK----QIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSE 133
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  226 EG--MvrcdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd14059   134 KStkM----SFAGTVAWMAPEVIRNEP----CSEKVDIWSFGVVLWELLTGEIPY 180
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
82-281 1.48e-13

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: 72.67  E-value: 1.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEmikRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd14222     1 LGKGFFGQAIKVTHKATGKVMVMKELIRCD---EETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNYDvPEKWAR--FYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKM-------------NKE 226
Cdd:cd14222    78 KDFLRADD-PFPWQQkvSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveekkkpppdkptTKK 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167887698  227 GMVRCD------TAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEmLVGDTpfYAD 281
Cdd:cd14222   157 RTLRKNdrkkryTVVGNPYWMAPEMLNGKS----YDEKVDIFSFGIVLCE-IIGQV--YAD 210
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
59-291 2.16e-13

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: 73.01  E-value: 2.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   59 YKDTINKIrdLRMKAEDYEVVKVIGRGAFGEV-QLVRHKSTRKVYAMKLLSKFEMIKRSDSAFfwEERDIMAFANSPWVV 137
Cdd:cd07879     2 YREEVNKT--VWELPERYTSLKQVGSGAYGSVcSAIDKRTGEKVAIKKLSRPFQSEIFAKRAY--RELTLLKHMQHENVI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  138 QL---------FYAFQDdryLYMVMEYMPGgDLVNLMSNYDVPEKwARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDK 208
Cdd:cd07879    78 GLldvftsavsGDEFQD---FYLVMPYMQT-DLQKIMGHPLSEDK-VQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  209 SGHLKLADFGTCMKMNKEgmvrCDTAVGTPDYISPEVLKSQggdGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYS 288
Cdd:cd07879   153 DCELKILDFGLARHADAE----MTGYVVTRWYRAPEVILNW---MHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLT 225

                  ...
gi 167887698  289 KIM 291
Cdd:cd07879   226 QIL 228
PH_MRCK cd01243
MRCK (myotonic dystrophy-related Cdc42-binding kinase) pleckstrin homology (PH) domain; MRCK ...
1121-1198 2.33e-13

MRCK (myotonic dystrophy-related Cdc42-binding kinase) pleckstrin homology (PH) domain; MRCK is thought to be coincidence detector of signaling by Cdc42 and phosphoinositides. It has been shown to promote cytoskeletal reorganization, which affects many biological processes. There are 2 members of this family: MRCKalpha and MRCKbeta. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. The MRCK PH domain is responsible for its targeting to cell to cell junctions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269949  Cd Length: 135  Bit Score: 68.48  E-value: 2.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698 1121 IEGWLSVPNRGNIKRyGWKKQYVVVSSKKILFYNDEQDKEQS---NPSMVLDI-DKLFHVRPVTQGDVYRAETEEIPKIF 1196
Cdd:cd01243    14 YEGYVRVPKPGGVKK-GWQRQFAVVCDFKLFLFDISEDKASQpsqVASQVLDMrDEEFSVSSVLASDVIHANKKDIPCIF 92

                  ..
gi 167887698 1197 QI 1198
Cdd:cd01243    93 RV 94
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
426-698 2.77e-13

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 75.09  E-value: 2.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   426 ESLQKTIYKLEEQLHNEMQLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKEKMLLQHRINEYQRKAEQE 505
Cdd:TIGR02168  701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   506 NEKRRNVENEVSTLKDQLEDLKK--VSQNSQLAN---------EKLSQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKS 574
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREalDELRAELTLlneeaanlrERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   575 ISQLESLNRELQERNRILENSKSQTDKDYYQLQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVEGERKE 654
Cdd:TIGR02168  861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 167887698   655 AQDMLNhsEKEKNNLEIDLNY--KLKSLQQRLEQEVNEHKVTKARL 698
Cdd:TIGR02168  941 LQERLS--EEYSLTLEEAEALenKIEDDEEEARRRLKRLENKIKEL 984
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
79-272 3.91e-13

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: 71.46  E-value: 3.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   79 VKVIGRGAFGEVQLVRHK----STRKVYAMKLLSKFEMIKRSDsafFWEERDIMAFANSPWVVQ---LFYAfQDDRYLYM 151
Cdd:cd05081     9 ISQLGKGNFGSVELCRYDplgdNTGALVAVKQLQHSGPDQQRD---FQREIQILKALHSDFIVKyrgVSYG-PGRRSLRL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  152 VMEYMPGGDLVNLMsnydvPEKWARF-------YTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTC--MK 222
Cdd:cd05081    85 VMEYLPSGCLRDFL-----QRHRARLdasrlllYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAklLP 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 167887698  223 MNKEGMVRCDTAVGTPDYISPEVLksqgGDGYYGRECDWWSVGVFLYEML 272
Cdd:cd05081   160 LDKDYYVVREPGQSPIFWYAPESL----SDNIFSRQSDVWSFGVVLYELF 205
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
76-293 4.20e-13

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: 71.84  E-value: 4.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllskfemIKRSDSAFFWEERD-IMAF----------ANSPWVVQLFYAFQ 144
Cdd:cd14136    12 YHVVRKLGWGHFSTVWLCWDLQNKRFVALK-------VVKSAQHYTEAALDeIKLLkcvreadpkdPGREHVVQLLDDFK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  145 ----DDRYLYMVMEYMpGGDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHSM-GFIHRDVKPDNMLLD-KSGHLKLA 215
Cdd:cd14136    85 htgpNGTHVCMVFEVL-GPNLLKLIKRYNyrgIPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLLCiSKIEVKIA 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167887698  216 DFGTCMKMNKegmvRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSlvG-TYSKIMNH 293
Cdd:cd14136   164 DLGNACWTDK----HFTEDIQTRQYRSPEVILGAG----YGTPADIWSTACMAFELATGDYLFDPHS--GeDYSRDEDH 232
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
428-1104 4.35e-13

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 74.44  E-value: 4.35e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   428 LQKTIYKLEEQLHNEmqlkDEMEQKCRTSNIKLDKIMKELDEEGNQrrnLESTVSQIEKEKMLLQHRINEYQRKAEQENE 507
Cdd:pfam01576  101 MQQHIQDLEEQLDEE----EAARQKLQLEKVTTEAKIKKLEEDILL---LEDQNSKLSKERKLLEERISEFTSNLAEEEE 173
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   508 K-----------------------------------RRNVENEVSTLKDQLEDLKkvsqnsQLANEKLSQLQKQLEEAND 552
Cdd:pfam01576  174 KakslsklknkheamisdleerlkkeekgrqelekaKRKLEGESTDLQEQIAELQ------AQIAELRAQLAKKEEELQA 247
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   553 LL-RTESDTAVRlrkshTEMSKSISQLESLNRELQERnriLENSKSQTDKdyyqlqaiLEAERRDRGHDSEMIG----DL 627
Cdd:pfam01576  248 ALaRLEEETAQK-----NNALKKIRELEAQISELQED---LESERAARNK--------AEKQRRDLGEELEALKteleDT 311
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   628 QARITSLQE-------EVKHLKHNLEKvEGERKEAQ----------------DMLNHSEKEKNNLE----------IDLN 674
Cdd:pfam01576  312 LDTTAAQQElrskreqEVTELKKALEE-ETRSHEAQlqemrqkhtqaleeltEQLEQAKRNKANLEkakqalesenAELQ 390
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   675 YKLKSLQQRlEQEVnEHKVTKA-----RLTDKHQSIEEAKSVA---MCEMEKKLKEEREAREKAENRVVQIEKQCSMLDV 746
Cdd:pfam01576  391 AELRTLQQA-KQDS-EHKRKKLegqlqELQARLSESERQRAELaekLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLES 468
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   747 DLKQSQQKLEHLTGNK-------ERMEDEVKNLTLQLEQESNKRLLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKR 819
Cdd:pfam01576  469 QLQDTQELLQEETRQKlnlstrlRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKK 548
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   820 LLEFELAQLTKQYRGNEGQMRELQ---------------DQLEAEQYFSTLYKTQvkelkeeieeknrenlKKIQELQNE 884
Cdd:pfam01576  549 RLQRELEALTQQLEEKAAAYDKLEktknrlqqelddllvDLDHQRQLVSNLEKKQ----------------KKFDQMLAE 612
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   885 KETLATQLDLAETKAESE---------QLARGLLEEQyfELTQESKKAASRNRQEITD----KDHT---VSRLEEANSML 948
Cdd:pfam01576  613 EKAISARYAEERDRAEAEareketralSLARALEEAL--EAKEELERTNKQLRAEMEDlvssKDDVgknVHELERSKRAL 690
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   949 TKDIEILRRENEELTEKMKKAEEEYKLEKEEeISNLKAAFEKNINTERTL----KTQAVNKLAEIMNRKDfkiDRKKANT 1024
Cdd:pfam01576  691 EQQVEEMKTQLEELEDELQATEDAKLRLEVN-MQALKAQFERDLQARDEQgeekRRQLVKQVRELEAELE---DERKQRA 766
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  1025 QDLRKKekenRKLQLEL----------NQEREKFNQMVVKHQKELNDMQAQLVEECAHRNELQMQLASKESDIEQLRAKL 1094
Cdd:pfam01576  767 QAVAAK----KKLELDLkeleaqidaaNKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAEL 842
                          810
                   ....*....|
gi 167887698  1095 LDLSDSTSVA 1104
Cdd:pfam01576  843 LQLQEDLAAS 852
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
76-310 4.45e-13

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 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: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 71.98  E-value: 4.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAffweERDIMAF-----ANSPWVVQLFYAFQDDRYLY 150
Cdd:cd14229     2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQI----EVGILARlsnenADEFNFVRAYECFQHRNHTC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGG--DLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDN-MLLD---KSGHLKLADFGTCMKMN 224
Cdd:cd14229    78 LVFEMLEQNlyDFLKQNKFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENiMLVDpvrQPYRVKVIDFGSASHVS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  225 KegmVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGdTPFYADSLvgTYSKIMNHKNSLTFPDDND 304
Cdd:cd14229   158 K---TVCSTYLQSRYYRAPEIILGLP----FCEAIDMWSLGCVIAELFLG-WPLYPGAL--EYDQIRYISQTQGLPGEQL 227

                  ....*.
gi 167887698  305 ISKEAK 310
Cdd:cd14229   228 LNVGTK 233
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
447-772 4.52e-13

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 74.32  E-value: 4.52e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   447 DEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKEKMLLQHRINEYQRKAEQENEKRRNVENEVSTLKDQLEDL 526
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   527 --KKVSQNSQL--ANEKLSQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSISQLESLNRELQERNRILENSKSQTDKD 602
Cdd:TIGR02168  760 eaEIEELEERLeeAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   603 YYQLQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVEGERKEAQDMLNHSEKEKNNLE---IDLNYKLKS 679
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELEskrSELRRELEE 919
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   680 LQQRLEQEVNEHKVTKARLTDKHQSIEEAKSVAMCEMEKKLKEEREAREKAENRVVQIEKQCSML-DVDL------KQSQ 752
Cdd:TIGR02168  920 LREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgPVNLaaieeyEELK 999
                          330       340
                   ....*....|....*....|
gi 167887698   753 QKLEHLTGNKERMEDEVKNL 772
Cdd:TIGR02168 1000 ERYDFLTAQKEDLTEAKETL 1019
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
74-278 5.00e-13

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: 70.69  E-value: 5.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVyAMKLLSKFEMikrSDSAFFwEERDIMAFANSPWVVQLfYAFQDDRYLYMVM 153
Cdd:cd05067     7 ETLKLVERLGAGQFGEVWMGYYNGHTKV-AIKSLKQGSM---SPDAFL-AEANLMKQLQHQRLVRL-YAVVTQEPIYIIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLM---SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVR 230
Cdd:cd05067    81 EYMENGSLVDFLktpSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 167887698  231 CDTAVGTPDYISPEVLKSqggdGYYGRECDWWSVGVFLYEMLV-GDTPF 278
Cdd:cd05067   161 REGAKFPIKWTAPEAINY----GTFTIKSDVWSFGILLTEIVThGRIPY 205
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
70-271 5.14e-13

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: 70.46  E-value: 5.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   70 RMKAEDYEVVKVIGRGAFGEVQLVRHKStRKVyAMKllskfeMIKRSDSAF--FWEERDIMAFANSPWVVQLFYAFQDDR 147
Cdd:cd05039     2 AINKKDLKLGELIGKGEFGDVMLGDYRG-QKV-AVK------CLKDDSTAAqaFLAEASVMTTLRHPNLVQLLGVVLEGN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  148 YLYMVMEYMPGGDLVNLMS-------NYDVPEKWARfytaEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGtc 220
Cdd:cd05039    74 GLYIVTEYMAKGSLVDYLRsrgraviTRKDQLGFAL----DVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFG-- 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 167887698  221 mkMNKEGMVRCDTAVGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLYEM 271
Cdd:cd05039   148 --LAKEASSNQDGGKLPIKWTAPEALR----EKKFSTKSDVWSFGILLWEI 192
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
76-291 5.59e-13

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: 70.76  E-value: 5.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllskfeMIKRSdSAFF---WEERDIMAF------ANSPWVVQLFYAFQDD 146
Cdd:cd14133     1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALK------IIKNN-KDYLdqsLDEIRLLELlnkkdkADKYHIVRLKDVFYFK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  147 RYLYMVMEyMPGGDLVNLmSNYD----VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL---DKSGhLKLADFGT 219
Cdd:cd14133    74 NHLCIVFE-LLSQNLYEF-LKQNkfqyLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLasySRCQ-IKIIDFGS 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167887698  220 CMKMNKegmvRCDTAVGTPDYISPEVLKsqggdGY-YGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIM 291
Cdd:cd14133   151 SCFLTQ----RLYSYIQSRYYRAPEVIL-----GLpYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARII 214
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
79-278 5.96e-13

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: 70.55  E-value: 5.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   79 VKVIGRGAFGEVQLVRHKSTRKVyAMKLLSKFEMikrSDSAFFwEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPG 158
Cdd:cd05059     9 LKELGSGQFGVVHLGKWRGKIDV-AIKMIKEGSM---SEDDFI-EEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMAN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  159 GDLVNLMSnydvpEKWARFYTA-------EVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFgtcmkmnkeGMVR- 230
Cdd:cd05059    84 GCLLNYLR-----ERRGKFQTEqllemckDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDF---------GLARy 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  231 -------CDTAVGTP-DYISPEVLKSqggdGYYGRECDWWSVGVFLYEMLV-GDTPF 278
Cdd:cd05059   150 vlddeytSSVGTKFPvKWSPPEVFMY----SKFSSKSDVWSFGVLMWEVFSeGKMPY 202
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
434-709 6.16e-13

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 73.95  E-value: 6.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   434 KLEEQLHNEMQLKDEMEqkcrTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKEKMLLQHRINEYQRKAEQENEKRRNVE 513
Cdd:TIGR02169  675 ELQRLRERLEGLKRELS----SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   514 NEVSTLKDQLEDLKKVSQNSQlanEKLSQLQKQLEEANDLLRTESDTAVR--LRKSHTEMSKSISQLESLNRELQER--N 589
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELE---EDLHKLEEALNDLEARLSHSRIPEIQaeLSKLEEEVSRIEARLREIEQKLNRLtlE 827
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   590 RILENSKSQTDKDYYQLQAILEAERRDRGHDSEM-IGDLQARITSLQEEVKHLKHNLEKVEGERKEAQDMLNHSEKEKNN 668
Cdd:TIGR02169  828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGkKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 167887698   669 LEIDLnyklkslqQRLEQEVNEHKVTKARLTDKHQSIEEAK 709
Cdd:TIGR02169  908 LEAQI--------EKKRKRLSELKAKLEALEEELSEIEDPK 940
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
136-278 6.35e-13

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: 70.25  E-value: 6.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  136 VVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD--KSGHLK 213
Cdd:cd14112    62 VQRLIAAFKPSNFAYLVMEKLQEDVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQsvRSWQVK 141
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  214 LADFGTCMKMNKEGMVrcdTAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd14112   142 LVDFGRAQKVSKLGKV---PVDGDTDWASPEFHN---PETPITVQSDIWGLGVLTFCLLSGFHPF 200
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
79-342 8.01e-13

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: 71.23  E-value: 8.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   79 VKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPG 158
Cdd:cd06635    30 LREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYCLG 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  159 gDLVNLMSNYDVP--EKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKegmvrCDTAVG 236
Cdd:cd06635   110 -SASDLLEVHKKPlqEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASP-----ANSFVG 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  237 TPDYISPEVLKSQgGDGYYGRECDWWSVGVFLYEMLVGDTP-FYADSLVGTYSKIMNHKNSLtfpDDNDISKEAKNLICA 315
Cdd:cd06635   184 TPYWMAPEVILAM-DEGQYDGKVDVWSLGITCIELAERKPPlFNMNAMSALYHIAQNESPTL---QSNEWSDYFRNFVDS 259
                         250       260
                  ....*....|....*....|....*..
gi 167887698  316 FLtdREVRLGRNGVEEIKRHLFFKNDQ 342
Cdd:cd06635   260 CL--QKIPQDRPTSEELLKHMFVLRER 284
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
74-290 8.35e-13

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 70.62  E-value: 8.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllsKFEMIKRSDSAFFWEERDI-----MAFANspwVVQLFYAFQDDRY 148
Cdd:PLN00009    2 DQYEKVEKIGEGTYGVVYKARDRVTNETIALK---KIRLEQEDEGVPSTAIREIsllkeMQHGN---IVRLQDVVHSEKR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 LYMVMEYMpggDLvNLMSNYDVPEKWAR------FYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH-LKLADFGTCM 221
Cdd:PLN00009   76 LYLVFEYL---DL-DLKKHMDSSPDFAKnprlikTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNaLKLADFGLAR 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  222 KMNKEgmVRCDT-AVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKI 290
Cdd:PLN00009  152 AFGIP--VRTFThEVVTLWYRAPEILL---GSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKI 216
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
76-327 1.00e-12

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: 70.90  E-value: 1.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRK-----------VYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVvqlFYAFQ 144
Cdd:cd07857     2 YELIKELGQGAYGIVCSARNAETSEeetvaikkitnVFSKKILAKRALRELKLLRHFRGHKNITCLYDMDIV---FPGNF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  145 DDRYLYM-VMEYmpggDLVNLM-SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMK 222
Cdd:cd07857    79 NELYLYEeLMEA----DLHQIIrSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  223 MN---KEGMVRCDTAVGTPDYISPEVLKSQGGdgyYGRECDWWSVGVFLYEMLvGDTPFYADSlvgTYSKIMNH-KNSLT 298
Cdd:cd07857   155 FSenpGENAGFMTEYVATRWYRAPEIMLSFQS---YTKAIDVWSVGCILAELL-GRKPVFKGK---DYVDQLNQiLQVLG 227
                         250       260       270
                  ....*....|....*....|....*....|...
gi 167887698  299 FPDDNDISK----EAKNLICAFLTDREVRLGRN 327
Cdd:cd07857   228 TPDEETLSRigspKAQNYIRSLPNIPKKPFESI 260
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
76-278 1.38e-12

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: 70.67  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEmiKRSDSAFFweERDIMAF------ANSPWVVQLFYAFQDDRYL 149
Cdd:cd14134    14 YKILRLLGEGTFGKVLECWDRKRKRYVAVKIIRNVE--KYREAAKI--EIDVLETlaekdpNGKSHCVQLRDWFDYRGHM 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 YMVMEYMpGgdlvnlMSNYD---------VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD------------- 207
Cdd:cd14134    90 CIVFELL-G------PSLYDflkknnygpFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVdsdyvkvynpkkk 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  208 ------KSGHLKLADFGTCmkmnkegmvrCD------TAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGD 275
Cdd:cd14134   163 rqirvpKSTDIKLIDFGSA----------TFddeyhsSIVSTRHYRAPEVILGLG----WSYPCDVWSIGCILVELYTGE 228

                  ...
gi 167887698  276 TPF 278
Cdd:cd14134   229 LLF 231
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
79-272 1.46e-12

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: 69.72  E-value: 1.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   79 VKVIGRGAFGEVQLVRHK----STRKVYAMKLLSKfeMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDD--RYLYMV 152
Cdd:cd05038     9 IKQLGEGHFGSVELCRYDplgdNTGEQVAVKSLQP--SGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESPgrRSLRLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGGDLVNLMSNYDVPEKWARF--YTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG--TCMKMNKEGM 228
Cdd:cd05038    87 MEYLPSGSLRDYLQRHRDQIDLKRLllFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGlaKVLPEDKEYY 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 167887698  229 VrcdtaVGTPD-----YISPEVLKsqggDGYYGRECDWWSVGVFLYEML 272
Cdd:cd05038   167 Y-----VKEPGespifWYAPECLR----ESRFSSASDVWSFGVTLYELF 206
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
412-1058 1.66e-12

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 71.98  E-value: 1.66e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   412 NDNRTSSNADKSLQESLQK---TIYKLEEQLHNEMQLKDEMEQKCRTSNIKLDK-------IMKELDEEGNQRRNLESTV 481
Cdd:TIGR04523   47 NELKNKEKELKNLDKNLNKdeeKINNSNNKIKILEQQIKDLNDKLKKNKDKINKlnsdlskINSEIKNDKEQKNKLEVEL 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   482 SQIEKEK--------------MLLQHRINEYQRKAEQENEKRRNVENEVSTLKDQLEDLKKVSQNSQLANEKLSQLQKQL 547
Cdd:TIGR04523  127 NKLEKQKkenkknidkflteiKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNL 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   548 EEANDLLRTESDTAVRLRKSHTEMSKSISQLES----LNRELQERNRILENSKSQTDKDYYQLQA-ILEAERRDRGHD-- 620
Cdd:TIGR04523  207 KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQeineKTTEISNTQTQLNQLKDEQNKIKKQLSEkQKELEQNNKKIKel 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   621 SEMIGDLQARITSL-----QEEVKHLKHNLEKVEGERKEAQDMLNHSEKEKNnleiDLNYKLKSLQQRLEQEVNEHKVTK 695
Cdd:TIGR04523  287 EKQLNQLKSEISDLnnqkeQDWNKELKSELKNQEKKLEEIQNQISQNNKIIS----QLNEQISQLKKELTNSESENSEKQ 362
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   696 ARLTDKHQSIEEAKSvamcEMEKKLKEEREAREKAENRVVQIEKQcsmlDVDLKQSQQKLEHLTGNKERMEDEVKNLTLQ 775
Cdd:TIGR04523  363 RELEEKQNEIEKLKK----ENQSYKQEIKNLESQINDLESKIQNQ----EKLNQQKDEQIKKLQQEKELLEKEIERLKET 434
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   776 LEQESNKRLLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMRELQDQleaeqyfstl 855
Cdd:TIGR04523  435 IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE---------- 504
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   856 yKTQVKELKEEIEEKNRENLKKIQELQNEKETLATQLDLAETKaeseqlarglLEEQYFELTQES-KKAASRNRQEITDK 934
Cdd:TIGR04523  505 -KKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE----------LNKDDFELKKENlEKEIDEKNKEIEEL 573
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   935 DHTVSRLEEANSMLTKDIEILRRENEELTEKMkKAEEEYKLEKEEEISNLKAAFEKNINTERTLKTqAVNKLAEIMNRKD 1014
Cdd:TIGR04523  574 KQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI-EEKEKKISSLEKELEKAKKENEKLSSIIKNIKS-KKNKLKQEVKQIK 651
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....
gi 167887698  1015 FKIDRKKANTQDLRKKEKENRKLQLELNQEREKFNQMVVKHQKE 1058
Cdd:TIGR04523  652 ETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKK 695
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
81-290 1.66e-12

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie 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: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 69.30  E-value: 1.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   81 VIGRGAFGEV--QLVRHKSTRKVYAMKLLSKFEmiKRSDSAFFWEERDIMA-FANSPWVVQLFYAFQDDRYLYMVMEYMP 157
Cdd:cd05047     2 VIGEGNFGQVlkARIKKDGLRMDAAIKRMKEYA--SKDDHRDFAGELEVLCkLGHHPNIINLLGACEHRGYLYLAIEYAP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  158 GGDLVNLMSNYDVPEKWARF-----------------YTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGtc 220
Cdd:cd05047    80 HGNLLDFLRKSRVLETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG-- 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167887698  221 MKMNKEGMVRCDTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEML-VGDTPFYADSLVGTYSKI 290
Cdd:cd05047   158 LSRGQEVYVKKTMGRLPVRWMAIESLNYS----VYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEKL 224
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
80-278 2.10e-12

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: 68.79  E-value: 2.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVyAMKLLSKFEMikrSDSAFFwEERDIMAFANSPWVVQLfYAFQDDRYLYMVMEYMPGG 159
Cdd:cd14203     1 VKLGQGCFGEVWMGTWNGTTKV-AIKTLKPGTM---SPEAFL-EEAQIMKKLRHDKLVQL-YAVVSEEPIYIVTEFMSKG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DLVNLMSNYDvpEKWARF-----YTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTA 234
Cdd:cd14203    75 SLLDFLKDGE--GKYLKLpqlvdMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGA 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 167887698  235 VGTPDYISPEVlksqggdGYYGR---ECDWWSVGVFLYEMLV-GDTPF 278
Cdd:cd14203   153 KFPIKWTAPEA-------ALYGRftiKSDVWSFGILLTELVTkGRVPY 193
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
76-279 2.24e-12

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: 69.38  E-value: 2.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMK---LLSKFEMIkrSDSAFfwEERDIMAFANSPWVVQLFYAFQDDRYLYMV 152
Cdd:cd07839     2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKrvrLDDDDEGV--PSSAL--REICLLKELKHKNIVRLYDVLHSDKKLTLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMpGGDLVNLMS--NYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMnkeGM-V 229
Cdd:cd07839    78 FEYC-DQDLKKYFDscNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAF---GIpV 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 167887698  230 RCDTA-VGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFY 279
Cdd:cd07839   154 RCYSAeVVTLWYRPPDVLF---GAKLYSTSIDMWSAGCIFAELANAGRPLF 201
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
147-278 2.72e-12

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 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: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 69.81  E-value: 2.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  147 RYLYMVMEYMPGgDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH-LKLADFGTCMKMN- 224
Cdd:cd07854    89 NSVYIVQEYMET-DLANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLvLKIGDFGLARIVDp 167
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887698  225 --------KEGMVrcdtavgTPDYISPEVLKSQggdGYYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd07854   168 hyshkgylSEGLV-------TKWYRSPRLLLSP---NNYTKAIDMWAAGCIFAEMLTGKPLF 219
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
82-278 3.87e-12

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: 68.03  E-value: 3.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKllSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd05084     4 IGRGNFGEVFSGRLRADNTPVAVK--SCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNydvpeKWARFYTAEVV-LALDAIHSMGF------IHRDVKPDNMLLDKSGHLKLADFGtcmkMNKEGMVRCDTA 234
Cdd:cd05084    82 LTFLRT-----EGPRLKVKELIrMVENAAAGMEYleskhcIHRDLAARNCLVTEKNVLKISDFG----MSREEEDGVYAA 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 167887698  235 VGTPDYI-----SPEVLKSqggdGYYGRECDWWSVGVFLYEML-VGDTPF 278
Cdd:cd05084   153 TGGMKQIpvkwtAPEALNY----GRYSSESDVWSFGILLWETFsLGAVPY 198
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
74-290 3.91e-12

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: 69.14  E-value: 3.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKST-RKVYAMKLLSKFE---MIKRSdsaffWEERDIMAFANSPWVVQL---FYAFQDD 146
Cdd:cd07856    10 TRYSDLQPVGMGAFGLVCSARDQLTgQNVAVKKIMKPFStpvLAKRT-----YRELKLLKHLRHENIISLsdiFISPLED 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  147 ryLYMVMEYMpGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmKMNKE 226
Cdd:cd07856    85 --IYFVTELL-GTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLA-RIQDP 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167887698  227 GMVrcdTAVGTPDYISPEVLKSQGGdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKI 290
Cdd:cd07856   161 QMT---GYVSTRYYRAPEIMLTWQK---YDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSII 218
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
1229-1275 4.33e-12

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 62.10  E-value: 4.33e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 167887698   1229 HEFIPTLYHFPANCDACAKPLWHVFKPppALECRRCHVKCHRDHLDK 1275
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGSFKQ--GLRCSECKVKCHKKCADK 45
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
147-275 6.73e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 69.72  E-value: 6.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  147 RYLYMVMEYMPGGDLvnlmSNYDVPEKW-ARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNK 225
Cdd:PHA03210  244 KYDFDLYSFMYDEAF----DWKDRPLLKqTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFGTAMPFEK 319
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 167887698  226 EGMVRCDTAVGTPDYISPEVLksqGGDGYygreC---DWWSVGVFLYEMLVGD 275
Cdd:PHA03210  320 EREAFDYGWVGTVATNSPEIL---AGDGY----CeitDIWSCGLILLDMLSHD 365
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
80-278 7.85e-12

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: 66.95  E-value: 7.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEV--QLVRHKSTRKVYAMKllskfEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMP 157
Cdd:cd05085     2 ELLGKGNFGEVykGTLKDKTPVAVKTCK-----EDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  158 GGDLVNLMSnydvpEKWARFYTAEVV-LALDAIHSMGF------IHRDVKPDNMLLDKSGHLKLADFGtcMKMNKEGMVR 230
Cdd:cd05085    77 GGDFLSFLR-----KKKDELKTKQLVkFSLDAAAGMAYleskncIHRDLAARNCLVGENNALKISDFG--MSRQEDDGVY 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 167887698  231 CDTAVGT-P-DYISPEVLKSqggdGYYGRECDWWSVGVFLYEML-VGDTPF 278
Cdd:cd05085   150 SSSGLKQiPiKWTAPEALNY----GRYSSESDVWSFGILLWETFsLGVCPY 196
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
74-292 8.29e-12

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: 67.75  E-value: 8.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRH-KSTRKVYAMK---LLSKFEMIKRSDSAFFWEERDIMAFANsPWVVQLF---YAFQDD 146
Cdd:cd07862     1 QQYECVAEIGEGAYGKVFKARDlKNGGRFVALKrvrVQTGEEGMPLSTIREVAVLRHLETFEH-PNVVRLFdvcTVSRTD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  147 R--YLYMVMEYMpGGDLVNLMSNY---DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCM 221
Cdd:cd07862    80 RetKLTLVFEHV-DQDLTTYLDKVpepGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLAR 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167887698  222 KMNKEgmVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMN 292
Cdd:cd07862   159 IYSFQ--MALTSVVVTLWYRAPEVLLQSS----YATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILD 223
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
82-272 9.98e-12

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: 66.73  E-value: 9.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSkfemiKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALKMNT-----LSSNRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNyDVPEKWarfyTAEVVLALDA------IHSMGFIHRDVKPDNMLL--DKSGHLKL-ADFGTCMKMNKEGMVRCD 232
Cdd:cd14155    76 EQLLDS-NEPLSW----TVRVKLALDIarglsyLHSKGIFHRDLTSKNCLIkrDENGYTAVvGDFGLAEKIPDYSDGKEK 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 167887698  233 TA-VGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEML 272
Cdd:cd14155   151 LAvVGSPYWMAPEVLRGE----PYNEKADVFSYGIILCEII 187
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
79-278 1.09e-11

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) 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. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk 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: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 66.81  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   79 VKVIGRGAFGEVQLVRHKSTRKVyAMKLLSKFEMIKRSdsafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPG 158
Cdd:cd05114     9 MKELGSGLFGVVRLGKWRAQYKV-AIKAIREGAMSEED----FIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMEN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  159 GDLVNLMSnydvpEKWARFyTAEVVLAL--DAIHSM------GFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVR 230
Cdd:cd05114    84 GCLLNYLR-----QRRGKL-SRDMLLSMcqDVCEGMeylernNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQYTS 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 167887698  231 CDTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLV-GDTPF 278
Cdd:cd05114   158 SSGAKFPVKWSPPEVFNYS----KFSSKSDVWSFGVLMWEVFTeGKMPF 202
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
80-282 1.19e-11

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, 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. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros 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: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 66.67  E-value: 1.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEV-------QLVRHKSTRKVyAMKLLSKFEMIkrSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMV 152
Cdd:cd05044     1 KFLGSGAFGEVfegtakdILGDGSGETKV-AVKTLRKGATD--QEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGGDLVNLMSNydvpEKWARFYTAEVVL------ALDA------IHSMGFIHRDVKPDNMLLDKSGH----LKLAD 216
Cdd:cd05044    78 LELMEGGDLLSYLRA----ARPTAFTPPLLTLkdllsiCVDVakgcvyLEDMHFVHRDLAARNCLVSSKDYrervVKIGD 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  217 FGTCMKMNK--------EGM--VRcdtavgtpdYISPEVLKsqggDGYYGRECDWWSVGVFLYEML-VGDTPFYADS 282
Cdd:cd05044   154 FGLARDIYKndyyrkegEGLlpVR---------WMAPESLV----DGVFTTQSDVWAFGVLMWEILtLGQQPYPARN 217
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
1229-1275 1.23e-11

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


Pssm-ID: 410341  Cd Length: 50  Bit Score: 60.61  E-value: 1.23e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 167887698 1229 HEFIPTLYHFPANCDACAKPLWHVFKppPALECRRCHVKCHRDHLDK 1275
Cdd:cd00029     1 HRFVPTTFSSPTFCDVCGKLIWGLFK--QGLKCSDCGLVCHKKCLDK 45
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
501-1061 1.36e-11

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 69.37  E-value: 1.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   501 KAEQENEKRRNvENEVSTLKDQLEDLKKVSQNSQLANEKLS-QLQKQLEEANDLLRTESDT--------------AVRLR 565
Cdd:pfam05483   94 KVSIEAELKQK-ENKLQENRKIIEAQRKAIQELQFENEKVSlKLEEEIQENKDLIKENNATrhlcnllketcarsAEKTK 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   566 KSHTEMSKSISQLESLNRELQERNRILENSKSQTD-----------KDYYQLQAILEAERRDRGHDSEMIGDLQARITSL 634
Cdd:pfam05483  173 KYEYEREETRQVYMDLNNNIEKMILAFEELRVQAEnarlemhfklkEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEK 252
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   635 QEEVKHLKHNLEkvegerkEAQDMLNHSEkEKNNLEIDLNYKLKSLQQRLEQEVNEHKVTKARLTDKHQSIEEAKSVA-- 712
Cdd:pfam05483  253 ENKMKDLTFLLE-------ESRDKANQLE-EKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIAtk 324
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   713 -MC----EMEKKLKEEREAREKAENRVVQIEKQCSMLDVDLKQSQQKLEhltgnkeRMEDEVKNLTLQLEQES------- 780
Cdd:pfam05483  325 tICqlteEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLE-------KNEDQLKIITMELQKKSseleemt 397
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   781 ----NKRLLLQnELKTQAFEADNLKGLEKQMK----------QEINTLLEAKRL----LEFELAQLTKQYRGNEGQMREL 842
Cdd:pfam05483  398 kfknNKEVELE-ELKKILAEDEKLLDEKKQFEkiaeelkgkeQELIFLLQAREKeihdLEIQLTAIKTSEEHYLKEVEDL 476
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   843 QDQLEAEQYFSTLYKTQVKELKEEIEEKNRENLKKIQELQNEKEtlatqlDLAETKAESEQLARGL--LEEQYFELTQES 920
Cdd:pfam05483  477 KTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQE------DIINCKKQEERMLKQIenLEEKEMNLRDEL 550
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   921 KKAASRNRQEitdKDHTVSRLEEAnsmltkdieilrRENEELTEKMKKAEEEYKLEKEEEISNLKAAFEKNintertlkt 1000
Cdd:pfam05483  551 ESVREEFIQK---GDEVKCKLDKS------------EENARSIEYEVLKKEKQMKILENKCNNLKKQIENK--------- 606
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887698  1001 qavNKLAEIMNRKDFKIDRK-KANTQDLRKKEKENRKLQLELNQEREKFNQMVVKHQKELND 1061
Cdd:pfam05483  607 ---NKNIEELHQENKALKKKgSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIED 665
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
497-1100 1.60e-11

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 69.23  E-value: 1.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   497 EYQRKAEQENEKRRNVENEVSTLKDQLEDLKKVSQNSQLANEKLSQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSIS 576
Cdd:TIGR00618  202 RSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEE 281
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   577 QLESLNRELQeRNRILENSK--SQTDKDYYQLQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNL---EKVEGE 651
Cdd:TIGR00618  282 TQERINRARK-AAPLAAHIKavTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHsqeIHIRDA 360
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   652 RKEAQDMLNHSEKEK----------NNLEIDLNyKLKSLQQRLEQEVNEhkVTKARLTDKHQSIEEAKSVAMCEMEKKLK 721
Cdd:TIGR00618  361 HEVATSIREISCQQHtltqhihtlqQQKTTLTQ-KLQSLCKELDILQRE--QATIDTRTSAFRDLQGQLAHAKKQQELQQ 437
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   722 EEREAREKAENRVVQIEKQCSMLDVDLKQSQQKLEHLTGNKERM---EDEVKNLTLQ--LEQESNKRLLLQN--ELKTQA 794
Cdd:TIGR00618  438 RYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIhlqETRKKAVVLArlLELQEEPCPLCGSciHPNPAR 517
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   795 FEADNLKGLEKQMKQEINT---LLEAKRLLEFELAQLTKQYRGNEGQMRELQDQLEAEQYFSTLYKTQ-------VKELK 864
Cdd:TIGR00618  518 QDIDNPGPLTRRMQRGEQTyaqLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDipnlqniTVRLQ 597
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   865 EEIEEKNRENLKKIQELQNEKETLATQLDLAE------TKAESEQLARGLLEEQYFELTQES-KKAASRNRQEITDKDHT 937
Cdd:TIGR00618  598 DLTEKLSEAEDMLACEQHALLRKLQPEQDLQDvrlhlqQCSQELALKLTALHALQLTLTQERvREHALSIRVLPKELLAS 677
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   938 VSRLEEA----NSMLTKDIEILRRENEELTEkmKKAEEEYKLEKEEEISNLKAAFEKNINTERTLKTQAVNKLaeimnRK 1013
Cdd:TIGR00618  678 RQLALQKmqseKEQLTYWKEMLAQCQTLLRE--LETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKEL-----MH 750
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  1014 DFKIDRKKANTQDLRKKEKENRKLQL-----ELNQEREKFNQMVVKHQKELNDMQAQLVEECAH-RNELQMQLASKESDI 1087
Cdd:TIGR00618  751 QARTVLKARTEAHFNNNEEVTAALQTgaelsHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSdEDILNLQCETLVQEE 830
                          650
                   ....*....|...
gi 167887698  1088 EQLRAKLLDLSDS 1100
Cdd:TIGR00618  831 EQFLSRLEEKSAT 843
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
79-279 1.94e-11

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: 66.58  E-value: 1.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   79 VKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPG 158
Cdd:cd06634    20 LREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEYCLG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  159 G--DLVNLMSNyDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKegmvrCDTAVG 236
Cdd:cd06634   100 SasDLLEVHKK-PLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMAP-----ANSFVG 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 167887698  237 TPDYISPEVLKSQgGDGYYGRECDWWSVGVFLYEMLVGDTPFY 279
Cdd:cd06634   174 TPYWMAPEVILAM-DEGQYDGKVDVWSLGITCIELAERKPPLF 215
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
136-300 1.96e-11

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: 66.35  E-value: 1.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  136 VVQLFYAFQDDRYLYMVMEYMPGgDLVNLMSNYDVP----EKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH 211
Cdd:cd07836    60 IVRLHDVIHTENKLMLVFEYMDK-DLKKYMDTHGVRgaldPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGE 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  212 LKLADFGTC----MKMNKegmvrCDTAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFY----ADSL 283
Cdd:cd07836   139 LKLADFGLArafgIPVNT-----FSNEVVTLWYRAPDVLL---GSRTYSTSIDIWSVGCIMAEMITGRPLFPgtnnEDQL 210
                         170
                  ....*....|....*..
gi 167887698  284 VGTYsKIMNHKNSLTFP 300
Cdd:cd07836   211 LKIF-RIMGTPTESTWP 226
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
75-284 2.01e-11

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK 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: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 67.46  E-value: 2.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRH-KSTRKVYAMKLLSKFEMIKRSDSAFfwEERDIMAFANSPWVVQLFYAFQDD-----RY 148
Cdd:cd07853     1 DVEPDRPIGYGAFGVVWSVTDpRDGKRVALKKMPNVFQNLVSCKRVF--RELKMLCFFKHDNVLSALDILQPPhidpfEE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 LYMVMEYMPGgDLVNLM-SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEG 227
Cdd:cd07853    79 IYVVTELMQS-DLHKIIvSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEEPDE 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  228 MVRCDTAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLV 284
Cdd:cd07853   158 SKHMTQEVVTQYYRAPEILM---GSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPI 211
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
39-303 2.37e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 67.18  E-value: 2.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   39 YDLDFPALRKNKNIDNFLSRYKDTINKIRDLRMKaedYEVVKVIGRGAFGEVQL-VRH-KSTRKVYAMKLLSKFEMIKRs 116
Cdd:PHA03207   60 YDADEESLSPQTDVCQEPCETTSSSDPASVVRMQ---YNILSSLTPGSEGEVFVcTKHgDEQRKKVIVKAVTGGKTPGR- 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  117 dsaffweERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGgDL---VNLMSNydVPEKWARFYTAEVVLALDAIHSMG 193
Cdd:PHA03207  136 -------EIDILKTISHRAIINLIHAYRWKSTVCMVMPKYKC-DLftyVDRSGP--LPLEQAITIQRRLLEALAYLHGRG 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  194 FIHRDVKPDNMLLDKSGHLKLADFGTCMKMNK-EGMVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEML 272
Cdd:PHA03207  206 IIHRDVKTENIFLDEPENAVLGDFGAACKLDAhPDTPQCYGWSGTLETNSPELLALDP----YCAKTDIWSAGLVLFEMS 281
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 167887698  273 VGDTPFYADSLVGTYSKIMN-----HKNSLTFPDDN 303
Cdd:PHA03207  282 VKNVTLFGKQVKSSSSQLRSiircmQVHPLEFPQNG 317
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
80-292 2.54e-11

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 66.71  E-value: 2.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVYAMKllsKFEMIKRSDSAFFWE--------------ERDIMAFANSPWVVQLFYAFQD 145
Cdd:PTZ00024   15 AHLGEGTYGKVEKAYDTLTGKIVAIK---KVKIIEISNDVTKDRqlvgmcgihfttlrELKIMNEIKHENIMGLVDVYVE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  146 DRYLYMVMEYMpGGDLVNLM-SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMN 224
Cdd:PTZ00024   92 GDFINLVMDIM-ASDLKKVVdRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARRYG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  225 KEGMVRCDTAVGTPD-------------YISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIM 291
Cdd:PTZ00024  171 YPPYSDTLSKDETMQrreemtskvvtlwYRAPELLM---GAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGRIF 247

                  .
gi 167887698  292 N 292
Cdd:PTZ00024  248 E 248
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
76-279 2.75e-11

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 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: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 66.65  E-value: 2.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAffweERDIMA-----FANSPWVVQLFYAFQDDRYLY 150
Cdd:cd14227    17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQI----EVSILArlsteSADDYNFVRAYECFQHKNHTC 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGG--DLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDN-MLLDKSGH---LKLADFGTCMKMN 224
Cdd:cd14227    93 LVFEMLEQNlyDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENiMLVDPSRQpyrVKVIDFGSASHVS 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  225 KegmVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGdTPFY 279
Cdd:cd14227   173 K---AVCSTYLQSRYYRAPEIILGLP----FCEAIDMWSLGCVIAELFLG-WPLY 219
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
82-278 3.17e-11

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: 65.59  E-value: 3.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEV-QLVRHKSTrkVYAMKLLSKfEMIKRSDSAFfWEERDIMAFANSPWVVQL--FYAFQDDRYLymVMEYMPG 158
Cdd:cd14664     1 IGRGGAGTVyKGVMPNGT--LVAVKRLKG-EGTQGGDHGF-QAEIQTLGMIRHRNIVRLrgYCSNPTTNLL--VYEYMPN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  159 GDLVNLM---SNYDVPEKWARFYTaevvLALDAIHSMGF---------IHRDVKPDNMLLDKSGHLKLADFGTCMKMNKE 226
Cdd:cd14664    75 GSLGELLhsrPESQPPLDWETRQR----IALGSARGLAYlhhdcspliIHRDVKSNNILLDEEFEAHVADFGLAKLMDDK 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 167887698  227 GmVRCDTAV-GTPDYISPEVLKSqggdGYYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd14664   151 D-SHVMSSVaGSYGYIAPEYAYT----GKVSEKSDVYSYGVVLLELITGKRPF 198
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
76-279 4.01e-11

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 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: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 66.27  E-value: 4.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSD-------SAFFWEERDIMAFANSpwvvqlFYAFQDDRY 148
Cdd:cd14228    17 YEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGqievsilSRLSSENADEYNFVRS------YECFQHKNH 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 LYMVMEYMPGG--DLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL----DKSGHLKLADFGTCMK 222
Cdd:cd14228    91 TCLVFEMLEQNlyDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFGSASH 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  223 MNKegmVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGdTPFY 279
Cdd:cd14228   171 VSK---AVCSTYLQSRYYRAPEIILGLP----FCEAIDMWSLGCVIAELFLG-WPLY 219
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
71-278 4.08e-11

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: 64.90  E-value: 4.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   71 MKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVyAMKLLSKFEMikrSDSAFFwEERDIMAFANSPWVVQLFYAFQDDRYLY 150
Cdd:cd05113     1 IDPKDLTFLKELGTGQFGVVKYGKWRGQYDV-AIKMIKEGSM---SEDEFI-EEAKVMMNLSHEKLVQLYGVCTKQRPIF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGGDLVNLMSnydvpEKWARFYTAE-------VVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKM 223
Cdd:cd05113    76 IITEYMANGCLLNYLR-----EMRKRFQTQQllemckdVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYV 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 167887698  224 NKEGMVrcdTAVGTP---DYISPEVLKSQGgdgyYGRECDWWSVGVFLYEML-VGDTPF 278
Cdd:cd05113   151 LDDEYT---SSVGSKfpvRWSPPEVLMYSK----FSSKSDVWAFGVLMWEVYsLGKMPY 202
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
81-278 4.29e-11

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: 65.33  E-value: 4.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   81 VIGRGAFGEVQLVRHKStrKVYAMKLLSK----------FEMIKRSDSA--------FFWEERDIMAFANSPWVVQLFYA 142
Cdd:cd14000     1 LLGDGGFGSVYRASYKG--EPVAVKIFNKhtssnfanvpADTMLRHLRAtdamknfrLLRQELTVLSHLHHPSIVYLLGI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  143 FQDDRYLymVMEYMPGGDLVNLMSNYDVPE-KWARFYTAEVVL----ALDAIHSMGFIHRDVKPDNMLL-----DKSGHL 212
Cdd:cd14000    79 GIHPLML--VLELAPLGSLDHLLQQDSRSFaSLGRTLQQRIALqvadGLRYLHSAMIIYRDLKSHNVLVwtlypNSAIII 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167887698  213 KLADFGTCMKMNKEGMVrcdTAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd14000   157 KIADYGISRQCCRMGAK---GSEGTPGFRAPEIAR---GNVIYNEKVDVFSFGMLLYEILSGGAPM 216
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
526-903 4.64e-11

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 67.77  E-value: 4.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   526 LKKVSQNSQLANEKLSQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSISQLESLNRELQERNRILENSKSQTDKDYYQ 605
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   606 LQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVEGERKEAQDMLNhsekeknnleiDLNYKLKSLQQRLE 685
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT-----------LLNEEAANLRERLE 827
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   686 QEVNEHKVTKARLTDKHQSIEEAKSvamcemekklkeerearekaenRVVQIEKQCSMLDVDLKQSQQKLEHLTGNKERM 765
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSE----------------------DIESLAAEIEELEELIEELESELEALLNERASL 885
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   766 EDEVKNLTLQLEQESNKrlllQNELKTQAFEA-DNLKGLEKQMKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMRELQD 844
Cdd:TIGR02168  886 EEALALLRSELEELSEE----LRELESKRSELrRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEN 961
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167887698   845 QLEAEqyfSTLYKTQVKELKEEIEEKNRENLKKIQELQNEKE---TLATQL-DLAETKAESEQ 903
Cdd:TIGR02168  962 KIEDD---EEEARRRLKRLENKIKELGPVNLAAIEEYEELKErydFLTAQKeDLTEAKETLEE 1021
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
76-284 5.52e-11

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: 65.57  E-value: 5.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEV-QLVRHKSTRKVYAMKLLSKFEMIkrSDSAFFWEERDIMAFANSPWVVQLFY--------AFQDd 146
Cdd:cd07859     2 YKIQEVIGKGSYGVVcSAIDTHTGEKVAIKKINDVFEHV--SDATRILREIKLLRLLRHPDIVEIKHimlppsrrEFKD- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  147 ryLYMVMEYMpGGDLVNLM-SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNK 225
Cdd:cd07859    79 --IYVVFELM-ESDLHQVIkANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFN 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  226 EGmvrcDTAVGTPDYI------SPEVLKSQGGDgyYGRECDWWSVGVFLYEMLVGDTPFYADSLV 284
Cdd:cd07859   156 DT----PTAIFWTDYVatrwyrAPELCGSFFSK--YTPAIDIWSIGCIFAEVLTGKPLFPGKNVV 214
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
72-284 7.04e-11

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 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-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: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 65.01  E-value: 7.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   72 KAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSkfemIKRSDSAFFWEERDI-----MAFANspwVVQLFYAFQDD 146
Cdd:cd07872     4 KMETYIKLEKLGEGTYATVFKGRSKLTENLVALKEIR----LEHEEGAPCTAIREVsllkdLKHAN---IVTLHDIVHTD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  147 RYLYMVMEYMPGG------DLVNLMSNYDVpekwaRFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTC 220
Cdd:cd07872    77 KSLTLVFEYLDKDlkqymdDCGNIMSMHNV-----KIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLA 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167887698  221 MKMNKEGMVRCDTAVgTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGdTPFYADSLV 284
Cdd:cd07872   152 RAKSVPTKTYSNEVV-TLWYRPPDVLL---GSSEYSTQIDMWGVGCIFFEMASG-RPLFPGSTV 210
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
76-313 7.09e-11

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; 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 TLK2 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: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 65.08  E-value: 7.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKL--LSK--FEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQ-DDRYLY 150
Cdd:cd14041     8 YLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIhqLNKnwRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSlDTDSFC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMG--FIHRDVKPDNMLL---DKSGHLKLADFGTCMKMN 224
Cdd:cd14041    88 TVLEYCEGNDLDFYLKQHKLmSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLvngTACGEIKITDFGLSKIMD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  225 KE------GMVRCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSlvgTYSKIMNHKNSL- 297
Cdd:cd14041   168 DDsynsvdGMELTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFYQCLYGRKPFGHNQ---SQQDILQENTILk 244
                         250       260
                  ....*....|....*....|
gi 167887698  298 ----TFPDDNDISKEAKNLI 313
Cdd:cd14041   245 atevQFPPKPVVTPEAKAFI 264
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
74-219 7.59e-11

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR 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: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 64.67  E-value: 7.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVR-HKSTRKVYAMKLLSKFE--------MIKRSDSAF-----FWEERDIMAFANSPWVVQL 139
Cdd:cd05051     5 EKLEFVEKLGEGQFGEVHLCEaNGLSDLTSDDFIGNDNKdepvlvavKMLRPDASKnaredFLKEVKIMSQLKDPNIVRL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  140 FYAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIH-------------SMGFIHRDVKPDNMLL 206
Cdd:cd05051    85 LGVCTRDEPLCMIVEYMENGDLNQFLQKHEAETQGASATNSKTLSYGTLLYmatqiasgmkyleSLNFVHRDLATRNCLV 164
                         170
                  ....*....|...
gi 167887698  207 DKSGHLKLADFGT 219
Cdd:cd05051   165 GPNYTIKIADFGM 177
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
74-290 7.66e-11

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; 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. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 64.64  E-value: 7.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEV--QLVRHKSTRKVYAMKLLSKFEmiKRSDSAFFWEERDIMA-FANSPWVVQLFYAFQDDRYLY 150
Cdd:cd05089     2 EDIKFEDVIGEGNFGQVikAMIKKDGLKMNAAIKMLKEFA--SENDHRDFAGELEVLCkLGHHPNIINLLGACENRGYLY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGGDLVNLMSNYDVPEKWARF-----------------YTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLK 213
Cdd:cd05089    80 IAIEYAPYGNLLDFLRKSRVLETDPAFakehgtastltsqqllqFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSK 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  214 LADFGtcMKMNKEGMVRCDTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEML-VGDTPFYADSLVGTYSKI 290
Cdd:cd05089   160 IADFG--LSRGEEVYVKKTMGRLPVRWMAIESLNYS----VYTTKSDVWSFGVLLWEIVsLGGTPYCGMTCAELYEKL 231
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
75-313 7.86e-11

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: 64.29  E-value: 7.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVR-HKSTrkvyAMKLLSkFEMIKRSDSAFFWEErdIMAFANSPWV-VQLFY-AFQDDRYLYM 151
Cdd:cd14063     1 ELEIKEVIGKGRFGRVHRGRwHGDV----AIKLLN-IDYLNEEQLEAFKEE--VAAYKNTRHDnLVLFMgACMDPPHLAI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  152 VMEYMPGGDLVNLMSNY--DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKsGHLKLADFGTcmkMNKEGMV 229
Cdd:cd14063    74 VTSLCKGRTLYSLIHERkeKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLEN-GRVVITDFGL---FSLSGLL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  230 RCDTAVGT---P----DYISPEVLKS------QGGDGYYGRECDWWSVGVFLYEMLVGDTPF---YADSLVgtYSKIMNH 293
Cdd:cd14063   150 QPGRREDTlviPngwlCYLAPEIIRAlspdldFEESLPFTKASDVYAFGTVWYELLAGRWPFkeqPAESII--WQVGCGK 227
                         250       260
                  ....*....|....*....|
gi 167887698  294 KNSLtfpDDNDISKEAKNLI 313
Cdd:cd14063   228 KQSL---SQLDIGREVKDIL 244
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
82-218 8.53e-11

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: 61.30  E-value: 8.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKfemikRSDSAFFWEERDI----MAFANSPWVVQLFYAFQDDRYLYMVMEYMP 157
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKIGDD-----VNNEEGEDLESEMdilrRLKGLELNIPKVLVTEDVDGPNILLMELVK 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167887698  158 GGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG 218
Cdd:cd13968    76 GGTLIAYTQEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
76-218 9.08e-11

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 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: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 64.68  E-value: 9.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVyamkllSKFEMIKRSDSAFFWE---ERDIMAFANSPWVVQLF----YAFQDDRY 148
Cdd:cd13981     2 YVISKELGEGGYASVYLAKDDDEQSD------GSLVALKVEKPPSIWEfyiCDQLHSRLKNSRLRESIsgahSAHLFQDE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 LYMVMEYMPGG---DLVNLMSNY---DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL---------------D 207
Cdd:cd13981    76 SILVMDYSSQGtllDVVNKMKNKtggGMDEPLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLrleicadwpgegengW 155
                         170
                  ....*....|.
gi 167887698  208 KSGHLKLADFG 218
Cdd:cd13981   156 LSKGLKLIDFG 166
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
144-317 1.06e-10

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 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: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 63.36  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  144 QDDRYLYMVMEYmpgGDLVNLM-SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLA--DFGTC 220
Cdd:cd14024    57 QDRAYAFFSRHY---GDMHSHVrRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVlvNLEDS 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  221 MKMNKEGMVRCDTAvGTPDYISPEVLKSqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKImnHKNSLTFP 300
Cdd:cd14024   134 CPLNGDDDSLTDKH-GCPAYVGPEILSS--RRSYSGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKI--RRGAFSLP 208
                         170
                  ....*....|....*..
gi 167887698  301 DdnDISKEAKNLICAFL 317
Cdd:cd14024   209 A--WLSPGARCLVSCML 223
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
74-278 1.94e-10

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: 63.16  E-value: 1.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVyAMKLLSKFEMIKRSdsafFWEERDIMAFANSPWVVQLfYAFQDDRYLYMVM 153
Cdd:cd05070     9 ESLQLIKRLGNGQFGEVWMGTWNGNTKV-AIKTLKPGTMSPES----FLEEAQIMKKLKHDKLVQL-YAVVSEEPIYIVT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYD-----VPEKWArfYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGM 228
Cdd:cd05070    83 EYMSKGSLLDFLKDGEgralkLPNLVD--MAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEY 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 167887698  229 VRCDTAVGTPDYISPEVlksqggdGYYGR---ECDWWSVGVFLYEMLV-GDTPF 278
Cdd:cd05070   161 TARQGAKFPIKWTAPEA-------ALYGRftiKSDVWSFGILLTELVTkGRVPY 207
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
82-278 1.97e-10

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: 62.75  E-value: 1.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQ--LVRHKSTRKV-YAMKLLSKFEMIkrSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLyMVMEYMPG 158
Cdd:cd05060     3 LGHGNFGSVRkgVYLMKSGKEVeVAVKTLKQEHEK--AGKKEFLREASVMAQLDHPCIVRLIGVCKGEPLM-LVMELAPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  159 GDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGtcmkMNKegmvrcdtAVGT 237
Cdd:cd05060    80 GPLLKyLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFG----MSR--------ALGA 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 167887698  238 -PDYISPEvlksQGGD---GYYGREC----------DWWSVGVFLYEML-VGDTPF 278
Cdd:cd05060   148 gSDYYRAT----TAGRwplKWYAPECinygkfssksDVWSYGVTLWEAFsYGAKPY 199
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
79-278 2.16e-10

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: 62.66  E-value: 2.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   79 VKVIGRGAFGEVQLVRHKSTRKVyAMKLLSKFEMIKRSdsafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPG 158
Cdd:cd05112     9 VQEIGSGQFGLVHLGYWLNKDKV-AIKTIREGAMSEED----FIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  159 GDLvnlmSNYDVPEKWArfYTAEVVLA--LDAIHSMG------FIHRDVKPDNMLLDKSGHLKLADFGTCmKMNKEGMVR 230
Cdd:cd05112    84 GCL----SDYLRTQRGL--FSAETLLGmcLDVCEGMAyleeasVIHRDLAARNCLVGENQVVKVSDFGMT-RFVLDDQYT 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 167887698  231 CDTAVGTP-DYISPEVLKSqggdGYYGRECDWWSVGVFLYEMLV-GDTPF 278
Cdd:cd05112   157 SSTGTKFPvKWSSPEVFSF----SRYSSKSDVWSFGVLMWEVFSeGKIPY 202
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
80-281 2.39e-10

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: 62.88  E-value: 2.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEV---QLVRHKSTRKVYAMKLLSKFEMIKRSDSafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMV-MEY 155
Cdd:cd05058     1 EVIGKGHFGCVyhgTLIDSDGQKIHCAVKSLNRITDIEEVEQ--FLKEGIIMKDFSHPNVLSLLGICLPSEGSPLVvLPY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVNLMSN--YDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKM-NKEGM-VRC 231
Cdd:cd05058    79 MKHGDLRNFIRSetHNPTVKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIyDKEYYsVHN 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 167887698  232 DTAVGTP-DYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYAD 281
Cdd:cd05058   159 HTGAKLPvKWMALESLQTQK----FTTKSDVWSFGVLLWELMTRGAPPYPD 205
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
77-278 2.48e-10

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: 63.42  E-value: 2.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   77 EVVKVIGRG--AFGEVQLVRHKSTRKVYAMKLLSkFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVME 154
Cdd:cd08227     1 ELLTVIGRGfeDLMTVNLARYKPTGEYVTVRRIN-LEACTNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDLVNLMSNY--DVPEKWARFYTAEVVL-ALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMvRC 231
Cdd:cd08227    80 FMAYGSAKDLICTHfmDGMSELAIAYILQGVLkALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMINHGQ-RL 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 167887698  232 DTAVGTPDY-------ISPEVLKsQGGDGYYGREcDWWSVGVFLYEMLVGDTPF 278
Cdd:cd08227   159 RVVHDFPKYsvkvlpwLSPEVLQ-QNLQGYDAKS-DIYSVGITACELANGHVPF 210
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
345-399 2.53e-10

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 57.37  E-value: 2.53e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698    345 WETL--RDTVAPVVPDLSSDIDTSNFDDLEEDKGEEETFPIPKAFVG-NQLPFVGFTY 399
Cdd:smart00133    5 WDKLenKEIEPPFVPKIKSPTDTSNFDPEFTEETPVLTPVDSPLSGGiQQEPFRGFSY 62
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
82-287 2.88e-10

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; 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. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 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: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 62.92  E-value: 2.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTrkVYAMKLLSK-----FEMIKRSdsafFWEERDIMAFANSPWVVQLF-YAFQDDRYLyMVMEY 155
Cdd:cd14159     1 IGEGGFGCVYQAVMRNT--EYAVKRLKEdseldWSVVKNS----FLTEVEKLSRFRHPNIVDLAgYSAQQGNYC-LIYVY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVN-LMSNYDVPE-KWARfyTAEVVL----ALDAIH--SMGFIHRDVKPDNMLLDKSGHLKLADFG-------TC 220
Cdd:cd14159    74 LPNGSLEDrLHCQVSCPClSWSQ--RLHVLLgtarAIQYLHsdSPSLIHGDVKSSNILLDAALNPKLGDFGlarfsrrPK 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  221 MKMNKEGMVRCDTAVGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTY 287
Cdd:cd14159   152 QPGMSSTLARTQTVRGTLAYLPEEYVK----TGTLSVEIDVYSFGVVLLELLTGRRAMEVDSCSPTK 214
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
74-313 2.89e-10

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 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: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 63.15  E-value: 2.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKL--LSKF--EMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYL 149
Cdd:cd14040     6 ERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIhqLNKSwrDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 Y-MVMEYMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMG--FIHRDVKPDNMLL---DKSGHLKLADFGTCMK 222
Cdd:cd14040    86 FcTVLEYCEGNDLDFYLKQHKLmSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  223 MNKE-----GMVRCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSlvgTYSKIMNHKNSL 297
Cdd:cd14040   166 MDDDsygvdGMDLTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQ---SQQDILQENTIL 242
                         250       260
                  ....*....|....*....|.
gi 167887698  298 T-----FPDDNDISKEAKNLI 313
Cdd:cd14040   243 KatevqFPVKPVVSNEAKAFI 263
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
181-274 3.00e-10

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty 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: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 62.51  E-value: 3.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  181 EVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmkmNKEGMVRcDTAVGTPDYISPEVLksqggDGYYGRECD 260
Cdd:cd13975   110 DVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFC---KPEAMMS-GSIVGTPIHMAPELF-----SGKYDNSVD 180
                          90
                  ....*....|....
gi 167887698  261 WWSVGVFLYEMLVG 274
Cdd:cd13975   181 VYAFGILFWYLCAG 194
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
76-274 3.55e-10

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share 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 association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-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: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 62.78  E-value: 3.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSkfemIKRSDSAFFWEERDI-----MAFANspwVVQLFYAFQDDRYLY 150
Cdd:cd07844     2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEIR----LEHEEGAPFTAIREAsllkdLKHAN---IVTLHDIIHTKKTLT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGgDLVNLMSNYD--VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGtcmkMNKEGM 228
Cdd:cd07844    75 LVFEYLDT-DLKQYMDDCGggLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFG----LARAKS 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 167887698  229 VRCDT---AVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVG 274
Cdd:cd07844   150 VPSKTysnEVVTLWYRPPDVLL---GSTEYSTSLDMWGVGCIFYEMATG 195
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
72-278 3.75e-10

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: 62.79  E-value: 3.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   72 KAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFfwEERDIMAFANSPWVVQLFYAFQDDRYLYM 151
Cdd:cd07869     3 KADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAI--REASLLKGLKHANIVLLHDIIHTKETLTL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  152 VMEYMpGGDLVNLMSNYD---VPEKwARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGM 228
Cdd:cd07869    81 VFEYV-HTDLCQYMDKHPgglHPEN-VKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSH 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 167887698  229 VRCDTAVgTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd07869   159 TYSNEVV-TLWYRPPDVLL---GSTEYSTCLDMWGVGCIFVEMIQGVAAF 204
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
136-278 3.80e-10

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: 62.67  E-value: 3.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  136 VVQLFYAFQDDRYLYMVMEYMPGgDLVNLMSN-------YDVpekwaRFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDK 208
Cdd:cd07870    60 IVLLHDIIHTKETLTFVFEYMHT-DLAQYMIQhpgglhpYNV-----RLFMFQLLRGLAYIHGQHILHRDLKPQNLLISY 133
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167887698  209 SGHLKLADFGtcmkMNKEGMVRCDT---AVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd07870   134 LGELKLADFG----LARAKSIPSQTyssEVVTLWYRPPDVLL---GATDYSSALDIWGAGCIFIEMLQGQPAF 199
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
76-279 3.89e-10

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK 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: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 62.85  E-value: 3.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAffweERDIMAF-----ANSPWVVQLFYAFQDDRYLY 150
Cdd:cd14211     1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQI----EVSILSRlsqenADEFNFVRAYECFQHKNHTC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEyMPGGDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDN-MLLDKSGH---LKLADFGTCMKM 223
Cdd:cd14211    77 LVFE-MLEQNLYDFLKQNKfspLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENiMLVDPVRQpyrVKVIDFGSASHV 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 167887698  224 NKegmVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGdTPFY 279
Cdd:cd14211   156 SK---AVCSTYLQSRYYRAPEIILGLP----FCEAIDMWSLGCVIAELFLG-WPLY 203
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
74-284 4.32e-10

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-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 PCTAIRE-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: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 62.33  E-value: 4.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSkfemIKRSDSAFFWEERDI-----MAFANspwVVQLFYAFQDDRY 148
Cdd:cd07873     2 ETYIKLDKLGEGTYATVYKGRSKLTDNLVALKEIR----LEHEEGAPCTAIREVsllkdLKHAN---IVTLHDIIHTEKS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 LYMVMEYMPGG------DLVNLMSNYDVpekwaRFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmK 222
Cdd:cd07873    75 LTLVFEYLDKDlkqyldDCGNSINMHNV-----KLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLA-R 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887698  223 MNKEGMVRCDTAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGdTPFYADSLV 284
Cdd:cd07873   149 AKSIPTKTYSNEVVTLWYRPPDILL---GSTDYSTQIDMWGVGCIFYEMSTG-RPLFPGSTV 206
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
82-272 4.72e-10

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 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 (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 62.32  E-value: 4.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVR----HKSTRKVYAMK------LLSKFEMIK-------RSDsafFWEERDIMAFANSPWVVQLFYAFQ 144
Cdd:cd05095    13 LGEGQFGEVHLCEaegmEKFMDKDFALEvsenqpVLVAVKMLRadanknaRND---FLKEIKIMSRLKDPNIIRLLAVCI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  145 DDRYLYMVMEYMPGGDLVNLMSNYDVPEKWA-------------RFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH 211
Cdd:cd05095    90 TDDPLCMITEYMENGDLNQFLSRQQPEGQLAlpsnaltvsysdlRFMAAQIASGMKYLSSLNFVHRDLATRNCLVGKNYT 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887698  212 LKLADFGTCMKMNKEGMVRCD-TAVGTPDYISPEVLKSqggdGYYGRECDWWSVGVFLYEML 272
Cdd:cd05095   170 IKIADFGMSRNLYSGDYYRIQgRAVLPIRWMSWESILL----GKFTTASDVWAFGVTLWETL 227
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
82-273 4.77e-10

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-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: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 62.30  E-value: 4.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRK--------------VYAMKLL-SKFEMIKRSDsafFWEERDIMAFANSPWVVQLFYAFQDD 146
Cdd:cd05097    13 LGEGQFGEVHLCEAEGLAEflgegapefdgqpvLVAVKMLrADVTKTARND---FLKEIKIMSRLKNPNIIRLLGVCVSD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  147 RYLYMVMEYMPGGDLVNLMSNYDVPEKWAR-------------FYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLK 213
Cdd:cd05097    90 DPLCMITEYMENGDLNQFLSQREIESTFTHannipsvsianllYMAVQIASGMKYLASLNFVHRDLATRNCLVGNHYTIK 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167887698  214 LADFGTCMKMNKEGMVRCD-TAVGTPDYISPEVLKSqggdGYYGRECDWWSVGVFLYEMLV 273
Cdd:cd05097   170 IADFGMSRNLYSGDYYRIQgRAVLPIRWMAWESILL----GKFTTASDVWAFGVTLWEMFT 226
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
76-274 7.56e-10

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: 62.46  E-value: 7.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSK--------------FEMIKRSDSAffweerdimafaNSPWVVQLFY 141
Cdd:cd14224    67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNekrfhrqaaeeiriLEHLKKQDKD------------NTMNVIHMLE 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  142 AFQDDRYLYMVMEYMPggdlvnlMSNYDVPEK---------WARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH- 211
Cdd:cd14224   135 SFTFRNHICMTFELLS-------MNLYELIKKnkfqgfslqLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRs 207
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167887698  212 -LKLADFGTCMKMNKegmvRCDTAVGTPDYISPEVLKSqggdGYYGRECDWWSVGVFLYEMLVG 274
Cdd:cd14224   208 gIKVIDFGSSCYEHQ----RIYTYIQSRFYRAPEVILG----ARYGMPIDMWSFGCILAELLTG 263
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
82-278 7.60e-10

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: 61.75  E-value: 7.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVR----HKSTRKVYAMKLLSKFEMIKRsdsafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMP 157
Cdd:cd14158    23 LGEGGFGVVFKGYindkNVAVKKLAAMVDISTEDLTKQ-----FEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  158 GGDLVNLMS--NYDVPEKWA-RFYTAE-VVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGM-VRCD 232
Cdd:cd14158    98 NGSLLDRLAclNDTPPLSWHmRCKIAQgTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARASEKFSQtIMTE 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 167887698  233 TAVGTPDYISPEVLKsqggdGYYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd14158   178 RIVGTTAYMAPEALR-----GEITPKSDIFSFGVVLLEIITGLPPV 218
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
172-338 7.66e-10

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 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: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 60.83  E-value: 7.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  172 EKWARFYTaEVVLALDAIHSMGFIHRDVKPDNMLL--DKSGHLKLADFGTCMKMNKEGMVRCDTAvGTPDYISPEVLKSQ 249
Cdd:cd14023    84 EEAARLFK-QIVSAVAHCHQSAIVLGDLKLRKFVFsdEERTQLRLESLEDTHIMKGEDDALSDKH-GCPAYVSPEILNTT 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  250 GGdgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKImnHKNSLTFPDdnDISKEAKNLICAFLtdREVRLGRNGV 329
Cdd:cd14023   162 GT--YSGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKI--RRGQFCIPD--HVSPKARCLIRSLL--RREPSERLTA 233

                  ....*....
gi 167887698  330 EEIKRHLFF 338
Cdd:cd14023   234 PEILLHPWF 242
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
76-293 8.05e-10

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 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 that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 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: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 62.37  E-value: 8.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSK-FEMIKRSDSAFfwEERDIMAFANSPWVVQLFYAFQDDRYL----- 149
Cdd:cd07875    26 YQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRpFQNQTHAKRAY--RELVLMKCVNHKNIIGLLNVFTPQKSLeefqd 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 -YMVMEYMpGGDLVNLMsNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGM 228
Cdd:cd07875   104 vYIVMELM-DANLCQVI-QMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFM 181
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  229 VrcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNH 293
Cdd:cd07875   182 M--TPYVVTRYYRAPEVILGMG----YKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIEQ 240
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
82-272 8.20e-10

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: 61.00  E-value: 8.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKfemikRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKIYKN-----DVDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNYDVPEKWARfytaEVVLALDA------IHSMGFIHRDVKPDNMLLDKSGHLK---LADFG-----TCMKMNKEG 227
Cdd:cd14156    76 EELLAREELPLSWRE----KVELACDIsrgmvyLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGlarevGEMPANDPE 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 167887698  228 mvRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEML 272
Cdd:cd14156   152 --RKLSLVGSAFWMAPEMLRGEP----YDRKVDVFSFGIVLCEIL 190
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
81-274 9.34e-10

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. 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. The LRRK2 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: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 60.74  E-value: 9.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   81 VIGRGAFGEVqlVRHKSTRKVYAMKLLSKfemikRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLymVMEYMPGGD 160
Cdd:cd14068     1 LLGDGGFGSV--YRAVYRGEDVAVKIFNK-----HTSFRLLRQELVVLSHLHHPSLVALLAAGTAPRML--VMELAPKGS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  161 LVNLMS--NYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL-----DKSGHLKLADFGTCMKMNKEGMVRCDt 233
Cdd:cd14068    72 LDALLQqdNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQYCCRMGIKTSE- 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 167887698  234 avGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVG 274
Cdd:cd14068   151 --GTPGFRAPEVAR---GNVIYNQQADVYSFGLLLYDILTC 186
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
517-710 1.02e-09

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 62.15  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  517 STLKDQLEDLKKVSQNSQLANEKLSQLQKQLEEANDLLrteSDTAVRLRKSHTEMSKSISQLESLNRELQERNRILEN-- 594
Cdd:COG3883    16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEY---NELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  595 -SKSQTDKDYYQLQAILEaerrdrghdSEMIGDLQARITSLQEEVKHLKHNLEKVEGERKEAQDMLNHSEKEKNNLEiDL 673
Cdd:COG3883    93 rALYRSGGSVSYLDVLLG---------SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELE-AL 162
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 167887698  674 NYKLKSLQQRLEQEVNEHKVTKARLTDKHQSIEEAKS 710
Cdd:COG3883   163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
76-313 1.02e-09

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: 61.62  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSK-FEMI---KRSD------SAFFWEE----RDIMAFANSPwvvqlfy 141
Cdd:cd07858     7 YVPIKPIGRGAYGIVCSAKNSETNEKVAIKKIANaFDNRidaKRTLreikllRHLDHENviaiKDIMPPPHRE------- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  142 AFQDdryLYMVMEYMpGGDLVNLM-SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTC 220
Cdd:cd07858    80 AFND---VYIVYELM-DTDLHQIIrSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  221 MKMNKEGMVRCDTAVgTPDYISPEVLKSQGGdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSltfP 300
Cdd:cd07858   156 RTTSEKGDFMTEYVV-TRWYRAPELLLNCSE---YTTAIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLITELLGS---P 228
                         250
                  ....*....|....*..
gi 167887698  301 DDNDI----SKEAKNLI 313
Cdd:cd07858   229 SEEDLgfirNEKARRYI 245
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
71-279 1.21e-09

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). 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. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA 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: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 60.65  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   71 MKAEDYEVVKVIGRGAFGEVQLVRHK--STRKVY-AMKLLSKFEMIK-RSDsafFWEERDIMAFANSPWVVQLFYAFQDD 146
Cdd:cd05066     1 IDASCIKIEKVIGAGEFGEVCSGRLKlpGKREIPvAIKTLKAGYTEKqRRD---FLSEASIMGQFDHPNIIHLEGVVTRS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  147 RYLYMVMEYMPGGDLVNLMSNYDvpekwARFYTAEVVLALDAIHS-------MGFIHRDVKPDNMLLDKSGHLKLADFGT 219
Cdd:cd05066    78 KPVMIVTEYMENGSLDAFLRKHD-----GQFTVIQLVGMLRGIASgmkylsdMGYVHRDLAARNILVNSNLVCKVSDFGL 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167887698  220 CMKMNKEGMVRCDTAVGT-P-DYISPEVLKSQGgdgyYGRECDWWSVGVFLYE-MLVGDTPFY 279
Cdd:cd05066   153 SRVLEDDPEAAYTTRGGKiPiRWTAPEAIAYRK----FTSASDVWSYGIVMWEvMSYGERPYW 211
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
236-338 1.33e-09

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB 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: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 60.13  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  236 GTPDYISPEVLKSQGGdgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKImnHKNSLTFPDdnDISKEAKNLICA 315
Cdd:cd13976   148 GCPAYVSPEILNSGAT--YSGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKI--RRGQFAIPE--TLSPRARCLIRS 221
                          90       100
                  ....*....|....*....|...
gi 167887698  316 FLtdREVRLGRNGVEEIKRHLFF 338
Cdd:cd13976   222 LL--RREPSERLTAEDILLHPWL 242
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
236-338 1.56e-09

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 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: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 60.05  E-value: 1.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  236 GTPDYISPEVLKSQGGdgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKImnHKNSLTFPDdnDISKEAKNLICA 315
Cdd:cd14022   148 GCPAYVSPEILNTSGS--YSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKI--RRGQFNIPE--TLSPKAKCLIRS 221
                          90       100
                  ....*....|....*....|...
gi 167887698  316 FLtdREVRLGRNGVEEIKRHLFF 338
Cdd:cd14022   222 IL--RREPSERLTSQEILDHPWF 242
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
79-278 1.62e-09

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: 60.48  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   79 VKVIGRGAFGEVQ--LVRHKSTRKV---YAMKLLSkfEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd05036    11 IRALGQGAFGEVYegTVSGMPGDPSplqVAVKTLP--ELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQRLPRFILL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVN-LMSNYDVPEKWARFYTAEVV-LALDA------IHSMGFIHRDVKPDNMLLDKSGH---LKLADFGTCMK 222
Cdd:cd05036    89 ELMAGGDLKSfLRENRPRPEQPSSLTMLDLLqLAQDVakgcryLEENHFIHRDIAARNCLLTCKGPgrvAKIGDFGMARD 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  223 MNKEGMVR-CDTAVGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLYE-MLVGDTPF 278
Cdd:cd05036   169 IYRADYYRkGGKAMLPVKWMPPEAFL----DGIFTSKTDVWSFGVLLWEiFSLGYMPY 222
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
425-1090 1.76e-09

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 62.39  E-value: 1.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   425 QESLQKTIYKLEEQLHN----EMQLKDEMEQkcrtsnikLDKIMKELDEE-GNQRRNLESTVSQIEKEKMLLQHRINEYQ 499
Cdd:TIGR02169  289 QLRVKEKIGELEAEIASlersIAEKERELED--------AEERLAKLEAEiDKLLAEIEELEREIEEERKRRDKLTEEYA 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   500 RKAEQENEKRRNVENEVSTLKDQLEDLKKVsqnsqlaNEKLSQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSISQLE 579
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEFAETRDELKDY-------REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIE 433
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   580 SLNRELQERNRILENSKSQTDKDYYQLQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVE---GERKEAQ 656
Cdd:TIGR02169  434 AKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEervRGGRAVE 513
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   657 DMLNHSEKEKNNL-----EIDLNYKLK---SLQQRLEQEVNEHKVTKARltdkhqSIEEAKSVAMCEME----KKLKEER 724
Cdd:TIGR02169  514 EVLKASIQGVHGTvaqlgSVGERYATAievAAGNRLNNVVVEDDAVAKE------AIELLKRRKAGRATflplNKMRDER 587
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   725 EAREKAEnrvvqiEKQCSMLDVDLKQSQQKLEHL-------TGNKERME------DEVKNLTLQ---LEQE------SNK 782
Cdd:TIGR02169  588 RDLSILS------EDGVIGFAVDLVEFDPKYEPAfkyvfgdTLVVEDIEaarrlmGKYRMVTLEgelFEKSgamtggSRA 661
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   783 RLLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMRELQDQLEA-EQYFSTLyKTQVK 861
Cdd:TIGR02169  662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQlEQEEEKL-KERLE 740
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   862 ELKEEIEEKNRENLKKIQELQ-NEKETLATQLDLAETKAESEQLARGLLEEQYFELTQESKKAasrnRQEITDKDHTVSR 940
Cdd:TIGR02169  741 ELEEDLSSLEQEIENVKSELKeLEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKL----EEEVSRIEARLRE 816
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   941 LEEANSMLTKDIEILRRENEELTEKMkKAEEEYKLEKEEEISNLKAAFEKnINTERTLKTQAVNKLAEimNRKDFKIDRK 1020
Cdd:TIGR02169  817 IEQKLNRLTLEKEYLEKEIQELQEQR-IDLKEQIKSIEKEIENLNGKKEE-LEEELEELEAALRDLES--RLGDLKKERD 892
                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167887698  1021 KANTQdLRKKEKENRKLQLELNQEREKFNQMVVKHQ------KELNDMQAQLVEECAHR---NELQMQLASKESDIEQL 1090
Cdd:TIGR02169  893 ELEAQ-LRELERKIEELEAQIEKKRKRLSELKAKLEaleeelSEIEDPKGEDEEIPEEElslEDVQAELQRVEEEIRAL 970
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
76-293 1.87e-09

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. 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 JNK3 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: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 61.26  E-value: 1.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSK-FEMIKRSDSAFfwEERDIMAFANSPWVVQLFYAFQDDRYL----- 149
Cdd:cd07874    19 YQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRpFQNQTHAKRAY--RELVLMKCVNHKNIISLLNVFTPQKSLeefqd 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 -YMVMEYMpGGDLVNLMsNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGM 228
Cdd:cd07874    97 vYLVMELM-DANLCQVI-QMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFM 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  229 VrcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNH 293
Cdd:cd07874   175 M--TPYVVTRYYRAPEVILGMG----YKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQ 233
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
76-292 2.09e-09

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: 60.36  E-value: 2.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMK--------------------LLSKFEMIKRSDSAFFweeRDIMAFANSPW 135
Cdd:cd07863     2 YEPVAEIGVGAYGTVYKARDPHSGHFVALKsvrvqtnedglplstvrevaLLKRLEAFDHPNIVRL---MDVCATSRTDR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  136 VVQLFYAFQD-DRYLYMVMEYMPGGDLvnlmsnydvPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKL 214
Cdd:cd07863    79 ETKVTLVFEHvDQDLRTYLDKVPPPGL---------PAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKL 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  215 ADFGTCMKMNKEgmVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMN 292
Cdd:cd07863   150 ADFGLARIYSCQ--MALTPVVVTLWYRAPEVLLQST----YATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFD 221
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
74-278 2.15e-09

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: 60.04  E-value: 2.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVyAMKLLSKFEMikrSDSAFFwEERDIMAFANSPWVVQLfYAFQDDRYLYMVM 153
Cdd:cd05073    11 ESLKLEKKLGAGQFGEVWMATYNKHTKV-AVKTMKPGSM---SVEAFL-AEANVMKTLQHDKLVKL-HAVVTKEPIYIIT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVR 230
Cdd:cd05073    85 EFMAKGSLLDFLKSDEgskQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEYTA 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 167887698  231 CDTAVGTPDYISPEVLKSqggdGYYGRECDWWSVGVFLYEMLV-GDTPF 278
Cdd:cd05073   165 REGAKFPIKWTAPEAINF----GSFTIKSDVWSFGILLMEIVTyGRIPY 209
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
76-274 2.41e-09

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: 60.25  E-value: 2.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVR-HKsTRKVYAMKLL---SKF-----------EMIKRSDSAffweerdimafaNSPWVVQLF 140
Cdd:cd14210    15 YEVLSVLGKGSFGQVVKCLdHK-TGQLVAIKIIrnkKRFhqqalvevkilKHLNDNDPD------------DKHNIVRYK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  141 YAFQDDRYLYMVMEyMPGGDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL---DKSGhLKL 214
Cdd:cd14210    82 DSFIFRGHLCIVFE-LLSINLYELLKSNNfqgLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLkqpSKSS-IKV 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  215 ADFGT-CMKMNKegmvrcdtaVGTpdYI------SPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVG 274
Cdd:cd14210   160 IDFGSsCFEGEK---------VYT--YIqsrfyrAPEVILGLP----YDTAIDMWSLGCILAELYTG 211
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
422-1088 2.49e-09

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 61.99  E-value: 2.49e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   422 KSLQESLQKTIYKLEEQLHNEMQLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIekekmllqhRINEYQRK 501
Cdd:TIGR00606  229 KEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELK---------MEKVFQGT 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   502 AEQENEKRRNVENEVSTLKDQLED----LKKVSQNSQLANEKLSQLQKQLEE-------------ANDLLRTESDTAVRL 564
Cdd:TIGR00606  300 DEQLNDLYHNHQRTVREKERELVDcqreLEKLNKERRLLNQEKTELLVEQGRlqlqadrhqehirARDSLIQSLATRLEL 379
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   565 R--KSHTEMSKSISQLESLNRELQERN--RILENSKSQTDKDYYQLQAILEAERRDRGHdSEMIGDLQARITSLQEEVKH 640
Cdd:TIGR00606  380 DgfERGPFSERQIKNFHTLVIERQEDEakTAAQLCADLQSKERLKQEQADEIRDEKKGL-GRTIELKKEILEKKQEELKF 458
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   641 LKHNLEKVEGERK---EAQDMLNHSEK-----EKN--------------NLEIDLNYKLKSLQQRLEQeVNEHKVTKARL 698
Cdd:TIGR00606  459 VIKELQQLEGSSDrilELDQELRKAERelskaEKNsltetlkkevkslqNEKADLDRKLRKLDQEMEQ-LNHHTTTRTQM 537
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   699 -------TDKHQSIEEAKSVAMCE-------------MEKKLKEEREAREKAENRVVQIEKQCSMLDVDLKQSQQKLEHL 758
Cdd:TIGR00606  538 emltkdkMDKDEQIRKIKSRHSDEltsllgyfpnkkqLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESK 617
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   759 TGNKERMEDEV-------------KNLTLQLEQESNKRLLL--QNELKTQAFEADNLKG------------LEKQMKQEI 811
Cdd:TIGR00606  618 EEQLSSYEDKLfdvcgsqdeesdlERLKEEIEKSSKQRAMLagATAVYSQFITQLTDENqsccpvcqrvfqTEAELQEFI 697
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   812 NTLLEAKRLLEFELAQLTKQYRGNEGQMRELQDQLEAEQYFSTLYKTQVKELKEEIEEKNREnlkkIQELQN---EKETL 888
Cdd:TIGR00606  698 SDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRD----IQRLKNdieEQETL 773
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   889 ATQLDLAETKAESEQLARGLLEEQYFELTQESKKAA---------------SRNRQEITDKDHTVSRLEEANSMLTKDIE 953
Cdd:TIGR00606  774 LGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAqqaaklqgsdldrtvQQVNQEKQEKQHELDTVVSKIELNRKLIQ 853
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   954 ILRRENEELTEKMKKAEEEYKL--EKEEEISNLKAAFEKNINTERTLKTQAVNKLAEIMNRKDFKIDRKKANTQDLRKKE 1031
Cdd:TIGR00606  854 DQQEQIQHLKSKTNELKSEKLQigTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKE 933
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  1032 KENRKLQLELNQEREKFNQMV----------------VKHQKE--LNDMQAQLVEECAHRNELQMQLASKESDIE 1088
Cdd:TIGR00606  934 TSNKKAQDKVNDIKEKVKNIHgymkdienkiqdgkddYLKQKEteLNTVNAQLEECEKHQEKINEDMRLMRQDID 1008
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
66-278 2.91e-09

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 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 Tyro3 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: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 59.93  E-value: 2.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   66 IRDLRMKAEDYEVVKVIGRGAFG---EVQLVRHKSTRKVYAMKLLsKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYA 142
Cdd:cd05074     1 LKDVLIQEQQFTLGRMLGKGEFGsvrEAQLKSEDGSFQKVAVKML-KADIFSSSDIEEFLREAACMKEFDHPNVIKLIGV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  143 FQDDRY-----LYMV-MEYMPGGDLVN--LMSN-----YDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKS 209
Cdd:cd05074    80 SLRSRAkgrlpIPMViLPFMKHGDLHTflLMSRigeepFTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNEN 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167887698  210 GHLKLADFGTCMKMNKEGMVRCDTAVGTP-DYISPEVLksqgGDGYYGRECDWWSVGVFLYE-MLVGDTPF 278
Cdd:cd05074   160 MTVCVADFGLSKKIYSGDYYRQGCASKLPvKWLALESL----ADNVYTTHSDVWAFGVTMWEiMTRGQTPY 226
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
76-291 3.16e-09

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: 60.43  E-value: 3.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSK-FEMIKRSDSAFfwEERDIMAFANSPWVVQLFYAFQDDRYL----- 149
Cdd:cd07876    23 YQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRpFQNQTHAKRAY--RELVLLKCVNHKNIISLLNVFTPQKSLeefqd 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  150 -YMVMEYMpGGDLVNLMsNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGM 228
Cdd:cd07876   101 vYLVMELM-DANLCQVI-HMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFM 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167887698  229 VrcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIM 291
Cdd:cd07876   179 M--TPYVVTRYYRAPEVILGMG----YKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVI 235
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
415-1094 3.40e-09

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 61.60  E-value: 3.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   415 RTSSNADKSLQESLQKTIYKLEEQLHNEM-----------QLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQ 483
Cdd:TIGR00606  351 RLQLQADRHQEHIRARDSLIQSLATRLELdgfergpfserQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADE 430
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   484 IEKEKMLLQHRINEYQRKAEQENEKRRNVENEVSTLKDQLEDLKKVSQNSQLANEKLSQLQKqleeaNDLLRTESDTAVR 563
Cdd:TIGR00606  431 IRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK-----NSLTETLKKEVKS 505
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   564 LRKSHTEMSKSISQL----ESLNRELQERNRILENSKSQTDKDyyqlQAILEAERRDRGHDSEMIGD------LQARITS 633
Cdd:TIGR00606  506 LQNEKADLDRKLRKLdqemEQLNHHTTTRTQMEMLTKDKMDKD----EQIRKIKSRHSDELTSLLGYfpnkkqLEDWLHS 581
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   634 LQEEVKHLKHNLEKVEGERKEAQDMLNHSEKEKNNLEIDLNYKLKSLQQRLEQEVNEHKVTKAR----LTDKHQSIEEAK 709
Cdd:TIGR00606  582 KSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKeeieKSSKQRAMLAGA 661
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   710 SVAMCEMEKKLKEEREAREKAENRVVQIEKQCSMLDVDLkqsQQKLEHLTGNKERMEDEVKNLTLQLEQESNKRLLLQNE 789
Cdd:TIGR00606  662 TAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDL---QSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSI 738
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   790 LKTQAFEA----DNLKGLEKQMKQEINTLLEAKRLLEFELAQ--LTKQYRGNEGQMRELQDQLEA-----EQYFSTLYK- 857
Cdd:TIGR00606  739 IDLKEKEIpelrNKLQKVNRDIQRLKNDIEEQETLLGTIMPEeeSAKVCLTDVTIMERFQMELKDverkiAQQAAKLQGs 818
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   858 ------TQVKELKEEIEEKNRENLKKIQELQN-----EKETLATQLDLAETKAESEQLA-----RGLLEEQYFELT---Q 918
Cdd:TIGR00606  819 dldrtvQQVNQEKQEKQHELDTVVSKIELNRKliqdqQEQIQHLKSKTNELKSEKLQIGtnlqrRQQFEEQLVELStevQ 898
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   919 ESKKAASRNRQEI-----------TDKDHTVSRLEEANSMLTKDIEILRRE-------NEELTEKMKKAEEEYKLEKEEE 980
Cdd:TIGR00606  899 SLIREIKDAKEQDspletflekdqQEKEELISSKETSNKKAQDKVNDIKEKvknihgyMKDIENKIQDGKDDYLKQKETE 978
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   981 ISNLKAAFEKNintertlkTQAVNKLAEIMNRKDFKIDRKKANTQ------DLRKKEKENRKLQLELNQEREKFNQMVVK 1054
Cdd:TIGR00606  979 LNTVNAQLEEC--------EKHQEKINEDMRLMRQDIDTQKIQERwlqdnlTLRKRENELKEVEEELKQHLKEMGQMQVL 1050
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|.
gi 167887698  1055 HQK-ELNDMQAQLVEECAHRNELQMQLASKESDIEQLRAKL 1094
Cdd:TIGR00606 1051 QMKqEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL 1091
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
414-847 3.43e-09

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 61.67  E-value: 3.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   414 NRTSSNADKSLQEsLQKTIYKLEEQLHNEMQLKDEMEQKCRTSNIKLDKIMKELDEegnqrRNLEstvsqIEKEKMLLQH 493
Cdd:pfam15921  369 SQESGNLDDQLQK-LLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDD-----RNME-----VQRLEALLKA 437
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   494 RINEYQRKAEQenekrrnvenEVSTLKDQLEDLkkvsqnsqlanEKLSQLQKQLEEANDLLR--TESDTAVRLRKSHTEm 571
Cdd:pfam15921  438 MKSECQGQMER----------QMAAIQGKNESL-----------EKVSSLTAQLESTKEMLRkvVEELTAKKMTLESSE- 495
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   572 sKSISQLESlnrELQERNRILENSKSQTDKdyyqlqaileaerrdrghdsemigdLQARITSLQEEVKHLKHNLEKVEGE 651
Cdd:pfam15921  496 -RTVSDLTA---SLQEKERAIEATNAEITK-------------------------LRSRVDLKLQELQHLKNEGDHLRNV 546
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   652 RKEAQDM-LNHSEKEKnNLEIdLNYKLKSLQQ-----------------RLEQEVNEHKVTKARLtdkhQSIEEAKSVAM 713
Cdd:pfam15921  547 QTECEALkLQMAEKDK-VIEI-LRQQIENMTQlvgqhgrtagamqvekaQLEKEINDRRLELQEF----KILKDKKDAKI 620
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   714 CEMEKKLKEEREAREKAEN------RVVQ-IEKQCSMLDVDLKQSQQKLEHLTGNKERMEDEVKNLTLQLEQESNKrlll 786
Cdd:pfam15921  621 RELEARVSDLELEKVKLVNagserlRAVKdIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNK---- 696
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167887698   787 qneLKTQafeadnLKGLEKQMKQEINTL--LEAKRLLEFELAQ-LTKQYRGNEGQMRELQDQLE 847
Cdd:pfam15921  697 ---LKMQ------LKSAQSELEQTRNTLksMEGSDGHAMKVAMgMQKQITAKRGQIDALQSKIQ 751
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
444-913 3.49e-09

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 61.32  E-value: 3.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  444 QLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIekekmllqhriNEYQRKAEQENEKRRNVENEVSTLKDQL 523
Cdd:COG4717    50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEY-----------AELQEELEELEEELEELEAELEELREEL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  524 EDLKKVSQNSQLANEkLSQLQKQLEEANDLLRtesdtavRLRKSHTEMSKSISQLESLNRELQERNRILENSKSQTDkdY 603
Cdd:COG4717   119 EKLEKLLQLLPLYQE-LEALEAELAELPERLE-------ELEERLEELRELEEELEELEAELAELQEELEELLEQLS--L 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  604 YQLQAILEAERRdrghdsemIGDLQARITSLQEEVKHLKHNLEKVEGERKEAQDMLNHSEKEKNNLEIDLNYKLKSLQQR 683
Cdd:COG4717   189 ATEEELQDLAEE--------LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLA 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  684 LEQEVNEHKVTKARLTDKHQSIEEAKSVAMCEMEKKLKEEREAREKAENRVV-------QIEKQCSMLDVDLKQSQQKLE 756
Cdd:COG4717   261 LLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAleeleeeELEELLAALGLPPDLSPEELL 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  757 HLtgnkERMEDEVKNLTLQLEQESNKRLLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLEfELAQLTKQYRGNE 836
Cdd:COG4717   341 EL----LDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKE-ELEELEEQLEELL 415
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167887698  837 GQMRELQDQLEAEQYFSTLYKTQVKELKEEIEEknRENLKKIQELQNEKETLATQLDLAETKAESEQLARGL--LEEQY 913
Cdd:COG4717   416 GELEELLEALDEEELEEELEELEEELEELEEEL--EELREELAELEAELEQLEEDGELAELLQELEELKAELreLAEEW 492
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
82-278 3.52e-09

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: 59.70  E-value: 3.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVyAMKLLSKFEMIKRSdsafFWEERDIMAFANSPWVVQLfYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd05069    20 LGQGCFGEVWMGTWNGTTKV-AIKTLKPGTMMPEA----FLQEAQIMKKLRHDKLVPL-YAVVSEEPIYIVTEFMGKGSL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNYDvpEKWARF-----YTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVG 236
Cdd:cd05069    94 LDFLKEGD--GKYLKLpqlvdMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKF 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 167887698  237 TPDYISPEVlksqggdGYYGR---ECDWWSVGVFLYEMLV-GDTPF 278
Cdd:cd05069   172 PIKWTAPEA-------ALYGRftiKSDVWSFGILLTELVTkGRVPY 210
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
121-278 3.61e-09

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: 59.16  E-value: 3.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  121 FWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM--EYMPGGDLVNLMSNYDVP-----EKWARfytaEVVLALDAIHSMG 193
Cdd:cd13983    47 FKQEIEILKSLKHPNIIKFYDSWESKSKKEVIFitELMTSGTLKQYLKRFKRLklkviKSWCR----QILEGLNYLHTRD 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  194 --FIHRDVKPDNMLLD-KSGHLKLADFGTCMKMNKEGMVRCdtaVGTPDYISPEVLksqggDGYYGRECDWWSVGVFLYE 270
Cdd:cd13983   123 ppIIHRDLKCDNIFINgNTGEVKIGDLGLATLLRQSFAKSV---IGTPEFMAPEMY-----EEHYDEKVDIYAFGMCLLE 194

                  ....*...
gi 167887698  271 MLVGDTPF 278
Cdd:cd13983   195 MATGEYPY 202
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
181-292 5.46e-09

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: 58.56  E-value: 5.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  181 EVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG-TCMKMNKEGMVRCDTAVGTPDYISPEVLKSQGGDGYYGREc 259
Cdd:cd14062    97 QTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGlATVKTRWSGSQQFEQPTGSILWMAPEVIRMQDENPYSFQS- 175
                          90       100       110
                  ....*....|....*....|....*....|...
gi 167887698  260 DWWSVGVFLYEMLVGDTPfyadslvgtYSKIMN 292
Cdd:cd14062   176 DVYAFGIVLYELLTGQLP---------YSHINN 199
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
75-290 5.52e-09

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 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: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 59.24  E-value: 5.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEV--QLVRHKSTRKVYAMKLLSKFEmiKRSDSAFFWEERDIMA-FANSPWVVQLFYAFQDDRYLYM 151
Cdd:cd05088     8 DIKFQDVIGEGNFGQVlkARIKKDGLRMDAAIKRMKEYA--SKDDHRDFAGELEVLCkLGHHPNIINLLGACEHRGYLYL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  152 VMEYMPGGDLVNLMSNYDVPEKWARF-----------------YTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKL 214
Cdd:cd05088    86 AIEYAPHGNLLDFLRKSRVLETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKI 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  215 ADFGtcMKMNKEGMVRCDTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEML-VGDTPFYADSLVGTYSKI 290
Cdd:cd05088   166 ADFG--LSRGQEVYVKKTMGRLPVRWMAIESLNYS----VYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEKL 236
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
563-965 5.83e-09

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 60.55  E-value: 5.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  563 RLRKSHTEMSKSISQLESLN-RELQERNRILENSKSQTDkDYYQLQAILEAerrdrghdsemigdLQARITSLQEEVKHL 641
Cdd:COG4717    50 RLEKEADELFKPQGRKPELNlKELKELEEELKEAEEKEE-EYAELQEELEE--------------LEEELEELEAELEEL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  642 KHNLEKVEgERKEAQDMLNHSEKEKNNLEiDLNYKLKSLQQRLEQEVNehkvTKARLTDKHQSIEEAKSVAMCEMEKKLK 721
Cdd:COG4717   115 REELEKLE-KLLQLLPLYQELEALEAELA-ELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSL 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  722 EEREAREKAENRVVQIEKQCSMLDVDLKQSQQKLEHLTGNKERMEDEVKNLTLQLEQESNKRLLL--------------- 786
Cdd:COG4717   189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsl 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  787 ----------------------------QNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLE-------FELAQLTKQ 831
Cdd:COG4717   269 lsliltiagvlflvlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAALGLPPdlspeelLELLDRIEE 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  832 YRGNEGQMRELQDQLEAEQYFSTLYK--TQVKELKEEIEEKNRENLKKIQELQNEKETLATQLDLA--ETKAESEQLARG 907
Cdd:COG4717   349 LQELLREAEELEEELQLEELEQEIAAllAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELlgELEELLEALDEE 428
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167887698  908 LLEEQYFELTQESKKAASR---NRQEITDKDHTVSRLEEAN--SMLTKDIEILRRENEELTEK 965
Cdd:COG4717   429 ELEEELEELEEELEELEEEleeLREELAELEAELEQLEEDGelAELLQELEELKAELRELAEE 491
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
123-340 8.59e-09

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like 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: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 58.49  E-value: 8.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  123 EERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLvnlmsnYDVPEKWARFytaEVVLALDAIH-SMGFIHRDVKP 201
Cdd:cd14011    73 ESRESLAFATEPVFASLANVLGERDNMPSPPPELQDYKL------YDVEIKYGLL---QISEALSFLHnDVKLVHGNICP 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  202 DNMLLDKSGHLKLADFGTCMKM----NKEGMVRCDT------AVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEM 271
Cdd:cd14011   144 ESVVINSNGEWKLAGFDFCISSeqatDQFPYFREYDpnlpplAQPNLNYLAPEYILSKT----CDPASDMFSLGVLIYAI 219
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167887698  272 LV-GDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFL-TDREVRLgrnGVEEIKRHLFFKN 340
Cdd:cd14011   220 YNkGKPLFDCVNNLLSYKKNSNQLRQLSLSLLEKVPEELRDHVKTLLnVTPEVRP---DAEQLSKIPFFDD 287
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
82-341 8.60e-09

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: 58.19  E-value: 8.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKrSDSAFFWEERDIMAFANSPWVVQLFYAFQD----DRYLYMVMEYMP 157
Cdd:cd14031    18 LGRGAFKTVYKGLDTETWVEVAWCELQDRKLTK-AEQQRFKEEAEMLKGLQHPNIVRFYDSWESvlkgKKCIVLVTELMT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  158 GGDLVNLMSNYDVPE-KWARFYTAEVVLALDAIHSMG--FIHRDVKPDNMLLD-KSGHLKLADFGTCMKMNKEgmvRCDT 233
Cdd:cd14031    97 SGTLKTYLKRFKVMKpKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATLMRTS---FAKS 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  234 AVGTPDYISPEVLKSqggdgYYGRECDWWSVGVFLYEMLVGDTPFY-ADSLVGTYSKIMNHKNSLTFPDDNDisKEAKNL 312
Cdd:cd14031   174 VIGTPEFMAPEMYEE-----HYDESVDVYAFGMCMLEMATSEYPYSeCQNAAQIYRKVTSGIKPASFNKVTD--PEVKEI 246
                         250       260
                  ....*....|....*....|....*....
gi 167887698  313 ICAFLtdREVRLGRNGVEEIKRHLFFKND 341
Cdd:cd14031   247 IEGCI--RQNKSERLSIKDLLNHAFFAED 273
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
474-1112 8.94e-09

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 60.15  E-value: 8.94e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   474 RRNLESTvSQIEKEKMLLQHRineyqrkaEQENEKRRNVENEVSTLKDQLEDLKKvSQNSqLANEKLSQLqKQLEEAN-- 551
Cdd:pfam07111  131 RKNLEEG-SQRELEEIQRLHQ--------EQLSSLTQAHEEALSSLTSKAEGLEK-SLNS-LETKRAGEA-KQLAEAQke 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   552 -DLLRTEsdtavrLRKSHTEMSKSISQLESLNRELQERnrILENSKSQT-DKDYYQLQAILEAERRDRGhdsemigDLQA 629
Cdd:pfam07111  199 aELLRKQ------LSKTQEELEAQVTLVESLRKYVGEQ--VPPEVHSQTwELERQELLDTMQHLQEDRA-------DLQA 263
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   630 RITSLQEEVKHLKHNLEKVEGE---------------RKEAQDMLNH--------------SEKEKNNLEIDLNYKLKSL 680
Cdd:pfam07111  264 TVELLQVRVQSLTHMLALQEEEltrkiqpsdslepefPKKCRSLLNRwrekvfalmvqlkaQDLEHRDSVKQLRGQVAEL 343
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   681 QQRLEQEVNEHKVTKARLTDKHQSIE-EAKSVAMCEMEkkLKEEREAREKAENRVVQIEKQCSMLDVDLKQSQQKLEhlt 759
Cdd:pfam07111  344 QEQVTSQSQEQAILQRALQDKAAEVEvERMSAKGLQME--LSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLE--- 418
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   760 GNKERMEDEVKNLTLqleqesnkrllLQNELKTQAFEADNLKGLEK------QMKQEINTLLEAKRLLEFELAQLTKQyr 833
Cdd:pfam07111  419 TTMTRVEQAVARIPS-----------LSNRLSYAVRKVHTIKGLMArkvalaQLRQESCPPPPPAPPVDADLSLELEQ-- 485
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   834 gnegqMRELQDQLEAEQYFSTLYKTQVKELKEEIEEKNRENLKKIQElQNEKETLATQLDLAETKAESEQLARGlleeqy 913
Cdd:pfam07111  486 -----LREERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQ-QLEQELQRAQESLASVGQQLEVARQG------ 553
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   914 felTQESKKAASRNRQEITDKDHTVSRleeanSMLTKDIEILRRENEELTEKmkkaeeeyklekeeeisnlkaafEKNIN 993
Cdd:pfam07111  554 ---QQESTEEAASLRQELTQQQEIYGQ-----ALQEKVAEVETRLREQLSDT-----------------------KRRLN 602
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   994 TERTLKTQAVNKLAEIMNRKdfkiDRKKANTQDLRKKEKENRKlqlelnQEREKFNQMVVKHQKELNDMQAQLVEECAHR 1073
Cdd:pfam07111  603 EARREQAKAVVSLRQIQHRA----TQEKERNQELRRLQDEARK------EEGQRLARRVQELERDKNLMLATLQQEGLLS 672
                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 167887698  1074 NELQmqlaskesdiEQLRAKLLDLSDSTSVASFPSADET 1112
Cdd:pfam07111  673 RYKQ----------QRLLAVLPSGLDKKSVVSSPRPECS 701
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
485-966 9.16e-09

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 59.84  E-value: 9.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   485 EKEKMLlqhriNEYQRKAEQENEKRRNVENEVSTLKDQLeDLKKVSQNsqLANEKLSQLQKQLEEANDLLRTESDtavRL 564
Cdd:pfam10174  356 EKESFL-----NKKTKQLQDLTEEKSTLAGEIRDLKDML-DVKERKIN--VLQKKIENLQEQLRDKDKQLAGLKE---RV 424
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   565 RKSHTEMSKSISQLESLNRELQERNRILENSKSQTDKdyyqlqaileaERRDRGHDSEmigdlqaritSLQEEVKHLKHN 644
Cdd:pfam10174  425 KSLQTDSSNTDTALTTLEEALSEKERIIERLKEQRER-----------EDRERLEELE----------SLKKENKDLKEK 483
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   645 LEKVEGERKEAQDMLNHSEKEKNNLEIDLNYKLKSLQQrLEQEVNEHKVTKARLTDKHQSIEEAKSVAMCEMEkklkeer 724
Cdd:pfam10174  484 VSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKS-LEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPE------- 555
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   725 earekAENRVVQIEKQCSMLDVDLKQSQQKLEHLTGNKERMEDEvKNLTLQLEQESNKRLLLQneLKTQAFEADNLKGLE 804
Cdd:pfam10174  556 -----INDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENE-KNDKDKKIAELESLTLRQ--MKEQNKKVANIKHGQ 627
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   805 KQMKQEINTLLEAKRLLEFELAQLTKQYrgnegQMRELQDQLEaeqyfstlyktqvkelkeeieeknrenlKKIQELQNE 884
Cdd:pfam10174  628 QEMKKKGAQLLEEARRREDNLADNSQQL-----QLEELMGALE----------------------------KTRQELDAT 674
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   885 KETLA-TQLDLAETKAESEQLA---RGLLEEqYFELTQESKKAAsrnrqeITDKDHTVSRLEEANSMLTKDIE---ILRR 957
Cdd:pfam10174  675 KARLSsTQQSLAEKDGHLTNLRaerRKQLEE-ILEMKQEALLAA------ISEKDANIALLELSSSKKKKTQEevmALKR 747

                   ....*....
gi 167887698   958 ENEELTEKM 966
Cdd:pfam10174  748 EKDRLVHQL 756
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
74-278 1.04e-08

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general 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). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk 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: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 57.83  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEVQLVRHKSTRKVyAMKLLSKFEMIKRSDsafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd05148     6 EEFTLERKLGSGYFGEVWEGLWKNRVRV-AIKILKSDDLLKQQD---FQKEVQALKRLRHKHLISLFAVCSVGEPVYIIT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNydvPEKWAR------FYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmKMNKEG 227
Cdd:cd05148    82 ELMEKGSLLAFLRS---PEGQVLpvasliDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLA-RLIKED 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 167887698  228 MVRCDTAVGTPDYISPEVLksqgGDGYYGRECDWWSVGVFLYEMLV-GDTPF 278
Cdd:cd05148   158 VYLSSDKKIPYKWTAPEAA----SHGTFSTKSDVWSFGILLYEMFTyGQVPY 205
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
75-272 1.06e-08

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: 58.29  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSkFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRY--LYMV 152
Cdd:cd14049     7 EFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKIL-IKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTAWMEHVQlmLYIQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMP-------------GGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSG-HLKLADF 217
Cdd:cd14049    86 MQLCElslwdwivernkrPCEEEFKSAPYTpVDVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDiHVRIGDF 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167887698  218 G-TC----------MKMNKEGMVRCDTAVGTPDYISPEVLksQGGDgyYGRECDWWSVGVFLYEML 272
Cdd:cd14049   166 GlACpdilqdgndsTTMSRLNGLTHTSGVGTCLYAAPEQL--EGSH--YDFKSDMYSIGVILLELF 227
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
77-278 1.06e-08

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: 57.72  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   77 EVVKVIGRGAFGEVqlVRHKSTRKVyAMKLLSKFEMIKRSDSAFfweERDIMAFANSPWV-VQLFYAFQDDRYLYMVMEY 155
Cdd:cd14150     3 SMLKRIGTGSFGTV--FRGKWHGDV-AVKILKVTEPTPEQLQAF---KNEMQVLRKTRHVnILLFMGFMTRPNFAIITQW 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDL----------VNLMSNYDVPEKWARfytaevvlALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG-TCMKMN 224
Cdd:cd14150    77 CEGSSLyrhlhvtetrFDTMQLIDVARQTAQ--------GMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGlATVKTR 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 167887698  225 KEGMVRCDTAVGTPDYISPEVLKSQGGDGyYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd14150   149 WSGSQQVEQPSGSILWMAPEVIRMQDTNP-YSFQSDVYAYGVVLYELMSGTLPY 201
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
447-964 1.41e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 59.67  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  447 DEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKekmlLQHRINEYQRKAEQENEKRRNVENEVSTLKDQLEDL 526
Cdd:PRK02224  223 ERYEEQREQARETRDEADEVLEEHEERREELETLEAEIED----LRETIAETEREREELAEEVRDLRERLEELEEERDDL 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  527 KKVSQNSQLANEKLSQ----LQKQLEEANDLLRTESDTAVRLRKSHTEMSKSISQLESLNRELQERNRILEnsksqtdkd 602
Cdd:PRK02224  299 LAEAGLDDADAEAVEArreeLEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE--------- 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  603 yyqlqAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVEGERKEAQDMLNHSEKEKNNLEIDlnykLKSLQQ 682
Cdd:PRK02224  370 -----SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT----LRTARE 440
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  683 RLEQevNEHKVTKARLTDKHQSIEEAKSV-AMCEMEKKLKEEREAREKAENRVVQIEKQCSMLdVDLKQSQQKLEHLTGN 761
Cdd:PRK02224  441 RVEE--AEALLEAGKCPECGQPVEGSPHVeTIEEDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEER 517
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  762 KERMEDEVKNLTLQLEQESNKRLLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLEFELAQLtKQYRGNEGQMRE 841
Cdd:PRK02224  518 REDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAEL-KERIESLERIRT 596
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  842 LQDQLE-AEQYFSTLyktqvkelkeeieeknRENLKKIQELQNE-KETLAtqlDLAETKAESEqlarGLLEEQYFELTQE 919
Cdd:PRK02224  597 LLAAIAdAEDEIERL----------------REKREALAELNDErRERLA---EKRERKRELE----AEFDEARIEEARE 653
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 167887698  920 SKKAASRNRQEITDKdhtVSRLEEANSMLTKDIEILRRENEELTE 964
Cdd:PRK02224  654 DKERAEEYLEQVEEK---LDELREERDDLQAEIGAVENELEELEE 695
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
430-681 1.48e-08

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 59.36  E-value: 1.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   430 KTIYKLEEQLHNEMQL--------------KDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKEKMLLQHRI 495
Cdd:pfam15921  562 KVIEILRQQIENMTQLvgqhgrtagamqveKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAG 641
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   496 NEYQRKAEQENEKRRNVENEVSTLKDQL----EDLKKVSQNSQLANE-----------KLSQLQKQLEEANDLLRTESDT 560
Cdd:pfam15921  642 SERLRAVKDIKQERDQLLNEVKTSRNELnslsEDYEVLKRNFRNKSEemetttnklkmQLKSAQSELEQTRNTLKSMEGS 721
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   561 AVRLRKSHTEMSKSISQLESLNRELQERNRILENSKSQTDKDYYqlqaILEAERRDRGHD--------SEMIGDLQ---A 629
Cdd:pfam15921  722 DGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKH----FLKEEKNKLSQElstvatekNKMAGELEvlrS 797
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 167887698   630 RITSLQEEVKHLKHNLEKVEGERKEAQDMLNHSEKEKNNLEIDLNYKLKSLQ 681
Cdd:pfam15921  798 QERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
HR1 cd00089
Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small ...
489-554 1.62e-08

Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small GTPases; The HR1 domain, also called the ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. It is found in Rho effector proteins including PKC-related kinases such as vertebrate PRK1 (or PKN) and yeast PKC1 protein kinases C, as well as in rhophilins and Rho-associated kinase (ROCK). Rho family members function as molecular switches, cycling between inactive and active forms, controlling a variety of cellular processes. HR1 domains may occur in repeat arrangements (PKN contains three HR1 domains), separated by a short linker region.


Pssm-ID: 212008 [Multi-domain]  Cd Length: 68  Bit Score: 52.33  E-value: 1.62e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  489 MLLQHRINEYQRKAEQENEKRRNVENEVSTLKDQL--EDLKKVSQNSQLANEKLSQLQKQLEEANDLL 554
Cdd:cd00089     1 SKLQQRLEELRRKLEKELKIREGAENLLKLYSNPKvkKDLAEVQLNLKESKEKIDLLKRQLERYNALV 68
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
80-278 1.85e-08

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: 56.81  E-value: 1.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVqLVRHKSTRKVyAMKLLsKFEMIKRSdsafFWEERDIMAFANSPWVVQLFYAFQDDRyLYMVMEYMPGG 159
Cdd:cd05083    12 EIIGEGEFGAV-LQGEYMGQKV-AVKNI-KCDVTAQA----FLEETAVMTKLQHKNLVRLLGVILHNG-LYIVMELMSKG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DLVNLMSN---YDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGtcmkMNKEGMVRCDTAVG 236
Cdd:cd05083    84 NLVNFLRSrgrALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFG----LAKVGSMGVDNSRL 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 167887698  237 TPDYISPEVLKsqggDGYYGRECDWWSVGVFLYEML-VGDTPF 278
Cdd:cd05083   160 PVKWTAPEALK----NKKFSSKSDVWSYGVLLWEVFsYGRAPY 198
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
406-771 1.92e-08

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 58.88  E-value: 1.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   406 LSSANPNDNRTSSNADKSLQESlQKTIYKLEEQLHN-EMQLKDEMEQKCR--TSNIK--LDKIMKELDEEGNQRRN---- 476
Cdd:TIGR04523  258 LKDEQNKIKKQLSEKQKELEQN-NKKIKELEKQLNQlKSEISDLNNQKEQdwNKELKseLKNQEKKLEEIQNQISQnnki 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   477 ---LESTVSQIEKEKMLLQHRINEYQRKAEQENEKRRNVENEVSTLKDQLEDLK--------KVSQNSQLANEKLSQLQK 545
Cdd:TIGR04523  337 isqLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLEsqindlesKIQNQEKLNQQKDEQIKK 416
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   546 QLEEANDLLR----------TESDTAVRLRKSHTEMSKSISQLESLNRELQERNRILENSKSQTDKDYYQLQAILEAERR 615
Cdd:TIGR04523  417 LQQEKELLEKeierlketiiKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEK 496
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   616 DRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVEGERKEAQDMLNHSEKEKNNLEIDLNY-KLKSLQQRLEQEVNEHKVT 694
Cdd:TIGR04523  497 ELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKeNLEKEIDEKNKEIEELKQT 576
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   695 KARLTDKHQSIEE---AKSVAMCEMEKKLKEEREAREKAENRVVQIEKQCSMLDVDLKQSQQKLEHLTGNKERMEDEVKN 771
Cdd:TIGR04523  577 QKSLKKKQEEKQElidQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKE 656
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
78-279 1.95e-08

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: 57.00  E-value: 1.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   78 VVKVIGRGAFGEVQLVRHKSTRKVY---AMKLL-SKFEMIKRSDsafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 153
Cdd:cd05033     8 IEKVIGGGEFGEVCSGSLKLPGKKEidvAIKTLkSGYSDKQRLD---FLTEASIMGQFDHPNVIRLEGVVTKSRPVMIVT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  154 EYMPGGDLVNLMSNYDvpekwARFYTAEVVLALDAIHS-------MGFIHRDVKPDNMLLDKSGHLKLADFGTCMKM-NK 225
Cdd:cd05033    85 EYMENGSLDKFLREND-----GKFTVTQLVGMLRGIASgmkylseMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLeDS 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  226 EGMVrcDTAVG-TP-DYISPEVLKSQggdgYYGRECDWWSVGVFLYE-MLVGDTPFY 279
Cdd:cd05033   160 EATY--TTKGGkIPiRWTAPEAIAYR----KFTSASDVWSFGIVMWEvMSYGERPYW 210
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
80-278 2.19e-08

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl 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 its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl 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: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 56.94  E-value: 2.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEV---QLVRHKSTRKVyAMKLLsKFEMIKRSDSAFFWEERDIMAFANSPWVVQLF-YAFQD-DRYLY---- 150
Cdd:cd05075     6 KTLGEGEFGSVmegQLNQDDSVLKV-AVKTM-KIAICTRSEMEDFLSEAVCMKEFDHPNVMRLIgVCLQNtESEGYpspv 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGGDLVNLM-------SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKM 223
Cdd:cd05075    84 VILPFMKHGDLHSFLlysrlgdCPVYLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSKKI 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  224 NKEGMVRCDTAVGTP-DYISPEVLksqgGDGYYGRECDWWSVGVFLYEMLV-GDTPF 278
Cdd:cd05075   164 YNGDYYRQGRISKMPvKWIAIESL----ADRVYTTKSDVWSFGVTMWEIATrGQTPY 216
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
82-272 2.57e-08

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 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: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 57.25  E-value: 2.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMK----------LLSKFEMIK-------RSDsafFWEERDIMAFANSPWVVQLFYAFQ 144
Cdd:cd05096    13 LGEGQFGEVHLCEVVNPQDLPTLQfpfnvrkgrpLLVAVKILRpdanknaRND---FLKEVKILSRLKDPNIIRLLGVCV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  145 DDRYLYMVMEYMPGGDLVNLMSNYDVPEKWAR--------------------FYTAEVVLALDAIHSMGFIHRDVKPDNM 204
Cdd:cd05096    90 DEDPLCMITEYMENGDLNQFLSSHHLDDKEENgndavppahclpaisyssllHVALQIASGMKYLSSLNFVHRDLATRNC 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167887698  205 LLDKSGHLKLADFGTCMKMNKEGMVRCD-TAVGTPDYISPEVLKSqggdGYYGRECDWWSVGVFLYEML 272
Cdd:cd05096   170 LVGENLTIKIADFGMSRNLYAGDYYRIQgRAVLPIRWMAWECILM----GKFTTASDVWAFGVTLWEIL 234
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
77-278 2.60e-08

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: 56.65  E-value: 2.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   77 EVVKVIGRGAFGEVQLVRHKSTRKVyAMKLLSKFEMikrsDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYM 156
Cdd:cd05068    11 KLLRKLGSGQFGEVWEGLWNNTTPV-AVKTLKPGTM----DPEDFLREAQIMKKLRHPKLIQLYAVCTLEEPIYIITELM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  157 PGGDLVNLMSNYDVPEKWARF--YTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTA 234
Cdd:cd05068    86 KHGSLLEYLQGKGRSLQLPQLidMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVIKVEDEYEAREG 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 167887698  235 VGTP-DYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLV-GDTPF 278
Cdd:cd05068   166 AKFPiKWTAPEAANYNR----FSIKSDVWSFGILLTEIVTyGRIPY 207
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
639-1097 2.64e-08

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 58.59  E-value: 2.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   639 KHLKHNLEKVEGERKEAQDMLNHS----EKEKNNLE---IDLNYKLKSLQQRLEQEVNEHKvtkarltDKHQSIEEAKSv 711
Cdd:pfam15921   74 EHIERVLEEYSHQVKDLQRRLNESnelhEKQKFYLRqsvIDLQTKLQEMQMERDAMADIRR-------RESQSQEDLRN- 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   712 amcemekklkeereareKAENRVVQIEKQCSMLDVDLKQSQQKLEHLTG---NKERMEDEVKNLTLQLEQESNKRLLLQN 788
Cdd:pfam15921  146 -----------------QLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKmmlSHEGVLQEIRSILVDFEEASGKKIYEHD 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   789 ELKTQAFEA---------------------------DNLKGLEKQMKQEINTLLEA-----KRLL---EFELAQLTKQYR 833
Cdd:pfam15921  209 SMSTMHFRSlgsaiskilreldteisylkgrifpveDQLEALKSESQNKIELLLQQhqdriEQLIsehEVEITGLTEKAS 288
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   834 GNEGQMRELQDQLEAEQ---------YFSTL--YKTQVKELKEEIEEKNRENLKKIQELqnEKETLATQLDLAETKAESE 902
Cdd:pfam15921  289 SARSQANSIQSQLEIIQeqarnqnsmYMRQLsdLESTVSQLRSELREAKRMYEDKIEEL--EKQLVLANSELTEARTERD 366
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   903 QLAR--GLLEEQYFEL--------------TQESKKAASRN----------RQEITDKDHTVSRLE-------------- 942
Cdd:pfam15921  367 QFSQesGNLDDQLQKLladlhkrekelsleKEQNKRLWDRDtgnsitidhlRRELDDRNMEVQRLEallkamksecqgqm 446
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   943 --------------EANSMLTKDI----EILRRENEELTEKmkkaeEEYKLEKEEEISNLKAAFEknintERTLKTQAVN 1004
Cdd:pfam15921  447 erqmaaiqgkneslEKVSSLTAQLestkEMLRKVVEELTAK-----KMTLESSERTVSDLTASLQ-----EKERAIEATN 516
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  1005 klAEIMNRKDfKIDRKKANTQDLRKKEKENRKLQLE-----------------LNQEREKFNQMVVKHQKELNDMQ---A 1064
Cdd:pfam15921  517 --AEITKLRS-RVDLKLQELQHLKNEGDHLRNVQTEcealklqmaekdkvieiLRQQIENMTQLVGQHGRTAGAMQvekA 593
                          570       580       590
                   ....*....|....*....|....*....|....*..
gi 167887698  1065 QLVEECAHR----NELQMQLASKESDIEQLRAKLLDL 1097
Cdd:pfam15921  594 QLEKEINDRrlelQEFKILKDKKDAKIRELEARVSDL 630
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
413-1050 3.00e-08

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 58.44  E-value: 3.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   413 DNRTSSNADKSLQESLQKTIYKLEEQLHNEMQLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKEKMLLQ 492
Cdd:pfam02463  304 KLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES 383
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   493 HRINEYQRKAEQENEKRRNVENEVSTLKD---QLEDLKKVSQNSQLANEKLSQLQKQLEEANDLLRTESDTAVRLRKS-- 567
Cdd:pfam02463  384 ERLSSAAKLKEEELELKSEEEKEAQLLLElarQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLkd 463
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   568 HTEMSKSISQLESLNRELQERNRILENSKSQTDKDYYQLQAILEA----ERRDRGHDSEMIGDLQARITSLQE------- 636
Cdd:pfam02463  464 ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGlkvlLALIKDGVGGRIISAHGRLGDLGVavenykv 543
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   637 ---------------EVKHLKHNLEKVEGERKEAQDMLNHSEKEKNNLEIDLNYKLKSLQQRLEQEVNEHKVTKARLTDK 701
Cdd:pfam02463  544 aistavivevsatadEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAK 623
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   702 HQSIEEAKSVAMCEMEKKLKEEREAREKAENRVVQIEKQCSMLDVDLKQSQQKLEHLTGNKERMEDEVKNLTLQLEQESN 781
Cdd:pfam02463  624 VVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK 703
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   782 KRLLLQNELKTQAFEADNLKgLEKQMKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMRELQDQLEAEQYFSTLYKTQVK 861
Cdd:pfam02463  704 KEQREKEELKKLKLEAEELL-ADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREK 782
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   862 ELKEEIEEKNRENLKKIQE--------------LQNEKETLATQLDLAETKAESEQLARGLLEEQYFELTQESKKAASRN 927
Cdd:pfam02463  783 TEKLKVEEEKEEKLKAQEEelraleeelkeeaeLLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEE 862
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   928 RQEITDKDHTVSRLEEANSMLTKDIEILRRENEELTEKMKKAEEEYKLEKEEEIS------------------------- 982
Cdd:pfam02463  863 ITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENeieerikeeaeillkyeeepeelll 942
                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167887698   983 ---NLKAAFEKNINTERTLKTQAVNKLAE-----IMNRKDFKIDRKKANTQDL---RKKEKENRKLQLELNQEREKFNQ 1050
Cdd:pfam02463  943 eeaDEKEKEENNKEEEEERNKRLLLAKEElgkvnLMAIEEFEEKEERYNKDELekeRLEEEKKKLIRAIIEETCQRLKE 1021
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
76-278 3.22e-08

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; 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. Mutations in TTBK2 is associated with the development of spinocerebellar ataxia type 11, belonging to a group of neurodegenerative disorders characterized by progressive incoordination, dysarthria and impairment of eye movements. Brain tissues of SCA11 patients show the presence of neurofibrillary tangles and tau deposition in the brain, similar to Alzheimer's disease (AD) patients. The TTBK2 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: 271031 [Multi-domain]  Cd Length: 262  Bit Score: 56.21  E-value: 3.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLlskfEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEy 155
Cdd:cd14129     2 WKVLRKIGGGGFGEIYDALDLLTRENVALKV----ESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNDRFNYVVMQ- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVNLMSNydvpEKWARFYTA-------EVVLALDAIHSMGFIHRDVKPDNMLLDK----SGHLKLADFGTCMKM- 223
Cdd:cd14129    77 LQGRNLADLRRS----QSRGTFTISttlrlgrQILESIESIHSVGFLHRDIKPSNFAMGRfpstCRKCYMLDFGLARQFt 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 167887698  224 NKEGMVRCDTAV----GTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd14129   153 NSCGDVRPPRAVagfrGTVRYASINAHRNR----EMGRHDDLWSLFYMLVEFVVGQLPW 207
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
80-292 3.23e-08

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: 56.72  E-value: 3.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQ------LVRHKSTRKVyAMKLLSkfEMIKRSDSAFFWEERDIMA-FANSPWVVQLFYAFQDDRYLYMV 152
Cdd:cd05055    41 KTLGAGAFGKVVeataygLSKSDAVMKV-AVKMLK--PTAHSSEREALMSELKIMShLGNHENIVNLLGACTIGGPILVI 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGGDLVNLMSNYDvpEKWARF-----YTAEVVLALDAIHSMGFIHRDVKPDNMLLdKSGHL-KLADFGTCMK-MNK 225
Cdd:cd05055   118 TEYCCYGDLLNFLRRKR--ESFLTLedllsFSYQVAKGMAFLASKNCIHRDLAARNVLL-THGKIvKICDFGLARDiMND 194
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  226 EGMVRCDTAVGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLYEML-VGDTPfYADSLVGT--YSKIMN 292
Cdd:cd05055   195 SNYVVKGNARLPVKWMAPESIF----NCVYTFESDVWSYGILLWEIFsLGSNP-YPGMPVDSkfYKLIKE 259
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
536-782 3.34e-08

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 57.47  E-value: 3.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  536 ANEKLSQLQKQLEEANDllrtesdtavRLRKSHTEMSKSISQLESLNRELQERNRILENSKSQtdkdyyqlqaILEAERR 615
Cdd:COG4942    25 AEAELEQLQQEIAELEK----------ELAALKKEEKALLKQLAALERRIAALARRIRALEQE----------LAALEAE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  616 drghdsemIGDLQARITSLQEEVKHLKHNLEKV-----EGERKEAQDMLNHSEkEKNNLEIDLNYkLKSLQQRLEQEVNE 690
Cdd:COG4942    85 --------LAELEKEIAELRAELEAQKEELAELlralyRLGRQPPLALLLSPE-DFLDAVRRLQY-LKYLAPARREQAEE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  691 HKVTKARLTDKHQSIEEAKSvamcEMEKKLKEEREAREKAENRVVQIEKQCSMLDVDLKQSQQKLEHLTGNKERMEDEVK 770
Cdd:COG4942   155 LRADLAELAALRAELEAERA----ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
                         250
                  ....*....|..
gi 167887698  771 NLTLQLEQESNK 782
Cdd:COG4942   231 RLEAEAAAAAER 242
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
148-289 3.41e-08

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: 56.80  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  148 YLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH---LKLADFG---TC- 220
Cdd:cd13977   109 YLWFVMEFCDGGDMNEYLLSRRPDRQTNTSFMLQLSSALAFLHRNQIVHRDLKPDNILISHKRGepiLKVADFGlskVCs 188
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  221 -MKMNKEGMV-----RCDTAVGTPDYISPEVLksqggDGYYGRECDWWSVGVFLYEMLVGDTPFYADS---LVGTYSK 289
Cdd:cd13977   189 gSGLNPEEPAnvnkhFLSSACGSDFYMAPEVW-----EGHYTAKADIFALGIIIWAMVERITFRDGETkkeLLGTYIQ 261
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
60-282 3.64e-08

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 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 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 Jak1 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: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 56.48  E-value: 3.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   60 KDTINKIRDLrmkaedyevvkviGRGAFGEVQLVRHK----STRKVYAMKLLSKFEmiKRSDSAFFWEERDIMAFANSPW 135
Cdd:cd05079     3 KRFLKRIRDL-------------GEGHFGKVELCRYDpegdNTGEQVAVKSLKPES--GGNHIADLKKEIEILRNLYHEN 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  136 VVQLFYAFQDD--RYLYMVMEYMPGGDLVNLM--SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH 211
Cdd:cd05079    68 IVKYKGICTEDggNGIKLIMEFLPSGSLKEYLprNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167887698  212 LKLADFG--TCMKMNKEGMVRCDTAVGTPDYISPEVLKSQggdGYYgRECDWWSVGVFLYEMLVgdtpfYADS 282
Cdd:cd05079   148 VKIGDFGltKAIETDKEYYTVKDDLDSPVFWYAPECLIQS---KFY-IASDVWSFGVTLYELLT-----YCDS 211
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
621-964 3.70e-08

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 58.16  E-value: 3.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   621 SEMIGDLQARITSLQEEVKHLKHNLEKVEGERKEAQDMLNHSEKEKNNLEIDLNY----------KLKSLQQRLEQEVNE 690
Cdd:TIGR02169  680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKlkerleeleeDLSSLEQEIENVKSE 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   691 HKVTKARLTDKHQSIEEAKSvAMCEMEKKLKEEREAREKAENRvvQIEKQCSMLDVDLKQSQQKLEHLTGNKERMEDEVK 770
Cdd:TIGR02169  760 LKELEARIEELEEDLHKLEE-ALNDLEARLSHSRIPEIQAELS--KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   771 NLTlqleqesNKRLLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMRELQ---DQLE 847
Cdd:TIGR02169  837 ELQ-------EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELErkiEELE 909
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   848 AEqyfstlyktqvkelkeeieeknRENLKKIQELQNEK-ETLATQLD-LAETKAE-----SEQLARGLLEEQYFELTQES 920
Cdd:TIGR02169  910 AQ----------------------IEKKRKRLSELKAKlEALEEELSeIEDPKGEdeeipEEELSLEDVQAELQRVEEEI 967
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 167887698   921 KKAASRNRQEITDKDHTVSRLEEansmLTKDIEILRRENEELTE 964
Cdd:TIGR02169  968 RALEPVNMLAIQEYEEVLKRLDE----LKEKRAKLEEERKAILE 1007
C1_p190RhoGEF-like cd20815
protein kinase C conserved region 1 (C1 domain) found in the 190 kDa guanine nucleotide ...
1227-1273 3.75e-08

protein kinase C conserved region 1 (C1 domain) found in the 190 kDa guanine nucleotide exchange factor (p190RhoGEF)-like family; The p190RhoGEF-like protein family includes p190RhoGEF, Rho guanine nucleotide exchange factor 2 (ARHGEF2), A-kinase anchor protein 13 (AKAP-13) and similar proteins. p190RhoGEF is a brain-enriched, RhoA-specific guanine nucleotide exchange factor that regulates signaling pathways downstream of integrins and growth factor receptors. It is involved in axonal branching, synapse formation and dendritic morphogenesis, as well as in focal adhesion formation, cell motility and B-lymphocytes activation. ARHGEF2 acts as a guanine nucleotide exchange factor (GEF) that activates Rho-GTPases by promoting the exchange of GDP for GTP. It is thought to play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. AKAP-13 is a scaffold protein that plays an important role in assembling signaling complexes downstream of several types of G protein-coupled receptors. It activates RhoA in response to signaling via G protein-coupled receptors via its function as Rho guanine nucleotide exchange factor. It may also activate other Rho family members. AKAP-13 plays a role in cell growth, cell development and actin fiber formation. Members of this family share a common domain architecture containing C1, RhoGEF or Dbl-homologous (DH), and Pleckstrin Homology (PH) domains. Some members may contain additional domains such as the DUF5401 domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410365  Cd Length: 54  Bit Score: 50.88  E-value: 3.75e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 167887698 1227 KGHEFIPTLYHFPANCDACAKPLwhvfKPPPALECRRCHVKCH----RDHL 1273
Cdd:cd20815     2 NTHQFVPVSFSNSTKCDVCSKPL----TNKPALQCENCSVNVHdsscKDQL 48
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
74-278 4.24e-08

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. 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 serine/threonine residues. The CLK2 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: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 56.56  E-value: 4.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   74 EDYEVVKVIGRGAFGEV-QLVRHKSTRKVYAMKLLSKFEMIKRSD--SAFFWEERDIMAFANSPWVVQLFYAFQDDRYLY 150
Cdd:cd14215    12 ERYEIVSTLGEGTFGRVvQCIDHRRGGARVALKIIKNVEKYKEAArlEINVLEKINEKDPENKNLCVQMFDWFDYHGHMC 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGGDLVNLMSN--YDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD-------------------KS 209
Cdd:cd14215    92 ISFELLGLSTFDFLKENnyLPYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVnsdyeltynlekkrdersvKS 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167887698  210 GHLKLADFGTCMKMNKEGmvrcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd14215   172 TAIRVVDFGSATFDHEHH----STIVSTRHYRAPEVILELG----WSQPCDVWSIGCIIFEYYVGFTLF 232
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
80-271 5.93e-08

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: 55.37  E-value: 5.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRKVyAMKLLSKFEMikrsDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 159
Cdd:cd05034     1 KKLGAGQFGEVWMGVWNGTTKV-AVKTLKPGTM----SPEAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DLVNLMSNYDvpEKWARFYT-----AEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG-TCMKMNKEGMVRCDT 233
Cdd:cd05034    76 SLLDYLRTGE--GRALRLPQlidmaAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGlARLIEDDEYTAREGA 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 167887698  234 AVgtP-DYISPEVLKsqggdgyYGR---ECDWWSVGVFLYEM 271
Cdd:cd05034   154 KF--PiKWTAPEAAL-------YGRftiKSDVWSFGILLYEI 186
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
444-655 6.51e-08

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 56.31  E-value: 6.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  444 QLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKEKMLLQHRINEYQRKAEQENEKRRNVENEVSTLKDQL 523
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  524 EDLKKV--------SQNSQLANEKLSQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSISQLESLNRELQERNRILENS 595
Cdd:COG4942   100 EAQKEElaellralYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  596 KSQTDKDYYQLQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVEGERKEA 655
Cdd:COG4942   180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
82-278 6.64e-08

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: 55.46  E-value: 6.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVyAMKLLSKFEMikrSDSAFFwEERDIMAFANSPWVVQLfYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd05071    17 LGQGCFGEVWMGTWNGTTRV-AIKTLKPGTM---SPEAFL-QEAQVMKKLRHEKLVQL-YAVVSEEPIYIVTEYMSKGSL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNYdvPEKWARF-----YTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVG 236
Cdd:cd05071    91 LDFLKGE--MGKYLRLpqlvdMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKF 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 167887698  237 TPDYISPEVlksqggdGYYGR---ECDWWSVGVFLYEMLV-GDTPF 278
Cdd:cd05071   169 PIKWTAPEA-------ALYGRftiKSDVWSFGILLTELTTkGRVPY 207
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
185-278 7.66e-08

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: 55.42  E-value: 7.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  185 ALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG-TCMKMNKEGMVRCDTAVGTPDYISPEVLKSQGGDGyYGRECDWWS 263
Cdd:cd14149   120 GMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGlATVKSRWSGSQQVEQPTGSILWMAPEVIRMQDNNP-FSFQSDVYS 198
                          90
                  ....*....|....*
gi 167887698  264 VGVFLYEMLVGDTPF 278
Cdd:cd14149   199 YGIVLYELMTGELPY 213
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
442-966 8.77e-08

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 57.11  E-value: 8.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   442 EMQLKDEMEQKCRTSNIKLDKIMKELDEEGNQ---RRNLESTVSQIEKE---------------KMLLQHRINEYQRKAE 503
Cdd:pfam01576    6 EMQAKEEELQKVKERQQKAESELKELEKKHQQlceEKNALQEQLQAETElcaeaeemrarlaarKQELEEILHELESRLE 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   504 QENEKRRNVENEVSTLKDQLEDLKKVSQNSQLANEKLsQLQKQLEEA------NDLLRTEsDTAVRLRKSHTEMSKSISQ 577
Cdd:pfam01576   86 EEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKL-QLEKVTTEAkikkleEDILLLE-DQNSKLSKERKLLEERISE 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   578 LESLNRELQERNRILENSKSQTDKDYYQLQAIL--------EAERRDRGHDSEmIGDLQARITSLQEEVKHLKHNLEKVE 649
Cdd:pfam01576  164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLkkeekgrqELEKAKRKLEGE-STDLQEQIAELQAQIAELRAQLAKKE 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   650 GERKEAQDMLNHSEKEKNNLEI---DLNYKLKSLQQRLEQEvnehKVTKARLTDKHQSIEEAKSVAMCEMEKKLKEEREA 726
Cdd:pfam01576  243 EELQAALARLEEETAQKNNALKkirELEAQISELQEDLESE----RAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQ 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   727 REKAENRVVQIEKQCSMLDVDLKQSQQKLEHLtgnKERMEDEVKNLTLQLEQEsnKRLLLQNELKTQAFEADNlkgleKQ 806
Cdd:pfam01576  319 QELRSKREQEVTELKKALEEETRSHEAQLQEM---RQKHTQALEELTEQLEQA--KRNKANLEKAKQALESEN-----AE 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   807 MKQEINTLLEAK-------RLLEFELAQLTKQYRGNEGQMRELQDQL---------------EAEQYFSTLYK------T 858
Cdd:pfam01576  389 LQAELRTLQQAKqdsehkrKKLEGQLQELQARLSESERQRAELAEKLsklqselesvssllnEAEGKNIKLSKdvssleS 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   859 QVKELKEEIEEKNRENLK---KIQELQNEKETLATQLdlaetkaESEQLARGLLEEQYFELTQEskkaASRNRQEITDKD 935
Cdd:pfam01576  469 QLQDTQELLQEETRQKLNlstRLRQLEDERNSLQEQL-------EEEEEAKRNVERQLSTLQAQ----LSDMKKKLEEDA 537
                          570       580       590
                   ....*....|....*....|....*....|.
gi 167887698   936 HTVSRLEEANSMLTKDIEILRRENEELTEKM 966
Cdd:pfam01576  538 GTLEALEEGKKRLQRELEALTQQLEEKAAAY 568
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
876-1146 1.47e-07

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 55.16  E-value: 1.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  876 KKIQELQNEKETLATQLDLAETKAESEQLARGLLEEQYFELTQESKKAASRNR---QEITDKDHTVSRLEEANSMLTKDI 952
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRaleQELAALEAELAELEKEIAELRAEL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  953 EILRRENEELTEKMKKAEEEYKLEKEEEISNLKAAFEKNINTERTlkTQAVNKLAEIMNRKDFKIDRKKantQDLRKKEK 1032
Cdd:COG4942   100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL--APARREQAEELRADLAELAALR---AELEAERA 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698 1033 ENRKLQLELNQEREKFNQMVVKHQKELNDMQAQLVEECAHRNELQMQLASKESDIEQLRAKLLDLSDSTSVASFPSAdet 1112
Cdd:COG4942   175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL--- 251
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 167887698 1113 DGNLPesriegWlsvPNRGNI-KRYGWKKQYVVVS 1146
Cdd:COG4942   252 KGKLP------W---PVSGRVvRRFGERDGGGGRN 277
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
76-274 1.49e-07

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 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: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 54.92  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVqlVR-HKSTR--KVYAMKLLSKFEMIKRSDSaffwEERDIMAFANSP------WVVQLFYAFQDD 146
Cdd:cd14135     2 YRVYGYLGKGVFSNV--VRaRDLARgnQEVAIKIIRNNELMHKAGL----KELEILKKLNDAdpddkkHCIRLLRHFEHK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  147 RYLYMVMEYMPggdlvnlMSNYDVPEKWA----------RFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH-LKLA 215
Cdd:cd14135    76 NHLCLVFESLS-------MNLREVLKKYGknvglnikavRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNtLKLC 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  216 DFGTCMKMNKEGMvrcdtavgTPD-----YISPEVLKsqggdGY-YGRECDWWSVGVFLYEMLVG 274
Cdd:cd14135   149 DFGSASDIGENEI--------TPYlvsrfYRAPEIIL-----GLpYDYPIDMWSVGCTLYELYTG 200
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
80-278 1.55e-07

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: 54.64  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   80 KVIGRGAFGEVQLVRHKSTRK-------VYAMKLLsKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMV 152
Cdd:cd05101    30 KPLGEGCFGQVVMAEAVGIDKdkpkeavTVAVKML-KDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVI 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGGDLVNLMS---------NYD---VPEKWARFY-----TAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLA 215
Cdd:cd05101   109 VEYASKGNLREYLRarrppgmeySYDinrVPEEQMTFKdlvscTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIA 188
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  216 DFGTCMKMNKEGMVRCDTAVGTP-DYISPEVLKsqggDGYYGRECDWWSVGVFLYEML-VGDTPF 278
Cdd:cd05101   189 DFGLARDINNIDYYKKTTNGRLPvKWMAPEALF----DRVYTHQSDVWSFGVLMWEIFtLGGSPY 249
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
450-990 1.78e-07

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 55.90  E-value: 1.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   450 EQKCRTSNIKLDKIMKELdEEGNQRRNLESTVS------QIEKEKML-LQHRINEYQrkaEQENEKRrnvenevSTLKDQ 522
Cdd:pfam05557    6 ESKARLSQLQNEKKQMEL-EHKRARIELEKKASalkrqlDRESDRNQeLQKRIRLLE---KREAEAE-------EALREQ 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   523 LEDLKKVSQNSQLANEKLSQLQKQLEEANDLLRTESDtavRLRKSHTEMSKSISQLESLNRELQERNRILENSKsQTDKD 602
Cdd:pfam05557   75 AELNRLKKKYLEALNKKLNEKESQLADAREVISCLKN---ELSELRRQIQRAELELQSTNSELEELQERLDLLK-AKASE 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   603 YYQLQAILEAERRDRGHDSEMIGDLQARI---TSLQEEVKHLKHNLEKV---EGERKEAQDMLNHSEKEKNNLEIdLNYK 676
Cdd:pfam05557  151 AEQLRQNLEKQQSSLAEAEQRIKELEFEIqsqEQDSEIVKNSKSELARIpelEKELERLREHNKHLNENIENKLL-LKEE 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   677 LKSLQQRLEQEvNEHKVTKARLTDKHQSIE-EAKSVAMCEMEKKLkeEREAREKAENRVVQIEKQCSMLDVDLKQSQQKL 755
Cdd:pfam05557  230 VEDLKRKLERE-EKYREEAATLELEKEKLEqELQSWVKLAQDTGL--NLRSPEDLSRRIEQLQQREIVLKEENSSLTSSA 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   756 EHLTGNKERMEDEVKNLTLQLEQESNKR-------LLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLE--FELA 826
Cdd:pfam05557  307 RQLEKARRELEQELAQYLKKIEDLNKKLkrhkalvRRLQRRVLLLTKERDGYRAILESYDKELTMSNYSPQLLEriEEAE 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   827 QLTKQYRGNEGQMRELQDQLEAEqyfSTLYKTQVKELKEEIEeknrenLKKIQELQNEKETLATQLDLAETKAESEQLAR 906
Cdd:pfam05557  387 DMTQKMQAHNEEMEAQLSVAEEE---LGGYKQQAQTLERELQ------ALRQQESLADPSYSKEEVDSLRRKLETLELER 457
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   907 GLLEEQYFELtqESKKAASRNRQEITDKDHTVSRLE-----EANSMLTKDIEILRRENEELTEKMKKAEEEYKLEKEEEI 981
Cdd:pfam05557  458 QRLREQKNEL--EMELERRCLQGDYDPKKTKVLHLSmnpaaEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPE 535

                   ....*....
gi 167887698   982 SNLKAAFEK 990
Cdd:pfam05557  536 TTSTMNFKE 544
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
79-272 1.86e-07

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 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 tyr kinase catalytic 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 Tyk2 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: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 54.14  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   79 VKVIGRGAFGEVQLVRH----KSTRKVYAMKLLsKFEMIKRSDSAFFwEERDIMAFANSPWVVQL--FYAFQDDRYLYMV 152
Cdd:cd05080     9 IRDLGEGHFGKVSLYCYdptnDGTGEMVAVKAL-KADCGPQHRSGWK-QEIDILKTLYHENIVKYkgCCSEQGGKSLQLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  153 MEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmKMNKEG--MVR 230
Cdd:cd05080    87 MEYVPLGSLRDYLPKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLA-KAVPEGheYYR 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 167887698  231 CDTAVGTPDY-ISPEVLKsqggDGYYGRECDWWSVGVFLYEML 272
Cdd:cd05080   166 VREDGDSPVFwYAPECLK----EYKFYYASDVWSFGVTLYELL 204
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
71-282 2.40e-07

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk 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: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 54.01  E-value: 2.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   71 MKAEDYEVVKVIGRGAFGEVQL-----VRHKSTRKVYAMKLLSkfEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQD 145
Cdd:cd05049     2 IKRDTIVLKRELGEGAFGKVFLgecynLEPEQDKMLVAVKTLK--DASSPDARKDFEREAELLTNLQHENIVKFYGVCTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  146 DRYLYMVMEYMPGGDLVNLMSNYDvPEkwARFYTAE------------------VVLALDAIHSMGFIHRDVKPDNMLLD 207
Cdd:cd05049    80 GDPLLMVFEYMEHGDLNKFLRSHG-PD--AAFLASEdsapgeltlsqllhiavqIASGMVYLASQHFVHRDLATRNCLVG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  208 KSGHLKLADFGtcmkMNKEgmvrcdtaVGTPDY-------------ISPEVLKsqggdgyYGR---ECDWWSVGVFLYEM 271
Cdd:cd05049   157 TNLVVKIGDFG----MSRD--------IYSTDYyrvgghtmlpirwMPPESIL-------YRKfttESDVWSFGVVLWEI 217
                         250
                  ....*....|..
gi 167887698  272 LV-GDTPFYADS 282
Cdd:cd05049   218 FTyGKQPWFQLS 229
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
77-278 2.58e-07

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: 54.11  E-value: 2.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   77 EVVKVIGRG--AFGEVQLVRHKSTRKVYAMKLlSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVME 154
Cdd:cd08226     1 ELQVELGKGfcNLTSVYLARHTPTGTLVTVKI-TNLDNCSEEHLKALQNEVVLSHFFRHPNIMTHWTVFTEGSWLWVISP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  155 YMPGGDLVNLMSNY---DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMvRC 231
Cdd:cd08226    80 FMAYGSARGLLKTYfpeGMNEALIGNILYGAIKALNYLHQNGCIHRSVKASHILISGDGLVSLSGLSHLYSMVTNGQ-RS 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 167887698  232 DTAVGTPDY-------ISPEVLKsQGGDGyYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd08226   159 KVVYDFPQFstsvlpwLSPELLR-QDLHG-YNVKSDIYSVGITACELARGQVPF 210
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
76-278 2.80e-07

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; 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. Genetic variations in TTBK1 are linked to Alzheimer's disease (AD). Hyperphosphorylated tau is a major component of paired helical filaments that accumulate in the brain of AD patients. Studies in transgenic mice show that TTBK1 is involved in the phosphorylation-dependent pathogenic aggregation of tau. The TTBK1 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: 271032 [Multi-domain]  Cd Length: 262  Bit Score: 53.49  E-value: 2.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLlskfEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEy 155
Cdd:cd14130     2 WKVLKKIGGGGFGEIYEAMDLLTRENVALKV----ESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQ- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGGDLVNLMSNYdvPEKWARFYTA-----EVVLALDAIHSMGFIHRDVKPDNMLLDK--SGHLK--LADFGTCMK-MNK 225
Cdd:cd14130    77 LQGRNLADLRRSQ--PRGTFTLSTTlrlgkQILESIEAIHSVGFLHRDIKPSNFAMGRlpSTYRKcyMLDFGLARQyTNT 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  226 EGMVRCDTAV----GTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd14130   155 TGEVRPPRNVagfrGTVRYASVNAHKNR----EMGRHDDLWSLFYMLVEFAVGQLPW 207
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
181-244 2.86e-07

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 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: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 53.98  E-value: 2.86e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887698  181 EVVLALDAIHSMGFIHRDVKPDNMLL-DKSGHLKLADFGT----CMKMN---KEGMVrcdtavgTPDYISPE 244
Cdd:cd14013   128 QILVALRKLHSTGIVHRDVKPQNIIVsEGDGQFKIIDLGAaadlRIGINyipKEFLL-------DPRYAPPE 192
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
121-282 2.96e-07

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 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: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 53.86  E-value: 2.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  121 FWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL------------VNLMSNYDVPEKWARFY------TAEV 182
Cdd:cd05090    54 FQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMNQGDLheflimrsphsdVGCSSDEDGTVKSSLDHgdflhiAIQI 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  183 VLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTP-DYISPEVLKSqggdGYYGRECDW 261
Cdd:cd05090   134 AAGMEYLSSHFFVHKDLAARNILVGEQLHVKISDLGLSREIYSSDYYRVQNKSLLPiRWMPPEAIMY----GKFSSDSDI 209
                         170       180
                  ....*....|....*....|..
gi 167887698  262 WSVGVFLYEML-VGDTPFYADS 282
Cdd:cd05090   210 WSFGVVLWEIFsFGLQPYYGFS 231
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
82-290 3.09e-07

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl 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: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 53.19  E-value: 3.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSdsafFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 161
Cdd:cd05052    14 LGGGQYGEVYEGVWKKYNLTVAVKTLKEDTMEVEE----FLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYGNL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  162 VNLMSNYDVPEKWA--RFYTA-EVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTP 238
Cdd:cd05052    90 LDYLRECNREELNAvvLLYMAtQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPI 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  239 DYISPEVLksqggdGYY--GRECDWWSVGVFLYEMLV-GDTPFYADSLVGTYSKI 290
Cdd:cd05052   170 KWTAPESL------AYNkfSIKSDVWAFGVLLWEIATyGMSPYPGIDLSQVYELL 218
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
185-278 3.55e-07

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: 53.53  E-value: 3.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  185 ALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG-TCMKMNKEGMVRCDTAVGTPDYISPEVLKSQGGDGyYGRECDWWS 263
Cdd:cd14151   116 GMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGlATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNP-YSFQSDVYA 194
                          90
                  ....*....|....*
gi 167887698  264 VGVFLYEMLVGDTPF 278
Cdd:cd14151   195 FGIVLYELMTGQLPY 209
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
79-272 3.86e-07

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: 53.48  E-value: 3.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   79 VKVIGRGAFGEVQLVRHK----STRKVYAMKLLSKFEMIKRSDsafFWEERDIMAFANSPWVVQ---LFYAfQDDRYLYM 151
Cdd:cd14205     9 LQQLGKGNFGSVEMCRYDplqdNTGEVVAVKKLQHSTEEHLRD---FEREIEILKSLQHDNIVKykgVCYS-AGRRNLRL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  152 VMEYMPGGDLVNLMSNYD--VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG--TCMKMNKEG 227
Cdd:cd14205    85 IMEYLPYGSLRDYLQKHKerIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGltKVLPQDKEY 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 167887698  228 MVRCDTAVGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLYEML 272
Cdd:cd14205   165 YKVKEPGESPIFWYAPESLT----ESKFSVASDVWSFGVVLYELF 205
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
82-278 4.29e-07

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: 53.08  E-value: 4.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   82 IGRGAFGEV-QLVRHKSTRKVYAMKLLSKfeMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQD----DRYLYMVMEYM 156
Cdd:cd14033     9 IGRGSFKTVyRGLDTETTVEVAWCELQTR--KLSKGERQRFSEEVEMLKGLQHPNIVRFYDSWKStvrgHKCIILVTELM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  157 PGGDLVNLMSNY-----DVPEKWARfytaEVVLALDAIHSMG--FIHRDVKPDNMLLD-KSGHLKLADFGTCMkMNKEGM 228
Cdd:cd14033    87 TSGTLKTYLKRFremklKLLQRWSR----QILKGLHFLHSRCppILHRDLKCDNIFITgPTGSVKIGDLGLAT-LKRASF 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 167887698  229 VRcdTAVGTPDYISPEVLKSQggdgyYGRECDWWSVGVFLYEMLVGDTPF 278
Cdd:cd14033   162 AK--SVIGTPEFMAPEMYEEK-----YDEAVDVYAFGMCILEMATSEYPY 204
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
76-222 4.35e-07

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; 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. CK1alpha plays a role in cell cycle progression, spindle dynamics, and chromosome segregation. It is also involved in regulating apoptosis mediated by Fas or the retinoid X receptor (RXR), and is a positive regulator of Wnt signaling. CK1alpha phosphorylates the NS5A protein of flaviviruses such as the Hepatitis C virus (HCV) and yellow fever virus (YFV), and influences flaviviral replication. The CK1 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: 271030 [Multi-domain]  Cd Length: 266  Bit Score: 52.89  E-value: 4.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLlskfEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 155
Cdd:cd14128     2 YRLVRKIGSGSFGDIYLGINITNGEEVAVKL----ESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  156 MPGG--DLVNLMSnydvpekwaRFYTAEVVLAL--------DAIHSMGFIHRDVKPDNMLLDKSGH---LKLADFGTCMK 222
Cdd:cd14128    78 LGPSleDLFNFCS---------RRFTMKTVLMLadqmigriEYVHNKNFIHRDIKPDNFLMGIGRHcnkLFLIDFGLAKK 148
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
75-279 4.56e-07

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk 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: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 53.30  E-value: 4.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   75 DYEVVKVIGRGAFGEVQLVRHKSTRKvYAMKLLSKFEMIKRSDSAF----FWEERDIMAFANSPWVVQLFYAFQDDRYLY 150
Cdd:cd05050     6 NIEYVRDIGQGAFGRVFQARAPGLLP-YEPFTMVAVKMLKEEASADmqadFQREAALMAEFDHPNIVKLLGVCAVGKPMC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  151 MVMEYMPGGDLVNL---MSNYDVPE-----KWARFY---------TAEVVLALDAIHSMG------FIHRDVKPDNMLLD 207
Cdd:cd05050    85 LLFEYMAYGDLNEFlrhRSPRAQCSlshstSSARKCglnplplscTEQLCIAKQVAAGMAylserkFVHRDLATRNCLVG 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  208 KSGHLKLADFGTCMKMNKEGMVRCDTAVGTP-DYISPEVLksqggdgYYGR---ECDWWSVGVFLYEML-VGDTPFY 279
Cdd:cd05050   165 ENMVVKIADFGLSRNIYSADYYKASENDAIPiRWMPPESI-------FYNRyttESDVWAYGVVLWEIFsYGMQPYY 234
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
149-271 5.45e-07

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, 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, like BMPR1, 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 BMPR1 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: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 52.86  E-value: 5.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  149 LYMVMEYMPGGDLVN-LMSNYDVPEKWARF-YTAEVVLAldAIHSMGF--------IHRDVKPDNMLLDKSGHLKLADFG 218
Cdd:cd14144    68 LYLITDYHENGSLYDfLRGNTLDTQSMLKLaYSAACGLA--HLHTEIFgtqgkpaiAHRDIKSKNILVKKNGTCCIADLG 145
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 167887698  219 TCMKMNKEGM---VRCDTAVGTPDYISPEVLKSQGGDGYYG--RECDWWSVGVFLYEM 271
Cdd:cd14144   146 LAVKFISETNevdLPPNTRVGTKRYMAPEVLDESLNRNHFDayKMADMYSFGLVLWEI 203
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
182-285 5.47e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 53.46  E-value: 5.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  182 VVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG-TCMKMNKEGMvRCDTAVGTPDYISPEVLKSQGgdgyYGRECD 260
Cdd:PHA03212  191 VLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGaACFPVDINAN-KYYGWAGTIATNAPELLARDP----YGPAVD 265
                          90       100
                  ....*....|....*....|....*.
gi 167887698  261 WWSVGVFLYEMLVG-DTPFYADSLVG 285
Cdd:PHA03212  266 IWSAGIVLFEMATChDSLFEKDGLDG 291
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
503-1094 5.74e-07

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 54.28  E-value: 5.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   503 EQENEKRRNVENEVSTLKDQLEDLKKVSQNSQLANEKLSQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSISQLESLN 582
Cdd:TIGR00606  213 KQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKM 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   583 REL-----QERNRILENSKSQT---DKDYYQLQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVEGERKE 654
Cdd:TIGR00606  293 EKVfqgtdEQLNDLYHNHQRTVrekERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQS 372
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   655 AQdmlNHSEKEKNNLEIDLNYKLKSLQQRLEQEVNEHKVTKARLTDKHQSIEEAKSVAMCEMEKKLkeeREAREKAENRV 734
Cdd:TIGR00606  373 LA---TRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEK---KGLGRTIELKK 446
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   735 VQIEKQCSMLDVDLKQSQQklehLTGNKERMEDEVKNLTL------QLEQESNKRLLLQNELKTQAFEADNLKGLEK--- 805
Cdd:TIGR00606  447 EILEKKQEELKFVIKELQQ----LEGSSDRILELDQELRKaerelsKAEKNSLTETLKKEVKSLQNEKADLDRKLRKldq 522
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   806 ---QMKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMRELQDQLEAEQYFSTLYKTqvKELKEEIEEKNRENLKKIQELQ 882
Cdd:TIGR00606  523 emeQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDW--LHSKSKEINQTRDRLAKLNKEL 600
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   883 NEKETLATQLDLAETKAESEQLArglLEEQYFEL--TQESKKAASRNRQEITDKDHTVSRLEEANSMLTKDIEILRRENE 960
Cdd:TIGR00606  601 ASLEQNKNHINNELESKEEQLSS---YEDKLFDVcgSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQ 677
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   961 E---LTEKMKKAEEEYKLEKEEEISNLKAAFEKNINTERTLKTQavNKLAEIM----NRKDFKIDRKKANTQDLRKK-EK 1032
Cdd:TIGR00606  678 SccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKK--EKRRDEMlglaPGRQSIIDLKEKEIPELRNKlQK 755
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167887698  1033 ENRKLQLELN--QEREKFNQMVVKHQKELNDMQAqlveECAHRNELQMQLASKESDIEQLRAKL 1094
Cdd:TIGR00606  756 VNRDIQRLKNdiEEQETLLGTIMPEEESAKVCLT----DVTIMERFQMELKDVERKIAQQAAKL 815
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
73-290 5.74e-07

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; 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. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and 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. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 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: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 53.09  E-value: 5.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   73 AEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllskfemIKRSDSAFFWE---ERDIMAFANSP------WVVQLFYAF 143
Cdd:cd14226    12 MDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIK-------IIKNKKAFLNQaqiEVRLLELMNKHdtenkyYIVRLKRHF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  144 QDDRYLYMVMEYMpGGDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHS--MGFIHRDVKPDNMLL--DKSGHLKLAD 216
Cdd:cd14226    85 MFRNHLCLVFELL-SYNLYDLLRNTNfrgVSLNLTRKFAQQLCTALLFLSTpeLSIIHCDLKPENILLcnPKRSAIKIID 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167887698  217 FGTCMKMNKegmvRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKI 290
Cdd:cd14226   164 FGSSCQLGQ----RIYQYIQSRFYRSPEVLLGLP----YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKI 229
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
76-274 7.26e-07

Catalytic domain of the Dual-specificity protein kinase, YAK1; 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 proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 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: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 53.02  E-value: 7.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   76 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLskfemikRSDSAFFWE---ERDIMAFANSPW-------VVQLFYAFQD 145
Cdd:cd14212     1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVL-------KNKPAYFRQamlEIAILTLLNTKYdpedkhhIVRLLDHFMH 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  146 DRYLYMVMEyMPGGDLVNLM---SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD--KSGHLKLADFGT- 219
Cdd:cd14212    74 HGHLCIVFE-LLGVNLYELLkqnQFRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVnlDSPEIKLIDFGSa 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887698  220 CMKmnkegmvrcDTAVGTpdYI------SPEVLKsqggdGY-YGRECDWWSVGVFLYEMLVG 274
Cdd:cd14212   153 CFE---------NYTLYT--YIqsrfyrSPEVLL-----GLpYSTAIDMWSLGCIAAELFLG 198
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
749-1094 7.28e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 7.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   749 KQSQQKLEHLTGNKERMEDEVKNLTLQLeqesnkrlllqNELKTQAFEADNLKGLEKQMKqEINTLLEAKRLLEF--ELA 826
Cdd:TIGR02168  175 KETERKLERTRENLDRLEDILNELERQL-----------KSLERQAEKAERYKELKAELR-ELELALLVLRLEELreELE 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   827 QLTKQYRGNEGQMRELQDQLEAEQyfstlykTQVKelkeeieeknrENLKKIQELQNEKETLatQLDLAETKAESEQLar 906
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAELQELE-------EKLE-----------ELRLEVSELEEEIEEL--QKELYALANEISRL-- 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   907 glleEQYFELTQESKKAASRNRQEITDkdhtvsRLEEANSMLTKDIEILRRENEELTEKMKKaeeeyklekeeeISNLKA 986
Cdd:TIGR02168  301 ----EQQKQILRERLANLERQLEELEA------QLEELESKLDELAEELAELEEKLEELKEE------------LESLEA 358
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   987 AFEKNINTERTLKTQAVNKLAEIMN-RKDFKIDRKKANTQDLRKKEKENRKLQLELNQER-------------------- 1045
Cdd:TIGR02168  359 ELEELEAELEELESRLEELEEQLETlRSKVAQLELQIASLNNEIERLEARLERLEDRRERlqqeieellkkleeaelkel 438
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 167887698  1046 ----EKFNQMVVKHQKELNDMQAQLVEECAHRNELQMQLASKESDIEQLRAKL 1094
Cdd:TIGR02168  439 qaelEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
767-966 7.83e-07

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 52.84  E-value: 7.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  767 DEVKNLTLQLEQESNKRLLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMRELQDQL 846
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  847 EAEQ-----YFSTLYKT----------------QVKELKEEIEEKNRENLKKIQELQNEKETLATQLDLAETKAESEQLA 905
Cdd:COG4942   100 EAQKeelaeLLRALYRLgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167887698  906 RGLLEEQYFELTQ---ESKKAASRNRQEITDKDHTVSRLEEANSMLTKDIEILRRENEELTEKM 966
Cdd:COG4942   180 LAELEEERAALEAlkaERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
PRK11637 PRK11637
AmiB activator; Provisional
520-707 8.03e-07

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 53.16  E-value: 8.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  520 KDQLEDL--------KKVSQNSQLANEKLSQLQKQ---LEEANDLLRTESDTAVRLRKSHTEMSKSISQLESLNRElQER 588
Cdd:PRK11637   46 RDQLKSIqqdiaakeKSVRQQQQQRASLLAQLKKQeeaISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAA-QER 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  589 NRilensKSQTDKDYYQ-----LQAILEAERRDRghdSEMI----GDL-QARitslQEEVKHLKHNLEKVEGERKEAQdm 658
Cdd:PRK11637  125 LL-----AAQLDAAFRQgehtgLQLILSGEESQR---GERIlayfGYLnQAR----QETIAELKQTREELAAQKAELE-- 190
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 167887698  659 lnhsekEKNNLEIDLNYKLKSLQQRLEQEVNEHKVTkarLTDKHQSIEE 707
Cdd:PRK11637  191 ------EKQSQQKTLLYEQQAQQQKLEQARNERKKT---LTGLESSLQK 230
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
523-942 8.53e-07

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.92  E-value: 8.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   523 LEDLKKVSQNSQLANEKLSQLQKQLEEandlLRTESDTAVRLRKshtemsksisqlesLNRELQERnrilensksqtdkD 602
Cdd:TIGR02169  176 LEELEEVEENIERLDLIIDEKRQQLER----LRREREKAERYQA--------------LLKEKREY-------------E 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   603 YYQLQAILEAERRDrghdsemIGDLQARITSLQEEvkhlkhnLEKVEGERKEAQDMLNHSEKEKNNLEIDLNYKLKSLQQ 682
Cdd:TIGR02169  225 GYELLKEKEALERQ-------KEAIERQLASLEEE-------LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL 290
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   683 RLEQEVNEHKVTKARLTDkhqSIEEAKSvamcEMEKklkeerearekAENRVVQIEKQCSMLDVDLKQSQQKLEHLTGNK 762
Cdd:TIGR02169  291 RVKEKIGELEAEIASLER---SIAEKER----ELED-----------AEERLAKLEAEIDKLLAEIEELEREIEEERKRR 352
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   763 ERMEDEVKNLTLQLEqesnkrlLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMREL 842
Cdd:TIGR02169  353 DKLTEEYAELKEELE-------DLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADL 425
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   843 QDQLEAEqyfstlyktqvkelkeeieeknrenLKKIQELQNEKETLATQLDLAETKAESEQLARGLLEEQYFELTQESKK 922
Cdd:TIGR02169  426 NAAIAGI-------------------------EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
                          410       420
                   ....*....|....*....|
gi 167887698   923 AASrnrqEITDKDHTVSRLE 942
Cdd:TIGR02169  481 VEK----ELSKLQRELAEAE 496
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
160-272 1.01e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 52.57  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  160 DLVNLMSNYDVPEKWARFYTAE--VVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTcmkmnkegmVRCDTA--- 234
Cdd:PHA03209  142 DLYTYLTKRSRPLPIDQALIIEkqILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGA---------AQFPVVapa 212
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 167887698  235 ----VGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEML 272
Cdd:PHA03209  213 flglAGTVETNAPEVLARDK----YNSKADIWSAGIVLFEML 250
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
516-1069 1.02e-06

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 53.64  E-value: 1.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   516 VSTLKDQLE-DLKKVSQNSQLANEKLSQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSISQLESLNRELQERNRILEN 594
Cdd:pfam01576   17 VKERQQKAEsELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQN 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   595 SKSQTDKDYYQLQAILEaerrdrghdsemigdlqaritslQEEVKHLKHNLEKVEGERKeaqdmLNHSEKEKNNLEiDLN 674
Cdd:pfam01576   97 EKKKMQQHIQDLEEQLD-----------------------EEEAARQKLQLEKVTTEAK-----IKKLEEDILLLE-DQN 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   675 YKLKSLQQRLEQEVNEHKVTKARLTDKHQSIEEAKS---VAMCEMEKKLKEEREAREKAENRVVQIEKQCSMLDVDLKQS 751
Cdd:pfam01576  148 SKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNkheAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAEL 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   752 QQKLEHLTGNKERMEDEVKNLTLQLEQESNKRLLLQN---ELKTQAFEADNLKGLEKQMKqeiNTLLEAKRLLEFELAQL 828
Cdd:pfam01576  228 QAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKkirELEAQISELQEDLESERAAR---NKAEKQRRDLGEELEAL 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   829 tkqyrgnEGQMRELQDQLEAEQYFSTLYKTQVKELKEEIEEKNRENLKKIQELQNEK----ETLATQLDLAETKAESEQL 904
Cdd:pfam01576  305 -------KTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHtqalEELTEQLEQAKRNKANLEK 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   905 ARGLLEEQYFELTQESKKAASRNRQEITDKDHTVSRLEEANSMLTKDieilRRENEELTEKMKKAEEEYKLEKeeeiSNL 984
Cdd:pfam01576  378 AKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSES----ERQRAELAEKLSKLQSELESVS----SLL 449
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   985 KAAFEKNINTERTLkTQAVNKLAEIMNRKDFKIDRKKANTQDLRKKEKENRKLQLELNQEREK---FNQMVVKHQKELND 1061
Cdd:pfam01576  450 NEAEGKNIKLSKDV-SSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAkrnVERQLSTLQAQLSD 528

                   ....*...
gi 167887698  1062 MQAQLVEE 1069
Cdd:pfam01576  529 MKKKLEED 536
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
465-962 1.10e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  465 KELDEEGNQRRNLESTVSQIEKEKMLLQHRIN--EYQRKAEQENEKRRNVENEVSTLKDQLEDLKKVSQNSQLANEKLSQ 542
Cdd:COG4717    95 EELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAE 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  543 LQKQLEEANDLLRTEsdTAVRLRKSHTEMSKSISQLESLNRELQERNRILENSKSQTDKDYYQLQAILEAERRDRGhdsE 622
Cdd:COG4717   175 LQEELEELLEQLSLA--TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA---R 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  623 MIGDLQARITSLQEEVKHLKHNLEKVEG--------------ERKEAQDMLNHSEKEKNNLEIDLNYKLKSLQQRLEQEV 688
Cdd:COG4717   250 LLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALG 329
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  689 NEHKVTKARLTDKHQSIEEAKSvAMCEMEKKLKEEREAREKAENRVVQIEKQCSMLDvDLKQSQQKLEHltgnKERMEDE 768
Cdd:COG4717   330 LPPDLSPEELLELLDRIEELQE-LLREAEELEEELQLEELEQEIAALLAEAGVEDEE-ELRAALEQAEE----YQELKEE 403
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  769 VKNLTLQLEQESNkrlllqnelktqAFEADNLKGLEKQMKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMRELQDQlea 848
Cdd:COG4717   404 LEELEEQLEELLG------------ELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED--- 468
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  849 eqyfstlyktqvkelkeeieeknrenlKKIQELQNEKETLATQLDLAETKAESEQLARGLLEE--QYFELTQESK--KAA 924
Cdd:COG4717   469 ---------------------------GELAELLQELEELKAELRELAEEWAALKLALELLEEarEEYREERLPPvlERA 521
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 167887698  925 SRNRQEITDKDHTVSRLEEANSMLTKDIEILRRENEEL 962
Cdd:COG4717   522 SEYFSRLTDGRYRLIRIDEDLSLKVDTEDGRTRPVEEL 559
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
732-1090 1.25e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 49.63  E-value: 1.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   732 NRVVQIEKQCSMLDVDLKQSQQKLEHLTGNKERMEDEVKNLTLQLEQESNKRLLLQNELKTQAFEADNLKGLEKQMKQEI 811
Cdd:TIGR04523   33 TEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEI 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   812 NTLLEAKRLLEFELAQLTKQYRGNEGQMRELQDQLEAEQyfstlyktqvkELKEEIEEKNRENLKKIQELQNEKETLATQ 891
Cdd:TIGR04523  113 KNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKE-----------KELEKLNNKYNDLKKQKEELENELNLLEKE 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   892 LDLAETKAESEQLARGLLEEQYFELTQESKKAASRNRQeitdkdhtVSRLEEANSMLTKDIEILRRENEELTEKMKKAEE 971
Cdd:TIGR04523  182 KLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQ--------ISELKKQNNQLKDNIEKKQQEINEKTTEISNTQT 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   972 EYKLEKEEEISNLKAAFEKNINTERTLK-----TQAVNKL-AEIMNRKDFKI-DRKKANTQDLRKKEKENRKLQLELNQE 1044
Cdd:TIGR04523  254 QLNQLKDEQNKIKKQLSEKQKELEQNNKkikelEKQLNQLkSEISDLNNQKEqDWNKELKSELKNQEKKLEEIQNQISQN 333
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 167887698  1045 REKFNQMvvkhQKELNDMQAQLVEECAHRNELQMQLASKESDIEQL 1090
Cdd:TIGR04523  334 NKIISQL----NEQISQLKKELTNSESENSEKQRELEEKQNEIEKL 375
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
576-1100 1.52e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 49.72  E-value: 1.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   576 SQLESLNRELQERNRILENSKSQTDKDYYQLQAILEAERRDRGHDSEMIGDLQAR---ITSLQEEVKHLKHNLEKVEGER 652
Cdd:pfam05483   99 AELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATrhlCNLLKETCARSAEKTKKYEYER 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   653 KEAQ----DMLNHSEK----------EKNNLEIDLNYKLKSLQQRLEQEVNEHKvtkARLTDKHQSIEeAKSVAMCEMEK 718
Cdd:pfam05483  179 EETRqvymDLNNNIEKmilafeelrvQAENARLEMHFKLKEDHEKIQHLEEEYK---KEINDKEKQVS-LLLIQITEKEN 254
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   719 KLKEEREAREKAENRVVQIEKQCSMLDVDLKQSQQKLEHLTgnkermeDEVKNLTLQLEQESNKRLLLQNELKTQAFEAD 798
Cdd:pfam05483  255 KMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLT-------KELEDIKMSLQRSMSTQKALEEDLQIATKTIC 327
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   799 NLKGLEKQMKQEINTLLEAKRLLEFEL----AQLTKQYRGNEGQMRELQDQLEAEQYfsTLYKTQVKELKEEIEEKNRE- 873
Cdd:pfam05483  328 QLTEEKEAQMEELNKAKAAHSFVVTEFeattCSLEELLRTEQQRLEKNEDQLKIITM--ELQKKSSELEEMTKFKNNKEv 405
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   874 NLKKIQELQNEKETLATQLDLAETKAE----SEQLARGLLEEQYFEL------TQESKKAASRNRQEITDKDHTVSRLEE 943
Cdd:pfam05483  406 ELEELKKILAEDEKLLDEKKQFEKIAEelkgKEQELIFLLQAREKEIhdleiqLTAIKTSEEHYLKEVEDLKTELEKEKL 485
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   944 ANSMLTKDIEILRRENEELTEKMKKAEEEYKLEKEEEISNLKAA--FEKNINTERTLKTQAVNKLAEImnRKDF------ 1015
Cdd:pfam05483  486 KNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEerMLKQIENLEEKEMNLRDELESV--REEFiqkgde 563
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  1016 ---KIDRKKANTQDLR----KKEKENRKLQLELNQER---EKFNQMVVKHQKELNDMQAQLVEECAHRNELQMQLASKES 1085
Cdd:pfam05483  564 vkcKLDKSEENARSIEyevlKKEKQMKILENKCNNLKkqiENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLEL 643
                          570
                   ....*....|....*
gi 167887698  1086 DIEQLRAKLLDLSDS 1100
Cdd:pfam05483  644 ELASAKQKFEEIIDN 658
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
576-1096 2.18e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 49.20  E-value: 2.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   576 SQLESLNRELQERNRILENSKSQTDK--DYYQLQAILEAERRDRGHDSEM------IGDLQARITSLQEEVKHLKHNLEK 647
Cdd:pfam02463  183 ENLAELIIDLEELKLQELKLKEQAKKalEYYQLKEKLELEEEYLLYLDYLklneerIDLLQELLRDEQEEIESSKQEIEK 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   648 VEGERKEAQDMLNHSEKEKNNLEIDLNYK---LKSLQQRLEQEVNEHKVTKARLTDKHQSIEEAKSVAMCEMEKKLKEER 724
Cdd:pfam02463  263 EEEKLAQVLKENKEEEKEKKLQEEELKLLakeEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEK 342
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   725 EAREKAENRVVQIEKQCSMLDVDLKQSQQKLEHLTGNKERMEDEvKNLTLQLEQESNKRLLLQNELKTQAFEADNLKG-L 803
Cdd:pfam02463  343 ELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERL-SSAAKLKEEELELKSEEEKEAQLLLELARQLEDlL 421
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   804 EKQMKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMRELQDQLEAEQYFSTLYKTQVKELKEEIEEKNRENLKKIQELQN 883
Cdd:pfam02463  422 KEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQK 501
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   884 E---KETLATQLDLAETKAESEQLARGLLEEQYFELTQESKKAASRNRQEITDKDHTVSRLEEANSMLTKDIEILRRENE 960
Cdd:pfam02463  502 EskaRSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLR 581
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   961 ELTEKMKKAEEEYKLEKEEEISNLKAAFEKNINTERTLKTQAVNKLAEIMNRKDFKIDRKKANTQDLRKKEKENRKLQLE 1040
Cdd:pfam02463  582 LLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEK 661
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 167887698  1041 LNQEREKFNQMVVKHQKELNDMQAQLVEECAHRNELQMQLASKESDIEQLRAKLLD 1096
Cdd:pfam02463  662 SEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKL 717
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
426-710 2.40e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 2.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  426 ESLQKTIYKLEEQLHnemQLKDEMEQKCRTSNIKLDKIMKELDEE----GNQRRNLESTVSQIEKEKMLLQHRINEYQRK 501
Cdd:COG4717   159 RELEEELEELEAELA---ELQEELEELLEQLSLATEEELQDLAEEleelQQRLAELEEELEEAQEELEELEEELEQLENE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  502 AEQENEKRRNVENEVS-----------------------------------------------TLKDQLEDLKKVSQNSQ 534
Cdd:COG4717   236 LEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflvlgllallflllarekaSLGKEAEELQALPALEE 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  535 LANEKLSQLQKQL----EEANDLLRTESDTAVRLRKSHTEMSKSISQLEsLNRELQERNRILENSKSQTDKDYYQLQAIL 610
Cdd:COG4717   316 LEEEELEELLAALglppDLSPEELLELLDRIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGVEDEEELRAALEQA 394
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  611 EAERRDRGHdsemIGDLQARITSLQEEVKHL--KHNLEKVEGERKEAQDMLNHSEKEKNnleiDLNYKLKSLQQRLEQEV 688
Cdd:COG4717   395 EEYQELKEE----LEELEEQLEELLGELEELleALDEEELEEELEELEEELEELEEELE----ELREELAELEAELEQLE 466
                         330       340
                  ....*....|....*....|..
gi 167887698  689 NEHKVTKARltdkhQSIEEAKS 710
Cdd:COG4717   467 EDGELAELL-----QELEELKA 483
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
836-1097 2.77e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  836 EGQMRELQDQLE-AEQYFStlYKTQvkelkeEIEEKNRENLKKIQELQNEKETLATQLDLAETKAESEQLARGLLEEQYF 914
Cdd:COG1196   199 ERQLEPLERQAEkAERYRE--LKEE------LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  915 ELTQESK---KAASRNRQEITDKDHTVSRLEEAnsmltKDIEILRREN-----------EELTEKMKKAEEEYKLEKEEE 980
Cdd:COG1196   271 ELRLELEeleLELEEAQAEEYELLAELARLEQD-----IARLEERRREleerleeleeeLAELEEELEELEEELEELEEE 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  981 ISNLKAAFEKNINTERTLKTQAVNKLAEIMNRKDfKIDRKKANTQDLRKKEKENRKLQLELNQEREKFNQMVVKHQKELN 1060
Cdd:COG1196   346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEE-ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 167887698 1061 DMQAQLVEECAHRNELQMQLASKESDIEQLRAKLLDL 1097
Cdd:COG1196   425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
419-709 3.67e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 48.18  E-value: 3.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   419 NADKSLQESLQKTIYKLEEQlhnEMQLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKEKMLLQHRINEY 498
Cdd:pfam05483  523 INCKKQEERMLKQIENLEEK---EMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNL 599
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   499 QRKAEQENEKRRNVENEVSTLKDqledlKKVSQNSQLA--NEKLSQLQKQLEEANDLLRTESDTavrlrkshtemsksiS 576
Cdd:pfam05483  600 KKQIENKNKNIEELHQENKALKK-----KGSAENKQLNayEIKVNKLELELASAKQKFEEIIDN---------------Y 659
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   577 QLESLNRELQERNRILENSKSQTDKD-YYQLQAilEAERRDRGHDSEMIGDLQaritslqeevKHlKHNLEKVEGERKEA 655
Cdd:pfam05483  660 QKEIEDKKISEEKLLEEVEKAKAIADeAVKLQK--EIDKRCQHKIAEMVALME----------KH-KHQYDKIIEERDSE 726
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167887698   656 QDMLNHSEKEKNNLEIDLNYKLK-------SLQQRLEQEVNEHKVTKARLTDKHQSIEEAK 709
Cdd:pfam05483  727 LGLYKNKEQEQSSAKAALEIELSnikaellSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
745-1043 4.03e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.14  E-value: 4.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   745 DVDLKQSQQKLEHLTGNKER---MEDEVKNLTLQLEQESNKRL---LLQNEL-KTQAFE-ADNLKGLEKQMKQ---EINT 813
Cdd:TIGR02169  169 DRKKEKALEELEEVEENIERldlIIDEKRQQLERLRREREKAEryqALLKEKrEYEGYElLKEKEALERQKEAierQLAS 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   814 LLEAKRLLEFELAQLTKQYRGNEGQMRELQDQLEAEQYFSTL-YKTQVKELKEEIEEKNRENLKKIQELQNEKETLA-TQ 891
Cdd:TIGR02169  249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLrVKEKIGELEAEIASLERSIAEKERELEDAEERLAkLE 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   892 LDLAETKAESEQLARGLLEEQ-----YFELTQESKKAASRNRQEITDKDHTVSRLEEANSMLTKDIEILRRENEELtEKM 966
Cdd:TIGR02169  329 AEIDKLLAEIEELEREIEEERkrrdkLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL-KRE 407
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   967 KKAEEEYKLEKEEEISNLKAAFEKNINTERTLKTQAVNKLAEI----MNRKDFKIDRKKAN------TQDLRKKEKENRK 1036
Cdd:TIGR02169  408 LDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIkkqeWKLEQLAADLSKYEqelydlKEEYDRVEKELSK 487

                   ....*..
gi 167887698  1037 LQLELNQ 1043
Cdd:TIGR02169  488 LQRELAE 494
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
405-962 4.28e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.14  E-value: 4.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   405 YLSSANPNDNRTSSNADKSLQESLQKTIYKLEEQLHnemQLKDEMEQKCRTSNIKLDKIMKELDEEGNQ-RRNLESTVSQ 483
Cdd:TIGR02169  226 YELLKEKEALERQKEAIERQLASLEEELEKLTEEIS---ELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAE 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   484 IEKekmlLQHRINEYQRKAEQENEKRRNVENEVSTLKDQLEDLKKVSQNSQLANEKLSQLQKQLEEANDLLRTE-SDTAV 562
Cdd:TIGR02169  303 IAS----LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAElEEVDK 378
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   563 RLRKSHTEMSKSISQLESLNRELQERNRILEnsksqtdkdyyQLQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLK 642
Cdd:TIGR02169  379 EFAETRDELKDYREKLEKLKREINELKRELD-----------RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   643 HNLEKVEGERKEAQDMLNHSEKEKNNLEIDLNY---KLKSLQQRLEQ--------------------------------- 686
Cdd:TIGR02169  448 LEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRvekELSKLQRELAEaeaqaraseervrggraveevlkasiqgvhgtv 527
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   687 --------------EV------------------------NEHKVTKA------RLTDKH-------------------- 702
Cdd:TIGR02169  528 aqlgsvgeryataiEVaagnrlnnvvveddavakeaiellKRRKAGRAtflplnKMRDERrdlsilsedgvigfavdlve 607
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   703 -------------------QSIEEA------------------KSVAMC---------------------EMEKKLKEER 724
Cdd:TIGR02169  608 fdpkyepafkyvfgdtlvvEDIEAArrlmgkyrmvtlegelfeKSGAMTggsraprggilfsrsepaelqRLRERLEGLK 687
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   725 EAREKAENRVVQIEKQCSMLDVDLKQSQQKLEHLTGNKERMEDEVKNLTLQLEQESNKRLLLQNELKTQAFEADNLKGLE 804
Cdd:TIGR02169  688 RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARI 767
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   805 KQMKQEINTLLEA-----KRLLEFELAQLTKQYRGNEGQMRELQ---DQLEAEQYFSTLYKTQVKELKEEIEEKNRENLK 876
Cdd:TIGR02169  768 EELEEDLHKLEEAlndleARLSHSRIPEIQAELSKLEEEVSRIEarlREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE 847
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   877 KIQELQNEKETLATQLDLAETKAESEQLARGLLEEQYFELTQESKKAASRNRQ---EITDKDHTVSRLEEANSMLTKDIE 953
Cdd:TIGR02169  848 QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRElerKIEELEAQIEKKRKRLSELKAKLE 927

                   ....*....
gi 167887698   954 ILRRENEEL 962
Cdd:TIGR02169  928 ALEEELSEI 936
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
644-1118 6.47e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 6.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  644 NLEKVEGERKEAQDMLNHSEKEKNNLEidlnyklkSLQQRLEQEVNEHKVTKARLTDKHQSIEEaksvamceMEKKLKEE 723
Cdd:PRK03918  156 GLDDYENAYKNLGEVIKEIKRRIERLE--------KFIKRTENIEELIKEKEKELEEVLREINE--------ISSELPEL 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  724 REAREKAENRVVQIEKqcsmLDVDLKQSQQKLEHLTGNKERMEDEVKNLTLQLEqESNKRLllqNELKTQAFEADNLKGL 803
Cdd:PRK03918  220 REELEKLEKEVKELEE----LKEEIEELEKELESLEGSKRKLEEKIRELEERIE-ELKKEI---EELEEKVKELKELKEK 291
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  804 EKQ---MKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMRELQDQLEaeqyfstlyktqvkelkeeieeKNRENLKKIQE 880
Cdd:PRK03918  292 AEEyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE----------------------RLEELKKKLKE 349
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  881 LQNEKETLATQLDLAET----KAESEQLARGLLEEQYFELTQESKKAASRnRQEITDKDHTV----SRLEEANSMLTKDI 952
Cdd:PRK03918  350 LEKRLEELEERHELYEEakakKEELERLKKRLTGLTPEKLEKELEELEKA-KEEIEEEISKItariGELKKEIKELKKAI 428
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  953 EILRRE-------NEELTEKmkkAEEEYKLEKEEEISNLKAAFEKNINTERTLKTQAVNklAEIMNRKDFKIDRKKANTQ 1025
Cdd:PRK03918  429 EELKKAkgkcpvcGRELTEE---HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE--LEKVLKKESELIKLKELAE 503
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698 1026 DLRKKEKENRKLQLE----LNQEREKFNQMVVKHQKELNDMQAQLVEEcahrNELQMQLASKESDIEQLRAKLLDLSDST 1101
Cdd:PRK03918  504 QLKELEEKLKKYNLEelekKAEEYEKLKEKLIKLKGEIKSLKKELEKL----EELKKKLAELEKKLDELEEELAELLKEL 579
                         490
                  ....*....|....*..
gi 167887698 1102 SVASFPSADETDGNLPE 1118
Cdd:PRK03918  580 EELGFESVEELEERLKE 596
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
448-944 6.81e-05

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 47.66  E-value: 6.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   448 EMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKEKMLLQHRI---NEYQRKAEQENEKRRNVENEVST---LKD 521
Cdd:TIGR00618  304 QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHsqeIHIRDAHEVATSIREISCQQHTLtqhIHT 383
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   522 QLEDLKKVSQNSQLANEKLSQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSISQLESLNRELQE-------RNRILEN 594
Cdd:TIGR00618  384 LQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCtaqceklEKIHLQE 463
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   595 SKSQTDKDYYQL---QAILEAERR---DRGH------------------------DSEMIGDLQARITSLQEEVKHLKHN 644
Cdd:TIGR00618  464 SAQSLKEREQQLqtkEQIHLQETRkkaVVLArllelqeepcplcgscihpnparqDIDNPGPLTRRMQRGEQTYAQLETS 543
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   645 LEKVEG----ERKEAQdmlnhSEKEKNNLEIDLNYKLKSLQQRLEQEVNEHKVTKARLTDKHQSIEEAKSVAMCEMEKKL 720
Cdd:TIGR00618  544 EEDVYHqltsERKQRA-----SLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALL 618
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   721 KEEREAREKAenRVVQIEKQCSmldvdlKQSQQKLEHLTGNKERMEDEVKNLTLQLEQESNKRLLLQNELKTQafEADNL 800
Cdd:TIGR00618  619 RKLQPEQDLQ--DVRLHLQQCS------QELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQ--KMQSE 688
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   801 KGLEKQMKQEINTLLEAKRLLEFELAQLTKQYR--------------GNEGQMRELQDQLEAEQ----------YFSTLY 856
Cdd:TIGR00618  689 KEQLTYWKEMLAQCQTLLRELETHIEEYDREFNeienassslgsdlaAREDALNQSLKELMHQArtvlkarteaHFNNNE 768
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   857 K--------TQVKELKEEIEEKNRENLKKIQELQNEKETLATQLDLAETKAESEQLARGLLEEQYFELTQESKKAASRNR 928
Cdd:TIGR00618  769 EvtaalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEIT 848
                          570
                   ....*....|....*.
gi 167887698   929 QEITDKDHTVSRLEEA 944
Cdd:TIGR00618  849 HQLLKYEECSKQLAQL 864
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
589-1099 1.14e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.57  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  589 NRILENSKSQTDKDYYQLQAILEAERRDRghdsemIGDLQARITSLQEEVKHLKHNLEKVEGERKEAQDMLnhSEKEKNN 668
Cdd:PRK02224  179 ERVLSDQRGSLDQLKAQIEEKEEKDLHER------LNGLESELAELDEEIERYEEQREQARETRDEADEVL--EEHEERR 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  669 LEIDlnyklkslqqRLEQEVNEHKVTKARLTDKHQSIEEAKSVAMCEMEkklkeereareKAENRVVQIEKQCSMLDVDL 748
Cdd:PRK02224  251 EELE----------TLEAEIEDLRETIAETEREREELAEEVRDLRERLE-----------ELEEERDDLLAEAGLDDADA 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  749 KQSQQKLEHLTGNKERMEDEVKNLTLQLEQESNKRLLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLEFELAQL 828
Cdd:PRK02224  310 EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  829 TKQYRGNEGQMRELQDQLEAEQYFSTLyktqvkelkeeiEEKNRENLKkiqelQNEKETLATQLDLAETKAESEQLargl 908
Cdd:PRK02224  390 EEEIEELRERFGDAPVDLGNAEDFLEE------------LREERDELR-----EREAELEATLRTARERVEEAEAL---- 448
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  909 leeqyfeltQESKKAASRNrQEITDKDH--TVSRLEEANSMLTKDIEILRRENEELTEKMkkaeeeyklekeEEISNLKA 986
Cdd:PRK02224  449 ---------LEAGKCPECG-QPVEGSPHveTIEEDRERVEELEAELEDLEEEVEEVEERL------------ERAEDLVE 506
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  987 AfEKNINTERTlKTQAVNKL----AEIMNRKDFKIDRKKANTQDLRKKEKENRKLQLELNQEREKFNQMVvkhqKELNDM 1062
Cdd:PRK02224  507 A-EDRIERLEE-RREDLEELiaerRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV----AELNSK 580
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 167887698 1063 QAQLVEECAHRN---ELQMQLASKESDIEQLRAKLLDLSD 1099
Cdd:PRK02224  581 LAELKERIESLErirTLLAAIADAEDEIERLREKREALAE 620
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
428-707 1.44e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 46.35  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   428 LQKTIYKLEEQLHNE----MQLKDEMeQKCRTSNIKLDKIMKELDEE-GNQRRNLESTVSQIEKEKMLLQHRINEYQRKA 502
Cdd:pfam10174  399 LQKKIENLQEQLRDKdkqlAGLKERV-KSLQTDSSNTDTALTTLEEAlSEKERIIERLKEQREREDRERLEELESLKKEN 477
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   503 EQENEKRRNVENEVSTLKDQLEDLKKVSQNSQLANEKLSQLQKQLEEAndlLRTESDTAVRLRKSHTEmSKSISQLESLN 582
Cdd:pfam10174  478 KDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIA---VEQKKEECSKLENQLKK-AHNAEEAVRTN 553
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   583 RELQERNRILEN---------SKSQTDKDyyQLQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVEGE-- 651
Cdd:pfam10174  554 PEINDRIRLLEQevarykeesGKAQAEVE--RLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEmk 631
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 167887698   652 RKEAQDMLNHSEKEKNNLEIDLNYKLKSLQQRLEQEVNEHKVTKARLTDKHQSIEE 707
Cdd:pfam10174  632 KKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAE 687
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
413-851 2.04e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 46.19  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   413 DNRTSSNADKslQESLQKTIYKLEEQlHNEMQLKDEMEQKcrtsniKLDKIMKELDEEGNQRRNLESTV----SQIEKEK 488
Cdd:TIGR00606  701 QSKLRLAPDK--LKSTESELKKKEKR-RDEMLGLAPGRQS------IIDLKEKEIPELRNKLQKVNRDIqrlkNDIEEQE 771
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   489 MLLQhrineyqrKAEQENEKRRNVENEVSTLKDQLEDLKKVSQnsqlaneKLSQLQKQLEeANDLLRTESDTAVRLRKSH 568
Cdd:TIGR00606  772 TLLG--------TIMPEEESAKVCLTDVTIMERFQMELKDVER-------KIAQQAAKLQ-GSDLDRTVQQVNQEKQEKQ 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   569 TEMSKSISQLESLNRELQERNRILENSKSQTDKDYYQLQAILEAERRdRGHDSEMIGDLQARITSLQEEVKHLKHNLEKV 648
Cdd:TIGR00606  836 HELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR-RQQFEEQLVELSTEVQSLIREIKDAKEQDSPL 914
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   649 EGERKEAQ---DMLNHSEKEKNNLEIDlnyKLKSLQQRLEQEVNEHKvtkarltDKHQSIEEAKSVAMCEMEKKLKEERE 725
Cdd:TIGR00606  915 ETFLEKDQqekEELISSKETSNKKAQD---KVNDIKEKVKNIHGYMK-------DIENKIQDGKDDYLKQKETELNTVNA 984
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   726 AREKAENRVVQIEKQCSMLDVDLKQSQQKLEHLTGNKERM--EDEVKNltlqleqesnkrllLQNELKTQAFEADNLKGL 803
Cdd:TIGR00606  985 QLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRkrENELKE--------------VEEELKQHLKEMGQMQVL 1050
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 167887698   804 ekQMKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMRELQDQLEAEQY 851
Cdd:TIGR00606 1051 --QMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQF 1096
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
424-655 4.60e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.67  E-value: 4.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   424 LQESLQKTIYKLEEQLHNEMQLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKEkmllqhrineyqrkae 503
Cdd:TIGR02169  827 EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE---------------- 890
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   504 qenekRRNVENEVSTLKDQLEDLKkvsQNSQLANEKLSQLQKQLEEANDLLrTESDTAVRLRKSHTEMSKSISQLESLNR 583
Cdd:TIGR02169  891 -----RDELEAQLRELERKIEELE---AQIEKKRKRLSELKAKLEALEEEL-SEIEDPKGEDEEIPEEELSLEDVQAELQ 961
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167887698   584 ELQERNRILENSKSQTDKDYYqlqailEAERRdrghdsemIGDLQARITSLQEEVKHLKHNLEKVEGERKEA 655
Cdd:TIGR02169  962 RVEEEIRALEPVNMLAIQEYE------EVLKR--------LDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
408-615 5.11e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 5.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  408 SANP--NDNRTSSNADKSLQESLQKTIYKLEEQLHNEMQLKDEMEQKCRTSNIKLDKIMKELDEegnqrrnLEstvSQIE 485
Cdd:COG3883    13 FADPqiQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE-------AE---AEIE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  486 KEKMLLQHRINEYQRKAEQENEkrrnVE-----NEVSTLKDQLEDLKKVSQNSQLANEKLSQLQKQLEEANDLLRTESDT 560
Cdd:COG3883    83 ERREELGERARALYRSGGSVSY----LDvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 167887698  561 AVRLRKshtEMSKSISQLESLNRELQERNRILENSKSQTDKDYYQLQAILEAERR 615
Cdd:COG3883   159 LEALKA---ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
429-749 7.04e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.19  E-value: 7.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   429 QKTIYKLEEQLHNEMQLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKEKMLLQHRINEYQRKAEQENEK 508
Cdd:pfam02463  744 KIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLL 823
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   509 RRNVENEVSTLKDQLEDLKKVSQNSQLANEKLSQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSISQLESLNRELQER 588
Cdd:pfam02463  824 IEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELE 903
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   589 NRILENSKSQTDKDYYQLQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVEGERKEAqdmlnhsEKEKNN 668
Cdd:pfam02463  904 EESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKE-------ELGKVN 976
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   669 LEIDLNYKlkslqqRLEQEVNEHKVTKARLTDKHQSIEEaksvamcemekklkeerearekaenrvVQIEKQCSMLDVDL 748
Cdd:pfam02463  977 LMAIEEFE------EKEERYNKDELEKERLEEEKKKLIR---------------------------AIIEETCQRLKEFL 1023

                   .
gi 167887698   749 K 749
Cdd:pfam02463 1024 E 1024
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
418-676 9.38e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.80  E-value: 9.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   418 SNADKSLQESLQKTIYKLEEQLHNemQLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKEKMLLQHRIN- 496
Cdd:TIGR00618  604 SEAEDMLACEQHALLRKLQPEQDL--QDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLa 681
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   497 --EYQRKAEQENEKRRNVENEVSTLKDQLEDLKK----VSQNSQLANEKLSQLQKQLEEANDLL---RTESDTAVRLR-- 565
Cdd:TIGR00618  682 lqKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEydreFNEIENASSSLGSDLAAREDALNQSLkelMHQARTVLKARte 761
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   566 -------------KSHTEMSKSISQLESLNRELQERNRILENSKSQTDKDYYQLQAILEAERRDRGHDSEMIGDLQARIT 632
Cdd:TIGR00618  762 ahfnnneevtaalQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKS 841
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 167887698   633 SLQEEVKHLKHNLEkvegERKEAQDMLNHSEKEKNNLEIDLNYK 676
Cdd:TIGR00618  842 ATLGEITHQLLKYE----ECSKQLAQLTQEQAKIIQLSDKLNGI 881
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
684-1051 1.09e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.42  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   684 LEQEVNEHKVTKARLTDKHQSIEEAKSVAMCEMEKKLKEEREAREKAENRVVQIEKQCSMLDVDLKQSQQKLEHLTGNKE 763
Cdd:pfam02463  158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEE 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   764 RMEDEVKNLTLQLEQESNKRLLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLEFELAQLTKqyrgNEGQMRELQ 843
Cdd:pfam02463  238 RIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK----LERRKVDDE 313
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   844 DQLEAEQyfSTLYKTQVKELKEEIEEKNRENLKKIQELQNEKETLATQLDLAETKAESEQLARglLEEQYFELTQESKKA 923
Cdd:pfam02463  314 EKLKESE--KEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEE--LLAKKKLESERLSSA 389
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   924 ASRNRQEITDKDHTVSRLEEANSMLTKDIEILRRENEELTEKmkkaeeeykLEKEEEISNLKAAFEKNintertlktqav 1003
Cdd:pfam02463  390 AKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEI---------LEEEEESIELKQGKLTE------------ 448
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 167887698  1004 NKLAEIMNRKDFKIDRKKANTQDLRKKEKENRKLQLELNQEREKFNQM 1051
Cdd:pfam02463  449 EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
717-926 1.17e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  717 EKKLKEEREAREKAENRVVQIEKQCSMLDVDLKQSQQKLEHLTGNKERMEDEVKNLTLQLEQESNKRLLLQNELKTQAFE 796
Cdd:COG4942    26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  797 -ADNLKGLEKQMKQ-EINTLLEAKRLLEFE-----LAQLTKQYRGNEGQMRELQDQLEAEQyfstLYKTQVKELKEEIEE 869
Cdd:COG4942   106 lAELLRALYRLGRQpPLALLLSPEDFLDAVrrlqyLKYLAPARREQAEELRADLAELAALR----AELEAERAELEALLA 181
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167887698  870 KNRENLKKIQELQNEKETLATQL--DLAETKAESEQLAR--GLLEEQYFELTQESKKAASR 926
Cdd:COG4942   182 ELEEERAALEALKAERQKLLARLekELAELAAELAELQQeaEELEALIARLEAEAAAAAER 242
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
798-1104 1.20e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   798 DNLKGLEKQMKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMRELQDQL---EAEQYFSTLYKTQVKELKEEIEEKNREN 874
Cdd:TIGR02169  198 QQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLaslEEELEKLTEEISELEKRLEEIEQLLEEL 277
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   875 LKKIQELqNEKETLATQLDLAETKAESEQLARGLLEEQyfeltQESKKAASRNRQEITDKDHTVSRLEEansmLTKDIEI 954
Cdd:TIGR02169  278 NKKIKDL-GEEEQLRVKEKIGELEAEIASLERSIAEKE-----RELEDAEERLAKLEAEIDKLLAEIEE----LEREIEE 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   955 LRRENEELTEkmkkaeeeyklekeeeisnlkaafeknintertlktqavnklaEIMNRKDfkidRKKANTQDLRKKEKEN 1034
Cdd:TIGR02169  348 ERKRRDKLTE-------------------------------------------EYAELKE----ELEDLRAELEEVDKEF 380
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  1035 RKLQLELNQEREKFNQMvvkhQKELNDMQAQLVEECAHRNELQMQLASKESDIEQLRAKLLDLSDSTSVA 1104
Cdd:TIGR02169  381 AETRDELKDYREKLEKL----KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK 446
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
678-1097 1.44e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 43.11  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   678 KSLQQRLEQEVNEHKVTKARLTDKHQSIEEAKSVAMCEMEKKLKEEREarekaenrvvqiEKQCSMLD-VDLKQSQQKLE 756
Cdd:TIGR00606  169 KALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYK------------EKACEIRDqITSKEAQLESS 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   757 H-LTGNKERMEDEVKNLTLQLEQESNKRLLLQNELKTqafeadnLKGLEKQMkQEINTLLEAKRllefelaqlTKQYRGN 835
Cdd:TIGR00606  237 ReIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKA-------LKSRKKQM-EKDNSELELKM---------EKVFQGT 299
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   836 EGQMRELQDQLEAEQYFSTLYKTQVKELKEEIEEKNRENLKKIQELQNEKETLATQLDLAE--------------TKAES 901
Cdd:TIGR00606  300 DEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQehirardsliqslaTRLEL 379
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   902 EQLARGLLEE----QYFELTQESK----KAASRNRQEITDKDHTVSR-LEEANSMLTKDIEILRRENEELTEKMKKAEEE 972
Cdd:TIGR00606  380 DGFERGPFSErqikNFHTLVIERQedeaKTAAQLCADLQSKERLKQEqADEIRDEKKGLGRTIELKKEILEKKQEELKFV 459
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698   973 YKLEKEEEIS--NLKAAFEKNINTERTLKTQAVN-----KLAEIMNRKDFKID-----RKKANTQDLRKKEKENRKLQLE 1040
Cdd:TIGR00606  460 IKELQQLEGSsdRILELDQELRKAERELSKAEKNsltetLKKEVKSLQNEKADldrklRKLDQEMEQLNHHTTTRTQMEM 539
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698  1041 LNQEREKFNQMVVKHQKELNDMQAQLVEECAHRNELQMQLASKESDIEQLRAKLLDL 1097
Cdd:TIGR00606  540 LTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKL 596
ROCK_SBD cd22250
Shroom-binding domain found in Rho-associated coiled-coil containing protein kinase; ...
1002-1058 1.99e-03

Shroom-binding domain found in Rho-associated coiled-coil containing protein kinase; Rho-associated coiled-coil containing protein kinase (ROCK) is a serine/threonine kinase (STK) that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. It is also referred to as Rho-associated protein kinase or simply as Rho kinase. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Rho-associated protein kinase 1 (ROCK1) is also called renal carcinoma antigen NY-REN-35, Rho-associated, coiled-coil-containing protein kinase 1, ROCK-I, p160 ROCK-1, or p160ROCK, 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 in ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. Rho-associated protein kinase 2 (ROCK2), also called Rho kinase 2, Rho-associated, coiled-coil-containing protein kinase 2, ROCK-II, or p164 ROCK-2, is more prominent in brain and skeletal muscle. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK subfamily proteins contain an N-terminal extension, a catalytic kinase domain, a coiled-coil (CC) 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 proteolytic cleavage, binding of lipids to the PH domain, or binding of GTP-bound RhoA to the CC region. More recently, the Shroom family of proteins have been identified as an additional regulator of ROCK. This model corresponds to the Shroom-binding domain (SBD) of ROCK, which forms a parallel coiled coil with the Shroom domain 2 (SD2) of Shroom.


Pssm-ID: 409019 [Multi-domain]  Cd Length: 75  Bit Score: 38.40  E-value: 1.99e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698 1002 AVNKLAEIMNRKDfkIDRKKANTQDLRKKEKENRKLQLELNQEREKFNQMVVKHQKE 1058
Cdd:cd22250    19 TLYKTQVKELKEE--LEEKTRQIKQELEDERESLSAQLELALAKADSEQLARSIAEE 73
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
744-1097 2.06e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  744 LDVDLKQSQQKLEH---LTGNKERMEDEVKNLTLQLEQESNKRLLLQNELKTQAFEADnLKGLEKQMKQEINTLLEAKRL 820
Cdd:COG4717    76 LEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE-LEALEAELAELPERLEELEER 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  821 LEfELAQLTKQYRGNEGQMRELQDQLEAEQYFSTLYK----TQVKELKEEIEEKNRENLKKIQELQNEKETLATQLDLAE 896
Cdd:COG4717   155 LE-ELRELEEELEELEAELAELQEELEELLEQLSLATeeelQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  897 TKAESEQLARGLLEEQY----------FELTQESKKAASRNRQEI--------------TDKDHTVSRLEEANSMLTKDI 952
Cdd:COG4717   234 NELEAAALEERLKEARLllliaaallaLLGLGGSLLSLILTIAGVlflvlgllallfllLAREKASLGKEAEELQALPAL 313
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  953 EILRREN-EELTEKMKKAEEEYKLEKEEEISNLKAAFEKnINTERTLKTQAvnKLAEIMNRKDFKIDRKKANT-QDLRKK 1030
Cdd:COG4717   314 EELEEEElEELLAALGLPPDLSPEELLELLDRIEELQEL-LREAEELEEEL--QLEELEQEIAALLAEAGVEDeEELRAA 390
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167887698 1031 EKENRKLQlELNQEREKFNQMVVKHQKELNDMQAQLVEECAHR--NELQMQLASKESDIEQLRAKLLDL 1097
Cdd:COG4717   391 LEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALDEEELEEelEELEEELEELEEELEELREELAEL 458
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
422-787 2.47e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  422 KSLQESLQKTIYKLEEQLHNEMQLKDEMEQkcrtsnikLDKIMKELDEEGNQRRNLESTVSQIEKEkmllqhRINEYQRK 501
Cdd:COG4717   135 EALEAELAELPERLEELEERLEELRELEEE--------LEELEAELAELQEELEELLEQLSLATEE------ELQDLAEE 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  502 AEQENEKRRNVENEVSTLKDQLEDLKKvsQNSQLANEKLS-QLQKQLEEANDLLRTES---------DTAVRLRKSHTEM 571
Cdd:COG4717   201 LEELQQRLAELEEELEEAQEELEELEE--ELEQLENELEAaALEERLKEARLLLLIAAallallglgGSLLSLILTIAGV 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  572 SKSISQLESLNRELQERNRILENSKSQTDKDYYQLQAILEAERRDRGHDSEMIGDLQ-ARITSLQEEVKHLKHNLEKVEG 650
Cdd:COG4717   279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSpEELLELLDRIEELQELLREAEE 358
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  651 ERKEAQdmLNHSEKEKNNLEIDLNYK-LKSLQQRLEQeVNEHKVTKARLTDKHQSIEEAKSVAMCEMEKKLKEEREAREK 729
Cdd:COG4717   359 LEEELQ--LEELEQEIAALLAEAGVEdEEELRAALEQ-AEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELE 435
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167887698  730 AENRVVQ-IEKQCSMLDVDLKQSQQKLEHLTGNKE--RMEDEVKNLTLQLEQESNKRLLLQ 787
Cdd:COG4717   436 ELEEELEeLEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALK 496
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
742-1111 4.71e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 4.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  742 SMLDVDLKQSQQKLEHLTGNK-ERMEDEVKNLTLQLEQESNKR---LLLQNELKTQAFEADNLKGLEKQMKQEINTLLEA 817
Cdd:COG4717    45 AMLLERLEKEADELFKPQGRKpELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  818 KRLLEfelaqLTKQYRGNEGQMRELQDQLEAEqyfstlyktqvkelkeeieeknRENLKKIQELQNEKETLATQLdlAET 897
Cdd:COG4717   125 LQLLP-----LYQELEALEAELAELPERLEEL----------------------EERLEELRELEEELEELEAEL--AEL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  898 KAESEQLARGLLEEQYFELtQESKKAASRNRQEITDKDHTVSRLEEAnsmltkdIEILRRENEELTEKMKKAEEEYKLEK 977
Cdd:COG4717   176 QEELEELLEQLSLATEEEL-QDLAEELEELQQRLAELEEELEEAQEE-------LEELEEELEQLENELEAAALEERLKE 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  978 EEEISNLKAA-------------FEKNINTERTLKTQAVNKLAEIMNRKDFKIDRKKANTQDLRKKEKENRKLQLELNQE 1044
Cdd:COG4717   248 ARLLLLIAAAllallglggsllsLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAA 327
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167887698 1045 REKFNQMVVKHQKELNDMQAQLVEECAHRNELQMQLasKESDIEQLRAKLLDLSDSTSVASFPSADE 1111
Cdd:COG4717   328 LGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALLAEAGVEDEEELRAALE 392
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
876-1123 8.15e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 8.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  876 KKIQELQNEKETLATQLDLAETKAESeqlarglLEEQYFELTQESKKAasrnRQEITDkdhtvsrleeansmLTKDIEIL 955
Cdd:COG3883    23 KELSELQAELEAAQAELDALQAELEE-------LNEEYNELQAELEAL----QAEIDK--------------LQAEIAEA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698  956 RRENEELTEKMKKAEEE--YKLEKEEEISNLKAA-----FEKNINTERTLKTQAVNKLAEIMNRKDfKIDRKKANT---- 1024
Cdd:COG3883    78 EAEIEERREELGERARAlyRSGGSVSYLDVLLGSesfsdFLDRLSALSKIADADADLLEELKADKA-ELEAKKAELeakl 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167887698 1025 QDLRKKEKENRKLQLELNQEREKFNQMVVKHQKELNDMQAQLVEECAHRNELQMQLASKESDIEQLRAKLLDLSDSTSVA 1104
Cdd:COG3883   157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
                         250
                  ....*....|....*....
gi 167887698 1105 SFPSADETDGNLPESRIEG 1123
Cdd:COG3883   237 AAAAAAAASAAGAGAAGAA 255
 
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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