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Conserved domains on  [gi|81915001|sp|Q8R2S1|]
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RecName: Full=Ribosomal protein S6 kinase-like 1

Protein Classification

ribosomal protein S6 kinase-like 1( domain architecture ID 10119364)

ribosomal protein S6 kinase-like 1 is a serine/threonine-protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
 148-534 2.90e-139

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: 403.47  E-value: 2.90e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 148 EQLKGCRVVGIIKKVQVVQDPATGGTFIVKSLPRCHMVSRERLTIIPHGVPYMTKLLRYFVSEDSIFLHLEHVQGGTLWS 227
Cdd:cd05576   1 EELKAFRVLGVIDKVLLVMDTRTQETFILKGLRKSSEYSRERKTIIPRCVPNMVCLRKYIISEESVFLVLQHAEGGKLWS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 228 HLLSQDHfqysglnsgsvqEKSQAQLSTRLslmtpaeltpghtlrqnripmepprtsqslppalqlqkeadaepssrpsa 307
Cdd:cd05576  81 YLSKFLN------------DKEIHQLFADL-------------------------------------------------- 98

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 308 vfssdpteapcghshsqvrragqssnpaptqrlhwvregadrvlgaygrgrgrnppsanrASLGSGRAAWSLREGQVKQW 387
Cdd:cd05576  99 ------------------------------------------------------------DERLAAASRFYIPEECIQRW 118

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 388 AAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCLYSAPEVGGISELTEACDWWSYGS 467
Cdd:cd05576 119 AAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIENMYCAPEVGGISEETEACDWWSLGA 198

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81915001 468 LLYELLTGMALSQSHPSGFQAHTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRLKSHPFF 534
Cdd:cd05576 199 LLFELLTGKALVECHPAGINTHTTLNIPEWVSEEARSLLQQLLQFNPTERLGAGVAGVEDIKSHPFF 265
MIT_SNX15 cd02677
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 48-122 1.46e-35

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT domain sub-family is found in sorting nexin 15 and related proteins. The molecular function of the MIT domain is unclear.


:

Pssm-ID: 239140  Cd Length: 75  Bit Score: 127.46  E-value: 1.46e-35
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81915001  48 DYLVDAATQIHLALERDVSEDYEAAFNHYQNGVDVLLRGVHVDPNKERREAVKLKITKYLRRAEEIFNCHLQRTL 122
Cdd:cd02677   1 DYLEQAAELIRLALEKEEEGDYEAAFEFYRAGVDLLLKGVQGDSSPERREAVKRKIAEYLKRAEEILRLHLSRSL 75
 
Name Accession Description Interval E-value
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
 148-534 2.90e-139

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: 403.47  E-value: 2.90e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 148 EQLKGCRVVGIIKKVQVVQDPATGGTFIVKSLPRCHMVSRERLTIIPHGVPYMTKLLRYFVSEDSIFLHLEHVQGGTLWS 227
Cdd:cd05576   1 EELKAFRVLGVIDKVLLVMDTRTQETFILKGLRKSSEYSRERKTIIPRCVPNMVCLRKYIISEESVFLVLQHAEGGKLWS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 228 HLLSQDHfqysglnsgsvqEKSQAQLSTRLslmtpaeltpghtlrqnripmepprtsqslppalqlqkeadaepssrpsa 307
Cdd:cd05576  81 YLSKFLN------------DKEIHQLFADL-------------------------------------------------- 98

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 308 vfssdpteapcghshsqvrragqssnpaptqrlhwvregadrvlgaygrgrgrnppsanrASLGSGRAAWSLREGQVKQW 387
Cdd:cd05576  99 ------------------------------------------------------------DERLAAASRFYIPEECIQRW 118

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 388 AAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCLYSAPEVGGISELTEACDWWSYGS 467
Cdd:cd05576 119 AAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIENMYCAPEVGGISEETEACDWWSLGA 198

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81915001 468 LLYELLTGMALSQSHPSGFQAHTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRLKSHPFF 534
Cdd:cd05576 199 LLFELLTGKALVECHPAGINTHTTLNIPEWVSEEARSLLQQLLQFNPTERLGAGVAGVEDIKSHPFF 265
MIT_SNX15 cd02677
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 48-122 1.46e-35

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT domain sub-family is found in sorting nexin 15 and related proteins. The molecular function of the MIT domain is unclear.


Pssm-ID: 239140  Cd Length: 75  Bit Score: 127.46  E-value: 1.46e-35
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81915001  48 DYLVDAATQIHLALERDVSEDYEAAFNHYQNGVDVLLRGVHVDPNKERREAVKLKITKYLRRAEEIFNCHLQRTL 122
Cdd:cd02677   1 DYLEQAAELIRLALEKEEEGDYEAAFEFYRAGVDLLLKGVQGDSSPERREAVKRKIAEYLKRAEEILRLHLSRSL 75
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
 385-544 5.35e-30

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 120.31  E-value: 5.35e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001  385 KQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCLYSAPEVGGISELTEACDWWS 464
Cdd:PTZ00263 121 KFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPDRTFTLCGTPEYLAPEVIQSKGHGKAVDWWT 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001  465 YGSLLYELLTGmalsqsHP-----SGFQAHTQ-----LQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRLKSHPFF 534
Cdd:PTZ00263 201 MGVLLYEFIAG------YPpffddTPFRIYEKilagrLKFPNWFDGRARDLVKGLLQTDHTKRLGTLKGGVADVKNHPYF 274

                        170
                 ....*....|
gi 81915001  535 STIQWSRLMG 544
Cdd:PTZ00263 275 HGANWDKLYA 284
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 378-534 9.19e-27

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 109.16  E-value: 9.19e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001    378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRCSQeavdC---LYSAPEVg 451
Cdd:smart00220  93 RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGlarQLDPGEKLTTF----VgtpEYMAPEV- 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001    452 gISEL--TEACDWWSYGSLLYELLTGMALsqshpsgFQAHTQLQL--------------PEW-LSHPAASLLTELLQFEP 514
Cdd:smart00220 168 -LLGKgyGKAVDIWSLGVILYELLTGKPP-------FPGDDQLLElfkkigkpkppfppPEWdISPEAKDLIRKLLVKDP 239

                          170       180
                   ....*....|....*....|
gi 81915001    515 QRRLGAggggtSRLKSHPFF 534
Cdd:smart00220 240 EKRLTA-----EEALQHPFF 254
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
46-120 5.81e-24

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 95.45  E-value: 5.81e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81915001     46 KRDYLVDAATQIHLALERDVSEDYEAAFNHYQNGVDVLLRGVHVDPNKERREAVKLKITKYLRRAEEIFNCHLQR 120
Cdd:smart00745   1 TRDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVESDSKRREALKAKAAEYLDRAEEIKKSLLER 75
MIT pfam04212
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
 50-115 3.45e-17

MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric three-helix bundle and binds ESCRT-III (endosomal sorting complexes required for transport) substrates.


Pssm-ID: 461228  Cd Length: 66  Bit Score: 75.66  E-value: 3.45e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81915001    50 LVDAATQIHLALERDVSEDYEAAFNHYQNGVDVLLRGVHVDPNKERREAVKLKITKYLRRAEEIFN 115
Cdd:pfam04212   1 LSKALELVKKAVEEDNAGNYEEALELYKEALDYLLLALKETKNEERRELLRAKIAEYLERAEELKE 66
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
379-517 1.61e-14

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 75.82  E-value: 1.61e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG----QWSEVEPRCSQEAVDCLYSAPEVGGIS 454
Cdd:COG0515 104 LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGiaraLGGATLTQTGTVVGTPGYMAPEQARGE 183

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81915001 455 ELTEACDWWSYGSLLYELLTGMAL--SQSHPSGFQAHTQ----------LQLPEWLSHpaasLLTELLQFEPQRR 517
Cdd:COG0515 184 PVDPRSDVYSLGVTLYELLTGRPPfdGDSPAELLRAHLRepppppselrPDLPPALDA----IVLRALAKDPEER 254
Pkinase pfam00069
Protein kinase domain;
445-534 6.81e-12

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 64.96  E-value: 6.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001   445 YSAPEVGGISELTEACDWWSYGSLLYELLTG-MALSQSHPSGFQAHTQLQLPEWLSHP------AASLLTELLQFEPQRR 517
Cdd:pfam00069 126 YMAPEVLGGNPYGPKVDVWSLGCILYELLTGkPPFPGINGNEIYELIIDQPYAFPELPsnlseeAKDLLKKLLKKDPSKR 205

                          90
                  ....*....|....*..
gi 81915001   518 LGAggggtSRLKSHPFF 534
Cdd:pfam00069 206 LTA-----TQALQHPWF 217
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
386-475 1.12e-04

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 44.79  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001  386 QWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG-----------QWSEVeprcsqeavdcL----YSAPEV 450
Cdd:NF033483 111 EIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGiaralssttmtQTNSV-----------LgtvhYLSPEQ 179

                         90       100
                 ....*....|....*....|....*..
gi 81915001  451 --GGISelTEACDWWSYGSLLYELLTG 475
Cdd:NF033483 180 arGGTV--DARSDIYSLGIVLYEMLTG 204
 
Name Accession Description Interval E-value
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
 148-534 2.90e-139

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: 403.47  E-value: 2.90e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 148 EQLKGCRVVGIIKKVQVVQDPATGGTFIVKSLPRCHMVSRERLTIIPHGVPYMTKLLRYFVSEDSIFLHLEHVQGGTLWS 227
Cdd:cd05576   1 EELKAFRVLGVIDKVLLVMDTRTQETFILKGLRKSSEYSRERKTIIPRCVPNMVCLRKYIISEESVFLVLQHAEGGKLWS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 228 HLLSQDHfqysglnsgsvqEKSQAQLSTRLslmtpaeltpghtlrqnripmepprtsqslppalqlqkeadaepssrpsa 307
Cdd:cd05576  81 YLSKFLN------------DKEIHQLFADL-------------------------------------------------- 98

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 308 vfssdpteapcghshsqvrragqssnpaptqrlhwvregadrvlgaygrgrgrnppsanrASLGSGRAAWSLREGQVKQW 387
Cdd:cd05576  99 ------------------------------------------------------------DERLAAASRFYIPEECIQRW 118

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 388 AAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCLYSAPEVGGISELTEACDWWSYGS 467
Cdd:cd05576 119 AAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIENMYCAPEVGGISEETEACDWWSLGA 198

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81915001 468 LLYELLTGMALSQSHPSGFQAHTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRLKSHPFF 534
Cdd:cd05576 199 LLFELLTGKALVECHPAGINTHTTLNIPEWVSEEARSLLQQLLQFNPTERLGAGVAGVEDIKSHPFF 265
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 378-534 1.61e-47

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: 165.77  E-value: 1.61e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEP---RCSQEAVDCLYSAPEVGGIS 454
Cdd:cd05123  89 RFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSdgdRTYTFCGTPEYLAPEVLLGK 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 455 ELTEACDWWSYGSLLYELLTGMALSQSHPSG--FQ--AHTQLQLPEWLSHPAASLLTELLQFEPQRRLGAggGGTSRLKS 530
Cdd:cd05123 169 GYGKAVDWWSLGVLLYEMLTGKPPFYAENRKeiYEkiLKSPLKFPEYVSPEAKSLISGLLQKDPTKRLGS--GGAEEIKA 246


                ....
gi 81915001 531 HPFF 534
Cdd:cd05123 247 HPFF 250
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
 381-543 2.54e-38

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: 142.92  E-value: 2.54e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGqwseveprCSQEAVD--------C---LYSAPE 449
Cdd:cd05582  96 EEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFG--------LSKESIDhekkaysfCgtvEYMAPE 167

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 450 VGGISELTEACDWWSYGSLLYELLTGMAlsqshPsgFQAHT-----------QLQLPEWLSHPAASLLTELLQFEPQRRL 518
Cdd:cd05582 168 VVNRRGHTQSADWWSFGVLMFEMLTGSL-----P--FQGKDrketmtmilkaKLGMPQFLSPEAQSLLRALFKRNPANRL 240

                       170       180
                ....*....|....*....|....*
gi 81915001 519 GAGGGGTSRLKSHPFFSTIQWSRLM 543
Cdd:cd05582 241 GAGPDGVEEIKRHPFFATIDWNKLY 265
MIT_SNX15 cd02677
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 48-122 1.46e-35

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT domain sub-family is found in sorting nexin 15 and related proteins. The molecular function of the MIT domain is unclear.


Pssm-ID: 239140  Cd Length: 75  Bit Score: 127.46  E-value: 1.46e-35
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81915001  48 DYLVDAATQIHLALERDVSEDYEAAFNHYQNGVDVLLRGVHVDPNKERREAVKLKITKYLRRAEEIFNCHLQRTL 122
Cdd:cd02677   1 DYLEQAAELIRLALEKEEEGDYEAAFEFYRAGVDLLLKGVQGDSSPERREAVKRKIAEYLKRAEEILRLHLSRSL 75
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
 374-542 1.11e-34

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: 132.32  E-value: 1.11e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 374 RAAWSLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCLYSAPEVggI 453
Cdd:cd05580  93 RRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVKDRTYTLCGTPEYLAPEI--I 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 454 SEL--TEACDWWSYGSLLYELLTG---------MALSQSHPSGFqahtqLQLPEWLSHPAASLLTELLQFEPQRRLGAGG 522
Cdd:cd05580 171 LSKghGKAVDWWALGILIYEMLAGyppffdenpMKIYEKILEGK-----IRFPSFFDPDAKDLIKRLLVVDLTKRLGNLK 245

                       170       180
                ....*....|....*....|
gi 81915001 523 GGTSRLKSHPFFSTIQWSRL 542
Cdd:cd05580 246 NGVEDIKNHPWFAGIDWDAL 265
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 380-537 1.94e-34

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: 130.98  E-value: 1.94e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 380 REGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVD-C---LYSAPEV--GGI 453
Cdd:cd05583  97 TESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGENDRAYSfCgtiEYMAPEVvrGGS 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 454 SELTEACDWWSYGSLLYELLTGMA--------LSQSHPSGFQAHTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGT 525
Cdd:cd05583 177 DGHDKAVDWWSLGVLTYELLTGASpftvdgerNSQSEISKRILKSHPPIPKTFSAEAKDFILKLLEKDPKKRLGAGPRGA 256

                       170
                ....*....|..
gi 81915001 526 SRLKSHPFFSTI 537
Cdd:cd05583 257 HEIKEHPFFKGL 268
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
 381-543 2.44e-33

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: 129.45  E-value: 2.44e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEvepRCSQEAVD---C---LYSAPEVGGIS 454
Cdd:cd05584  99 EDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKE---SIHDGTVThtfCgtiEYMAPEILTRS 175

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 455 ELTEACDWWSYGSLLYELLTGmalsqSHPsgFQA-----------HTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGG 523
Cdd:cd05584 176 GHGKAVDWWSLGALMYDMLTG-----APP--FTAenrkktidkilKGKLNLPPYLTNEARDLLKKLLKRNVSSRLGSGPG 248

                       170       180
                ....*....|....*....|
gi 81915001 524 GTSRLKSHPFFSTIQWSRLM 543
Cdd:cd05584 249 DAEEIKAHPFFRHINWDDLL 268
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
 387-542 7.13e-32

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: 125.19  E-value: 7.13e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 387 WAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDC---LYSAPEVGGISELTEACDWW 463
Cdd:cd05592 101 YGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGENKASTFCgtpDYIAPEILKGQKYNQSVDWW 180

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 464 SYGSLLYELLTGmalsQSHPSG------FQA--HTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRLKSHPFFS 535
Cdd:cd05592 181 SFGVLLYEMLIG----QSPFHGededelFWSicNDTPHYPRWLTKEAASCLSLLLERNPEKRLGVPECPAGDIRDHPFFK 256


                ....*..
gi 81915001 536 TIQWSRL 542
Cdd:cd05592 257 TIDWDKL 263
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
 378-539 1.17e-31

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: 123.10  E-value: 1.17e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG--------------QWSEVEPRCSQEAVDC 443
Cdd:cd05579  89 ALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGlskvglvrrqiklsIQKKSNGAPEKEDRRI 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 444 L----YSAPEVGGISELTEACDWWSYGSLLYELLTGMAlsqshPsgFQAHTQLQL-----------PE--WLSHPAASLL 506
Cdd:cd05579 169 VgtpdYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIP-----P--FHAETPEEIfqnilngkiewPEdpEVSDEAKDLI 241

                       170       180       190
                ....*....|....*....|....*....|...
gi 81915001 507 TELLQFEPQRRLGAggGGTSRLKSHPFFSTIQW 539
Cdd:cd05579 242 SKLLTPDPEKRLGA--KGIEEIKNHPFFKGIDW 272
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
 379-539 1.79e-30

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: 119.89  E-value: 1.79e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGqWSEV--EPRCSQEAVDCL-YSAPEVGGISE 455
Cdd:cd05611  94 LPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFG-LSRNglEKRHNKKFVGTPdYLAPETILGVG 172

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 456 LTEACDWWSYGSLLYELLTGmalsqsHPSgFQAHT-----------QLQLP----EWLSHPAASLLTELLQFEPQRRLGA 520
Cdd:cd05611 173 DDKMSDWWSLGCVIFEFLFG------YPP-FHAETpdavfdnilsrRINWPeevkEFCSPEAVDLINRLLCMDPAKRLGA 245

                       170
                ....*....|....*....
gi 81915001 521 GGGgtSRLKSHPFFSTIQW 539
Cdd:cd05611 246 NGY--QEIKSHPFFKSINW 262
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
 381-543 2.15e-30

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: 121.27  E-value: 2.15e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDC---LYSAPEVGGISELT 457
Cdd:cd05575  95 EPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSDTTSTFCgtpEYLAPEVLRKQPYD 174

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 458 EACDWWSYGSLLYELLTGMA--LSQSHPSGFQA--HTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSrLKSHPF 533
Cdd:cd05575 175 RTVDWWCLGAVLYEMLYGLPpfYSRDTAEMYDNilHKPLRLRTNVSPSARDLLEGLLQKDRTKRLGSGNDFLE-IKNHSF 253

                       170
                ....*....|
gi 81915001 534 FSTIQWSRLM 543
Cdd:cd05575 254 FRPINWDDLE 263
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
 385-544 5.35e-30

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 120.31  E-value: 5.35e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001  385 KQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCLYSAPEVGGISELTEACDWWS 464
Cdd:PTZ00263 121 KFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPDRTFTLCGTPEYLAPEVIQSKGHGKAVDWWT 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001  465 YGSLLYELLTGmalsqsHP-----SGFQAHTQ-----LQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRLKSHPFF 534
Cdd:PTZ00263 201 MGVLLYEFIAG------YPpffddTPFRIYEKilagrLKFPNWFDGRARDLVKGLLQTDHTKRLGTLKGGVADVKNHPYF 274

                        170
                 ....*....|
gi 81915001  535 STIQWSRLMG 544
Cdd:PTZ00263 275 HGANWDKLYA 284
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 379-542 2.64e-29

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: 118.10  E-value: 2.64e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQ----WSEVEPRCSQEAVDCLYSAPE-VGGI 453
Cdd:cd05614 102 FSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLskefLTEEKERTYSFCGTIEYMAPEiIRGK 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 454 SELTEACDWWSYGSLLYELLTGMAL--------SQSHPSGFQAHTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGT 525
Cdd:cd05614 182 SGHGKAVDWWSLGILMFELLTGASPftlegeknTQSEVSRRILKCDPPFPSFIGPVARDLLQKLLCKDPKKRLGAGPQGA 261

                       170
                ....*....|....*..
gi 81915001 526 SRLKSHPFFSTIQWSRL 542
Cdd:cd05614 262 QEIKEHPFFKGLDWEAL 278
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
 381-543 2.71e-29

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


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 117.70  E-value: 2.71e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSE-VEPRCSQEAVdC---LYSAPEVggISEL 456
Cdd:cd05570  95 EERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEgIWGGNTTSTF-CgtpDYIAPEI--LREQ 171

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 457 --TEACDWWSYGSLLYELLTGmalsQSHPSG------FQA--HTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTS 526
Cdd:cd05570 172 dyGFSVDWWALGVLLYEMLAG----QSPFEGddedelFEAilNDEVLYPRWLSREAVSILKGLLTKDPARRLGCGPKGEA 247

                       170
                ....*....|....*..
gi 81915001 527 RLKSHPFFSTIQWSRLM 543
Cdd:cd05570 248 DIKAHPFFRNIDWDKLE 264
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 379-542 6.55e-29

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: 116.25  E-value: 6.55e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCL----YSAPEV--GG 452
Cdd:cd05613 102 FTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLDENERAYSFCgtieYMAPEIvrGG 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 453 ISELTEACDWWSYGSLLYELLTGMAL--------SQSHPSGFQAHTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGG 524
Cdd:cd05613 182 DSGHDKAVDWWSLGVLMYELLTGASPftvdgeknSQAEISRRILKSEPPYPQEMSALAKDIIQRLLMKDPKKRLGCGPNG 261

                       170
                ....*....|....*...
gi 81915001 525 TSRLKSHPFFSTIQWSRL 542
Cdd:cd05613 262 ADEIKKHPFFQKINWDDL 279
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
 387-542 3.35e-28

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: 114.76  E-value: 3.35e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 387 WAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQwseveprCSQEAVD-------C---LYSAPEVGGISEL 456
Cdd:cd05571 100 YGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGL-------CKEEISYgattktfCgtpEYLAPEVLEDNDY 172

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 457 TEACDWWSYGSLLYELLTGMA--LSQSHPSGFQ--AHTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRLKSHP 532
Cdd:cd05571 173 GRAVDWWGLGVVMYEMMCGRLpfYNRDHEVLFEliLMEEVRFPSTLSPEAKSLLAGLLKKDPKKRLGGGPRDAKEIMEHP 252

                       170
                ....*....|
gi 81915001 533 FFSTIQWSRL 542
Cdd:cd05571 253 FFASINWDDL 262
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
 380-543 2.23e-27

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: 112.28  E-value: 2.23e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 380 REG-----QVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDC---LYSAPEVG 451
Cdd:cd05585  87 REGrfdlsRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDKTNTFCgtpEYLAPELL 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 452 GISELTEACDWWSYGSLLYELLTGMA--LSQSHPSGFQAHTQ--LQLPEWLSHPAASLLTELLQFEPQRRLGAGGGgtSR 527
Cdd:cd05585 167 LGHGYTKAVDWWTLGVLLYEMLTGLPpfYDENTNEMYRKILQepLRFPDGFDRDAKDLLIGLLNRDPTKRLGYNGA--QE 244

                       170
                ....*....|....*.
gi 81915001 528 LKSHPFFSTIQWSRLM 543
Cdd:cd05585 245 IKNHPFFDQIDWKRLL 260
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
 381-543 5.66e-27

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: 110.22  E-value: 5.66e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCL-YSAPEV--GGISELT 457
Cdd:cd05606  97 EAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHASVGTHgYMAPEVlqKGVAYDS 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 458 EAcDWWSYGSLLYELLTGMALSQSHPSGFQAHT-------QLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRLKS 530
Cdd:cd05606 177 SA-DWFSLGCMLYKLLKGHSPFRQHKTKDKHEIdrmtltmNVELPDSFSPELKSLLEGLLQRDVSKRLGCLGRGATEVKE 255

                       170
                ....*....|...
gi 81915001 531 HPFFSTIQWSRLM 543
Cdd:cd05606 256 HPFFKGVDWQQVY 268
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 378-534 9.19e-27

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 109.16  E-value: 9.19e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001    378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRCSQeavdC---LYSAPEVg 451
Cdd:smart00220  93 RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGlarQLDPGEKLTTF----VgtpEYMAPEV- 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001    452 gISEL--TEACDWWSYGSLLYELLTGMALsqshpsgFQAHTQLQL--------------PEW-LSHPAASLLTELLQFEP 514
Cdd:smart00220 168 -LLGKgyGKAVDIWSLGVILYELLTGKPP-------FPGDDQLLElfkkigkpkppfppPEWdISPEAKDLIRKLLVKDP 239

                          170       180
                   ....*....|....*....|
gi 81915001    515 QRRLGAggggtSRLKSHPFF 534
Cdd:smart00220 240 EKRLTA-----EEALQHPFF 254
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
 381-539 3.16e-26

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: 109.33  E-value: 3.16e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDC---LYSAPEVGGISELT 457
Cdd:cd05595  94 EDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMKTFCgtpEYLAPEVLEDNDYG 173

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 458 EACDWWSYGSLLYELLTGMA--LSQSHPSGFQ--AHTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRLKSHPF 533
Cdd:cd05595 174 RAVDWWGLGVVMYEMMCGRLpfYNQDHERLFEliLMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGGGPSDAKEVMEHRF 253


                ....*.
gi 81915001 534 FSTIQW 539
Cdd:cd05595 254 FLSINW 259
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
 379-542 3.94e-26

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: 108.00  E-value: 3.94e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEP--RCSQEAVDCLYSAPEV--GGIS 454
Cdd:cd05577  92 FSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKGgkKIKGRVGTHGYMAPEVlqKEVA 171

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 455 eLTEACDWWSYGSLLYELLTGMALSQSHPSGFQAH--------TQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTS 526
Cdd:cd05577 172 -YDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEelkrrtleMAVEYPDSFSPEARSLCEGLLQKDPERRLGCRGGSAD 250

                       170
                ....*....|....*.
gi 81915001 527 RLKSHPFFSTIQWSRL 542
Cdd:cd05577 251 EVKEHPFFRSLNWQRL 266
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
 387-542 1.15e-25

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: 106.67  E-value: 1.15e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 387 WAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEA-VDCL-YSAPEVGGISELTEACDWWS 464
Cdd:cd05605 107 YAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGETIRGrVGTVgYMAPEVVKNERYTFSPDWWG 186

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 465 YGSLLYELLTGMAlsqshPsgFQAH---------------TQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRLK 529
Cdd:cd05605 187 LGCLIYEMIEGQA-----P--FRARkekvkreevdrrvkeDQEEYSEKFSEEAKSICSQLLQKDPKTRLGCRGEGAEDVK 259

                       170
                ....*....|...
gi 81915001 530 SHPFFSTIQWSRL 542
Cdd:cd05605 260 SHPFFKSINFKRL 272
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
 387-542 1.16e-25

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: 107.70  E-value: 1.16e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 387 WAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEV---EPRCSQEAVDCLYSAPEVGGISELTEACDWW 463
Cdd:cd05619 111 YAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENmlgDAKTSTFCGTPDYIAPEILLGQKYNTSVDWW 190

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 464 SYGSLLYELLTGMalsqshpSGFQAHTQLQL-----------PEWLSHPAASLLTELLQFEPQRRLGAGGGgtsrLKSHP 532
Cdd:cd05619 191 SFGVLLYEMLIGQ-------SPFHGQDEEELfqsirmdnpfyPRWLEKEAKDILVKLFVREPERRLGVRGD----IRQHP 259

                       170
                ....*....|
gi 81915001 533 FFSTIQWSRL 542
Cdd:cd05619 260 FFREINWEAL 269
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
 381-542 4.01e-25

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: 105.11  E-value: 4.01e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEV-EPRCSQEAVDCL-YSAPEVGGISELTE 458
Cdd:cd05630 101 EARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVpEGQTIKGRVGTVgYMAPEVVKNERYTF 180

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 459 ACDWWSYGSLLYELLTGMALSQSHPSGFQ--------AHTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRLKS 530
Cdd:cd05630 181 SPDWWALGCLLYEMIAGQSPFQQRKKKIKreeverlvKEVPEEYSEKFSPQARSLCSMLLCKDPAERLGCRGGGAREVKE 260

                       170
                ....*....|..
gi 81915001 531 HPFFSTIQWSRL 542
Cdd:cd05630 261 HPLFKKLNFKRL 272
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
 378-534 6.24e-25

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: 104.22  E-value: 6.24e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG--------QWSEVEPRCSQEAVDCL----- 444
Cdd:cd05581  97 SLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGtakvlgpdSSPESTKGDADSQIAYNqaraa 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 445 -------YSAPEVGGISELTEACDWWSYGSLLYELLTGmalsqSHPsgFQAHTQLQL-----------PEWLSHPAASLL 506
Cdd:cd05581 177 sfvgtaeYVSPELLNEKPAGKSSDLWALGCIIYQMLTG-----KPP--FRGSNEYLTfqkivkleyefPENFPPDAKDLI 249

                       170       180
                ....*....|....*....|....*....
gi 81915001 507 TELLQFEPQRRLGAG-GGGTSRLKSHPFF 534
Cdd:cd05581 250 QKLLVLDPSKRLGVNeNGGYDELKAHPFF 278
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
 389-542 1.33e-24

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: 104.71  E-value: 1.33e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 389 AEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG-----QWSEVEPR-CSQEAVDCL-YSAPEVGGISELTEACD 461
Cdd:cd05598 108 AELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfRWTHDSKYyLAHSLVGTPnYIAPEVLLRTGYTQLCD 187

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 462 WWSYGSLLYELLTGMA--LSQShpsgfQAHTQLQLPEW-----------LSHPAASLLTELLQfEPQRRLGAggGGTSRL 528
Cdd:cd05598 188 WWSVGVILYEMLVGQPpfLAQT-----PAETQLKVINWrttlkipheanLSPEAKDLILRLCC-DAEDRLGR--NGADEI 259

                       170
                ....*....|....
gi 81915001 529 KSHPFFSTIQWSRL 542
Cdd:cd05598 260 KAHPFFAGIDWEKL 273
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
 379-539 1.36e-24

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


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 104.24  E-value: 1.36e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYF-------------------GQWSEVEPRCSQE 439
Cdd:cd05574 100 LPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFdlskqssvtpppvrkslrkGSRRSSVKSIEKE 179

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 440 AVDCL-------------YSAPEVGGISELTEACDWWSYGSLLYELLTGMAlsqshPsgFQAHTQ-----------LQLP 495
Cdd:cd05574 180 TFVAEpsarsnsfvgteeYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTT-----P--FKGSNRdetfsnilkkeLTFP 252

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 81915001 496 E--WLSHPAASLLTELLQFEPQRRLGAGGGGtSRLKSHPFFSTIQW 539
Cdd:cd05574 253 EspPVSSEAKDLIRKLLVKDPSKRLGSKRGA-SEIKRHPFFRGVNW 297
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
 380-542 3.49e-24

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: 103.24  E-value: 3.49e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 380 REGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEvepRCSQEAVDCL------YSAPEVGGI 453
Cdd:cd05587  95 KEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKE---GIFGGKTTRTfcgtpdYIAPEIIAY 171

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 454 SELTEACDWWSYGSLLYELLTGmalsQSHPSG------FQAHTQ--LQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGT 525
Cdd:cd05587 172 QPYGKSVDWWAYGVLLYEMLAG----QPPFDGededelFQSIMEhnVSYPKSLSKEAVSICKGLLTKHPAKRLGCGPTGE 247

                       170
                ....*....|....*..
gi 81915001 526 SRLKSHPFFSTIQWSRL 542
Cdd:cd05587 248 RDIKEHPFFRRIDWEKL 264
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
46-120 5.81e-24

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 95.45  E-value: 5.81e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81915001     46 KRDYLVDAATQIHLALERDVSEDYEAAFNHYQNGVDVLLRGVHVDPNKERREAVKLKITKYLRRAEEIFNCHLQR 120
Cdd:smart00745   1 TRDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVESDSKRREALKAKAAEYLDRAEEIKKSLLER 75
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
 378-542 5.86e-24

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: 102.73  E-value: 5.86e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDC---LYSAPEVGGIS 454
Cdd:cd05604  93 SFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTTFCgtpEYLAPEVIRKQ 172

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 455 ELTEACDWWSYGSLLYELLTGMALSQSHPSGFQ----AHTQLQLPEWLSHPAASLLTELLQFEPQRRLGAgGGGTSRLKS 530
Cdd:cd05604 173 PYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMyeniLHKPLVLRPGISLTAWSILEELLEKDRQLRLGA-KEDFLEIKN 251

                       170
                ....*....|..
gi 81915001 531 HPFFSTIQWSRL 542
Cdd:cd05604 252 HPFFESINWTDL 263
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
 379-542 8.65e-24

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: 102.75  E-value: 8.65e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG-----QWSEVEPRCSQEAVDCL--------- 444
Cdd:cd05573  98 FPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGlctkmNKSGDRESYLNDSVNTLfqdnvlarr 177

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 445 ------------------YSAPEVGGISELTEACDWWSYGSLLYELLTGMA-LSQSHPSG-------FQAHtqLQLP--E 496
Cdd:cd05573 178 rphkqrrvraysavgtpdYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPpFYSDSLVEtyskimnWKES--LVFPddP 255

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 81915001 497 WLSHPAASLLTELLQfEPQRRLGAGGGgtsrLKSHPFFSTIQWSRL 542
Cdd:cd05573 256 DVSPEAIDLIRRLLC-DPEDRLGSAEE----IKAHPFFKGIDWENL 296
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
 387-544 1.02e-23

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: 101.94  E-value: 1.02e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 387 WAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEV---EPRCSQEAVDCLYSAPEVGGISELTEACDWW 463
Cdd:cd05620 101 YAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENvfgDNRASTFCGTPDYIAPEILQGLKYTFSVDWW 180

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 464 SYGSLLYELLTGMalsqshpSGFQAHTQLQL-----------PEWLSHPAASLLTELLQFEPQRRLGAGGggtsRLKSHP 532
Cdd:cd05620 181 SFGVLLYEMLIGQ-------SPFHGDDEDELfesirvdtphyPRWITKESKDILEKLFERDPTRRLGVVG----NIRGHP 249

                       170
                ....*....|..
gi 81915001 533 FFSTIQWSRLMG 544
Cdd:cd05620 250 FFKTINWTALEK 261
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
 381-534 1.38e-23

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: 100.02  E-value: 1.38e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPrcSQEAVDCL----YSAPEVGGISEL 456
Cdd:cd05578  99 EETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTD--GTLATSTSgtkpYMAPEVFMRAGY 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 457 TEACDWWSYGSLLYELLTGMALSQSHPSG--------FQAHTQLQLPEWlSHPAASLLTELLQFEPQRRLgaggGGTSRL 528
Cdd:cd05578 177 SFAVDWWSLGVTAYEMLRGKRPYEIHSRTsieeirakFETASVLYPAGW-SEEAIDLINKLLERDPQKRL----GDLSDL 251


                ....*.
gi 81915001 529 KSHPFF 534
Cdd:cd05578 252 KNHPYF 257
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
 379-542 4.43e-23

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: 100.00  E-value: 4.43e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVepRCSQEAVDCL----YSAPEVGGIS 454
Cdd:cd05599  98 LTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGL--KKSHLAYSTVgtpdYIAPEVFLQK 175

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 455 ELTEACDWWSYGSLLYELLTGMA--LSQSHPSGFQA-----HTqLQLPEWLS-HPAASLLTELLQFEPQRRLGAggGGTS 526
Cdd:cd05599 176 GYGKECDWWSLGVIMYEMLIGYPpfCSDDPQETCRKimnwrET-LVFPPEVPiSPEAKDLIERLLCDAEHRLGA--NGVE 252

                       170
                ....*....|....*.
gi 81915001 527 RLKSHPFFSTIQWSRL 542
Cdd:cd05599 253 EIKSHPFFKGVDWDHI 268
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
 381-543 5.45e-23

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: 99.02  E-value: 5.45e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCLYSAPEVGGISELTEAC 460
Cdd:cd14209 100 EPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAV 179

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 461 DWWSYGSLLYELLTGMalsqshpSGFQAHTQLQL-----------PEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRLK 529
Cdd:cd14209 180 DWWALGVLIYEMAAGY-------PPFFADQPIQIyekivsgkvrfPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIK 252

                       170
                ....*....|....
gi 81915001 530 SHPFFSTIQWSRLM 543
Cdd:cd14209 253 NHKWFATTDWIAIY 266
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
 384-539 8.60e-23

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: 98.25  E-value: 8.60e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 384 VKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---------------QWSEVEPRCSQEAVDC---LY 445
Cdd:cd05609 102 ARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGlskiglmslttnlyeGHIEKDTREFLDKQVCgtpEY 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 446 SAPEVGGISELTEACDWWSYGSLLYELLTGMA-LSQSHPSGFQAHT---QLQLPE---WLSHPAASLLTELLQFEPQRRL 518
Cdd:cd05609 182 IAPEVILRQGYGKPVDWWAMGIILYEFLVGCVpFFGDTPEELFGQVisdEIEWPEgddALPDDAQDLITRLLQQNPLERL 261

                       170       180
                ....*....|....*....|.
gi 81915001 519 GAGGGgtSRLKSHPFFSTIQW 539
Cdd:cd05609 262 GTGGA--EEVKQHPFFQDLDW 280
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
 379-542 8.88e-23

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: 99.27  E-value: 8.88e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSE-VEPRCSQEAVdC---LYSAPEVGGIS 454
Cdd:cd05603  93 FLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEgMEPEETTSTF-CgtpEYLAPEVLRKE 171

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 455 ELTEACDWWSYGSLLYELLTGMA--LSQSHPSGFQA--HTQLQLPEWLSHPAASLLTELLQFEPQRRLGAgGGGTSRLKS 530
Cdd:cd05603 172 PYDRTVDWWCLGAVLYEMLYGLPpfYSRDVSQMYDNilHKPLHLPGGKTVAACDLLQGLLHKDQRRRLGA-KADFLEIKN 250

                       170
                ....*....|..
gi 81915001 531 HPFFSTIQWSRL 542
Cdd:cd05603 251 HVFFSPINWDDL 262
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
 381-542 1.02e-22

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


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 99.10  E-value: 1.02e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDC---LYSAPEVGGISELT 457
Cdd:cd05591  95 EPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTTTTFCgtpDYIAPEILQELEYG 174

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 458 EACDWWSYGSLLYELLTGmalsqsHPSgFQA-----------HTQLQLPEWLSHPAASLLTELLQFEPQRRLG--AGGGG 524
Cdd:cd05591 175 PSVDWWALGVLMYEMMAG------QPP-FEAdneddlfesilHDDVLYPVWLSKEAVSILKAFMTKNPAKRLGcvASQGG 247

                       170
                ....*....|....*...
gi 81915001 525 TSRLKSHPFFSTIQWSRL 542
Cdd:cd05591 248 EDAIRQHPFFREIDWEAL 265
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
 381-542 1.82e-22

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: 98.44  E-value: 1.82e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDC---LYSAPEVGGISELT 457
Cdd:cd05590  95 EARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTSTFCgtpDYIAPEILQEMLYG 174

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 458 EACDWWSYGSLLYELLTGMAlsqshpsGFQAHTQLQL-----------PEWLSHPAASLLTELLQFEPQRRLGA-GGGGT 525
Cdd:cd05590 175 PSVDWWAMGVLLYEMLCGHA-------PFEAENEDDLfeailndevvyPTWLSQDAVDILKAFMTKNPTMRLGSlTLGGE 247

                       170
                ....*....|....*..
gi 81915001 526 SRLKSHPFFSTIQWSRL 542
Cdd:cd05590 248 EAILRHPFFKELDWEKL 264
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
 379-542 2.11e-22

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: 99.34  E-value: 2.11e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG-----------QWSEVEP-RCSQEAVDCL-- 444
Cdd:cd05600 108 LSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGlasgtlspkkiESMKIRLeEVKNTAFLELta 187

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 445 --------------------------YSAPEVGGISELTEACDWWSYGSLLYELLTGMA-LSQSHPSGFQAH-----TQL 492
Cdd:cd05600 188 kerrniyramrkedqnyansvvgspdYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPpFSGSTPNETWANlyhwkKTL 267

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 81915001 493 QLPEW--------LSHPAASLLTELLQfEPQRRLgaggGGTSRLKSHPFFSTIQWSRL 542
Cdd:cd05600 268 QRPVYtdpdlefnLSDEAWDLITKLIT-DPQDRL----QSPEQIKNHPFFKNIDWDRL 320
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
 379-542 2.74e-22

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: 97.77  E-value: 2.74e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEprcSQEAVDCL-------YSAPEV- 450
Cdd:cd05601  99 FEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLS---SDKTVTSKmpvgtpdYIAPEVl 175

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 451 -----GGISELTEACDWWSYGSLLYELLTG--------MALSQSHPSGFQahTQLQLPE--WLSHPAASLLTELLQfEPQ 515
Cdd:cd05601 176 tsmngGSKGTYGVECDWWSLGIVAYEMLYGktpftedtVIKTYSNIMNFK--KFLKFPEdpKVSESAVDLIKGLLT-DAK 252

                       170       180
                ....*....|....*....|....*..
gi 81915001 516 RRLGAGGggtsrLKSHPFFSTIQWSRL 542
Cdd:cd05601 253 ERLGYEG-----LCCHPFFSGIDWNNL 274
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
 379-542 3.16e-22

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: 97.88  E-value: 3.16e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDC---LYSAPEVGGISE 455
Cdd:cd05588  93 LPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCgtpNYIAPEILRGED 172

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 456 LTEACDWWSYGSLLYELLTG-----MALSQSHPSG------FQA--HTQLQLPEWLSHPAASLLTELLQFEPQRRLGAG- 521
Cdd:cd05588 173 YGFSVDWWALGVLMFEMLAGrspfdIVGSSDNPDQntedylFQVilEKPIRIPRSLSVKAASVLKGFLNKNPAERLGCHp 252

                       170       180
                ....*....|....*....|.
gi 81915001 522 GGGTSRLKSHPFFSTIQWSRL 542
Cdd:cd05588 253 QTGFADIQSHPFFRTIDWEQL 273
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
 387-542 4.45e-22

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: 96.22  E-value: 4.45e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 387 WAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEV-EPRCSQEAVDCL-YSAPEVGGISELTEACDWWS 464
Cdd:cd05631 107 YAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIpEGETVRGRVGTVgYMAPEVINNEKYTFSPDWWG 186

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 465 YGSLLYELLTGMALSQSHPSGFQ--------AHTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRLKSHPFFST 536
Cdd:cd05631 187 LGCLIYEMIQGQSPFRKRKERVKreevdrrvKEDQEEYSEKFSEDAKSICRMLLTKNPKERLGCRGNGAAGVKQHPIFKN 266


                ....*.
gi 81915001 537 IQWSRL 542
Cdd:cd05631 267 INFKRL 272
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
 379-542 5.22e-22

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: 97.37  E-value: 5.22e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQwseveprCSQEAVDCL----------YSAP 448
Cdd:cd05615 108 FKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGM-------CKEHMVEGVttrtfcgtpdYIAP 180

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 449 EVGGISELTEACDWWSYGSLLYELLTGMAL--SQSHPSGFQA--HTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGG 524
Cdd:cd05615 181 EIIAYQPYGRSVDWWAYGVLLYEMLAGQPPfdGEDEDELFQSimEHNVSYPKSLSKEAVSICKGLMTKHPAKRLGCGPEG 260

                       170
                ....*....|....*...
gi 81915001 525 TSRLKSHPFFSTIQWSRL 542
Cdd:cd05615 261 ERDIREHAFFRRIDWDKL 278
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
 381-539 5.79e-22

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: 97.46  E-value: 5.79e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDC---LYSAPEVGGISELT 457
Cdd:cd05593 114 EDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCgtpEYLAPEVLEDNDYG 193

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 458 EACDWWSYGSLLYELLTGMA--LSQSHPSGFQ--AHTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRLKSHPF 533
Cdd:cd05593 194 RAVDWWGLGVVMYEMMCGRLpfYNQDHEKLFEliLMEDIKFPRTLSADAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSF 273


                ....*.
gi 81915001 534 FSTIQW 539
Cdd:cd05593 274 FTGVNW 279
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
 387-542 6.73e-22

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: 96.61  E-value: 6.73e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 387 WAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQ-----WSEVEPRCSQEAVDclYSAPEVGGISELTEACD 461
Cdd:cd05616 106 YAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMckeniWDGVTTKTFCGTPD--YIAPEIIAYQPYGKSVD 183

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 462 WWSYGSLLYELLTGMAL--SQSHPSGFQA--HTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRLKSHPFFSTI 537
Cdd:cd05616 184 WWAFGVLLYEMLAGQAPfeGEDEDELFQSimEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYI 263


                ....*
gi 81915001 538 QWSRL 542
Cdd:cd05616 264 DWEKL 268
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
 374-539 7.82e-22

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: 95.97  E-value: 7.82e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 374 RAAWSLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCLYSAPEVGGI 453
Cdd:cd05612  93 RNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLRDRTWTLCGTPEYLAPEVIQS 172

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 454 SELTEACDWWSYGSLLYELLTGM-ALSQSHPSG-FQA--HTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRLK 529
Cdd:cd05612 173 KGHNKAVDWWALGILIYEMLVGYpPFFDDNPFGiYEKilAGKLEFPRHLDLYAKDLIKKLLVVDRTRRLGNMKNGADDVK 252

                       170
                ....*....|
gi 81915001 530 SHPFFSTIQW 539
Cdd:cd05612 253 NHRWFKSVDW 262
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
 381-539 2.47e-21

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: 95.48  E-value: 2.47e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALH-QQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDC---LYSAPEVGGISEL 456
Cdd:cd05594 124 EDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCgtpEYLAPEVLEDNDY 203

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 457 TEACDWWSYGSLLYELLTGMA--LSQSHPSGFQA--HTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRLKSHP 532
Cdd:cd05594 204 GRAVDWWGLGVVMYEMMCGRLpfYNQDHEKLFELilMEEIRFPRTLSPEAKSLLSGLLKKDPKQRLGGGPDDAKEIMQHK 283


                ....*..
gi 81915001 533 FFSTIQW 539
Cdd:cd05594 284 FFAGIVW 290
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
 386-540 2.98e-21

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: 95.14  E-value: 2.98e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 386 QWA----AEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEP----RCSQEAVDCLYSAPEV----GGI 453
Cdd:cd05596 125 KWArfytAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCMKMDKdglvRSDTAVGTPDYISPEVlksqGGD 204

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 454 SELTEACDWWSYGSLLYELLTGM------ALSQSHPSGFQAHTQLQLPE--WLSHPAASLLTELLQFEPQrRLGAggGGT 525
Cdd:cd05596 205 GVYGRECDWWSVGVFLYEMLVGDtpfyadSLVGTYGKIMNHKNSLQFPDdvEISKDAKSLICAFLTDREV-RLGR--NGI 281

                       170
                ....*....|....*
gi 81915001 526 SRLKSHPFFSTIQWS 540
Cdd:cd05596 282 EEIKAHPFFKNDQWT 296
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
 389-540 3.43e-21

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: 93.06  E-value: 3.43e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 389 AEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPR------CSQEAvdclYSAPEVGGISELTEACDW 462
Cdd:cd05572 100 ACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSGrktwtfCGTPE----YVAPEIILNKGYDFSVDY 175

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 463 WSYGSLLYELLTGMA-LSQSHPSGFQAHT-------QLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRLKSHPFF 534
Cdd:cd05572 176 WSLGILLYELLTGRPpFGGDDEDPMKIYNiilkgidKIEFPKYIDKNAKNLIKQLLRRNPEERLGYLKGGIRDIKKHKWF 255


                ....*.
gi 81915001 535 STIQWS 540
Cdd:cd05572 256 EGFDWE 261
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
 379-542 5.09e-21

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


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 94.34  E-value: 5.09e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPR---CSQEAV---DclYSAPEV-- 450
Cdd:cd05597  99 LPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSCLKLREDgtvQSSVAVgtpD--YISPEIlq 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 451 ---GGISELTEACDWWSYGSLLYELLTGM------ALSQSHPSGFQAHTQLQLP---EWLSHPAASLLTELLQfEPQRRL 518
Cdd:cd05597 177 ameDGKGRYGPECDWWSLGVCMYEMLYGEtpfyaeSLVETYGKIMNHKEHFSFPddeDDVSEEAKDLIRRLIC-SRERRL 255

                       170       180
                ....*....|....*....|....
gi 81915001 519 GAggGGTSRLKSHPFFSTIQWSRL 542
Cdd:cd05597 256 GQ--NGIDDFKKHPFFEGIDWDNI 277
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
 387-543 5.13e-21

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


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 93.90  E-value: 5.13e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 387 WAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDC---LYSAPEVGGISELTEACDWW 463
Cdd:cd05589 106 YAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGDRTSTFCgtpEFLAPEVLTDTSYTRAVDWW 185

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 464 SYGSLLYELLTGmalsQSHPSG------FQA--HTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRLKSHPFFS 535
Cdd:cd05589 186 GLGVLIYEMLVG----ESPFPGddeeevFDSivNDEVRYPRFLSTEAISIMRRLLRKNPERRLGASERDAEDVKKQPFFR 261


                ....*...
gi 81915001 536 TIQWSRLM 543
Cdd:cd05589 262 NIDWEALL 269
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
 381-543 7.76e-21

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: 93.93  E-value: 7.76e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSE-VEPRcSQEAVDC---LYSAPEVGGISEL 456
Cdd:cd05602 107 EPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKEnIEPN-GTTSTFCgtpEYLAPEVLHKQPY 185

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 457 TEACDWWSYGSLLYELLTGMALSQSHPSGFQ----AHTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTsRLKSHP 532
Cdd:cd05602 186 DRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMydniLNKPLQLKPNITNSARHLLEGLLQKDRTKRLGAKDDFT-EIKNHI 264

                       170
                ....*....|.
gi 81915001 533 FFSTIQWSRLM 543
Cdd:cd05602 265 FFSPINWDDLI 275
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
 379-542 8.54e-21

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: 93.93  E-value: 8.54e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDC---LYSAPEVGGISE 455
Cdd:cd05617 113 LPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCgtpNYIAPEILRGEE 192

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 456 LTEACDWWSYGSLLYELLTGMA---LSQSHPSG------FQA--HTQLQLPEWLSHPAASLLTELLQFEPQRRLGAG-GG 523
Cdd:cd05617 193 YGFSVDWWALGVLMFEMMAGRSpfdIITDNPDMntedylFQVilEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCQpQT 272

                       170
                ....*....|....*....
gi 81915001 524 GTSRLKSHPFFSTIQWSRL 542
Cdd:cd05617 273 GFSDIKSHTFFRSIDWDLL 291
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
 381-539 2.51e-20

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: 92.03  E-value: 2.51e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCL-YSAPEV--GGISELT 457
Cdd:cd14223 102 EAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKKKPHASVGTHgYMAPEVlqKGVAYDS 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 458 EAcDWWSYGSLLYELLTGMALSQSHPSGFQAHTQ-------LQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRLKS 530
Cdd:cd14223 182 SA-DWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDrmtltmaVELPDSFSPELRSLLEGLLQRDVNRRLGCMGRGAQEVKE 260


                ....*....
gi 81915001 531 HPFFSTIQW 539
Cdd:cd14223 261 EPFFRGLDW 269
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
 381-542 3.70e-20

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: 92.05  E-value: 3.70e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCL-YSAPEV-GGISELTE 458
Cdd:cd05633 107 EKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHASVGTHgYMAPEVlQKGTAYDS 186

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 459 ACDWWSYGSLLYELLTGMALSQSHPSG-------FQAHTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRLKSH 531
Cdd:cd05633 187 SADWFSLGCMLFKLLRGHSPFRQHKTKdkheidrMTLTVNVELPDSFSPELKSLLEGLLQRDVSKRLGCHGRGAQEVKEH 266

                       170
                ....*....|.
gi 81915001 532 PFFSTIQWSRL 542
Cdd:cd05633 267 SFFKGIDWQQV 277
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
 385-540 5.72e-20

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: 91.99  E-value: 5.72e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 385 KQWA----AEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEP----RCSQEAVDCLYSAPEV----GG 452
Cdd:cd05622 171 EKWArfytAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKegmvRCDTAVGTPDYISPEVlksqGG 250

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 453 ISELTEACDWWSYGSLLYELLTG------MALSQSHPSGFQAHTQLQLPE--WLSHPAASLLTELLQfepQRRLGAGGGG 524
Cdd:cd05622 251 DGYYGRECDWWSVGVFLYEMLVGdtpfyaDSLVGTYSKIMNHKNSLTFPDdnDISKEAKNLICAFLT---DREVRLGRNG 327

                       170
                ....*....|....*.
gi 81915001 525 TSRLKSHPFFSTIQWS 540
Cdd:cd05622 328 VEEIKRHLFFKNDQWA 343
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
 377-540 7.36e-20

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: 91.60  E-value: 7.36e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 377 WSLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEP----RCSQEAVDCLYSAPEV-- 450
Cdd:cd05621 146 YDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKMDEtgmvHCDTAVGTPDYISPEVlk 225

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 451 --GGISELTEACDWWSYGSLLYELLTG------MALSQSHPSGFQAHTQLQLPE--WLSHPAASLLTELLQfepQRRLGA 520
Cdd:cd05621 226 sqGGDGYYGRECDWWSVGVFLFEMLVGdtpfyaDSLVGTYSKIMDHKNSLNFPDdvEISKHAKNLICAFLT---DREVRL 302

                       170       180
                ....*....|....*....|
gi 81915001 521 GGGGTSRLKSHPFFSTIQWS 540
Cdd:cd05621 303 GRNGVEEIKQHPFFRNDQWN 322
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
 379-542 1.43e-19

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: 89.65  E-value: 1.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEV-EPRCSQEAVDCL-YSAPEVGGISEL 456
Cdd:cd05632 101 FEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIpEGESIRGRVGTVgYMAPEVLNNQRY 180

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 457 TEACDWWSYGSLLYELLTGMALSQSHPSGFQ--------AHTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRL 528
Cdd:cd05632 181 TLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKreevdrrvLETEEVYSAKFSEEAKSICKMLLTKDPKQRLGCQEEGAGEV 260

                       170
                ....*....|....
gi 81915001 529 KSHPFFSTIQWSRL 542
Cdd:cd05632 261 KRHPFFRNMNFKRL 274
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
 379-542 2.96e-19

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 90.07  E-value: 2.96e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG------QWSEVEPRCSQEAVDclYSAPEV-- 450
Cdd:cd05624 170 LPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGsclkmnDDGTVQSSVAVGTPD--YISPEIlq 247

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 451 ---GGISELTEACDWWSYGSLLYELLTG------MALSQSHPSGFQAHTQLQLPEWL---SHPAASLLTELLqFEPQRRL 518
Cdd:cd05624 248 ameDGMGKYGPECDWWSLGVCMYEMLYGetpfyaESLVETYGKIMNHEERFQFPSHVtdvSEEAKDLIQRLI-CSRERRL 326

                       170       180
                ....*....|....*....|....
gi 81915001 519 GAggGGTSRLKSHPFFSTIQWSRL 542
Cdd:cd05624 327 GQ--NGIEDFKKHAFFEGLNWENI 348
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
 387-542 6.10e-19

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: 87.24  E-value: 6.10e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 387 WAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQwsEVEPRCSQEAVDCL-----YSAPEVGGISELTEACD 461
Cdd:cd05608 110 YTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGL--AVELKDGQTKTKGYagtpgFMAPELLLGEEYDYSVD 187

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 462 WWSYGSLLYELLT--------GMALSQSHPSGFQAHTQLQLPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRLKSHPF 533
Cdd:cd05608 188 YFTLGVTLYEMIAargpfrarGEKVENKELKQRILNDSVTYSEKFSPASKSICEALLAKDPEKRLGFRDGNCDGLRTHPF 267


                ....*....
gi 81915001 534 FSTIQWSRL 542
Cdd:cd05608 268 FRDINWRKL 276
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
 379-539 7.43e-19

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 88.17  E-value: 7.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDC---LYSAPEVGGISE 455
Cdd:cd05618 118 LPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCgtpNYIAPEILRGED 197

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 456 LTEACDWWSYGSLLYELLTG-----MALSQSHPSG------FQA--HTQLQLPEWLSHPAASLLTELLQFEPQRRLGA-G 521
Cdd:cd05618 198 YGFSVDWWALGVLMFEMMAGrspfdIVGSSDNPDQntedylFQVilEKQIRIPRSLSVKAASVLKSFLNKDPKERLGChP 277

                       170
                ....*....|....*...
gi 81915001 522 GGGTSRLKSHPFFSTIQW 539
Cdd:cd05618 278 QTGFADIQGHPFFRNVDW 295
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
 387-540 1.30e-18

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: 87.76  E-value: 1.30e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 387 WAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQ-----------------------------WSEV----- 432
Cdd:cd05626 106 YIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLctgfrwthnskyyqkgshirqdsmepsdlWDDVsncrc 185

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 433 -------EPRCSQEAVDCL---------YSAPEVGGISELTEACDWWSYGSLLYELLTGM-ALSQSHPSgfqaHTQLQLP 495
Cdd:cd05626 186 gdrlktlEQRATKQHQRCLahslvgtpnYIAPEVLLRKGYTQLCDWWSVGVILFEMLVGQpPFLAPTPT----ETQLKVI 261

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 81915001 496 EW-----------LSHPAASLLTELLQFEPQRrlgAGGGGTSRLKSHPFFSTIQWS 540
Cdd:cd05626 262 NWentlhippqvkLSPEAVDLITKLCCSAEER---LGRNGADDIKAHPFFSEVDFS 314
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
 381-533 2.80e-18

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: 84.45  E-value: 2.80e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGqWSEVEPRCSQEAV----DclYSAPEVGGISEL 456
Cdd:cd14007  99 EKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFG-WSVHAPSNRRKTFcgtlD--YLPPEMVEGKEY 175

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 457 TEACDWWSYGSLLYELLTGMAlsqshPsgFQAHTQ-----------LQLPEWLSHPAASLLTELLQFEPQRRLGAggggt 525
Cdd:cd14007 176 DYKVDIWSLGVLCYELLVGKP-----P--FESKSHqetykriqnvdIKFPSSVSPEAKDLISKLLQKDPSKRLSL----- 243


                ....*...
gi 81915001 526 SRLKSHPF 533
Cdd:cd14007 244 EQVLNHPW 251
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
 387-540 1.56e-17

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: 84.71  E-value: 1.56e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 387 WAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG-----------------------------QWSE------ 431
Cdd:cd05625 106 YIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrwthdskyyqsgdhlrqdsmdfsnEWGDpencrc 185

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 432 ------VEPRCSQEAVDCL---------YSAPEVGGISELTEACDWWSYGSLLYELLTGMA--LSQShpsgfQAHTQLQL 494
Cdd:cd05625 186 gdrlkpLERRAARQHQRCLahslvgtpnYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPpfLAQT-----PLETQMKV 260

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 81915001 495 PEW-----------LSHPAASLLTELLQfEPQRRLGAggGGTSRLKSHPFFSTIQWS 540
Cdd:cd05625 261 INWqtslhippqakLSPEASDLIIKLCR-GPEDRLGK--NGADEIKAHPFFKTIDFS 314
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
 379-533 2.23e-17

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: 81.79  E-value: 2.23e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVdC---LYSAPEV-GGIS 454
Cdd:cd14003  96 LSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGGSLLKTF-CgtpAYAAPEVlLGRK 174

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 455 ELTEACDWWSYGSLLYELLTG---------MALSQShpsgfQAHTQLQLPEWLSHPAASLLTELLQFEPQRRLgagggGT 525
Cdd:cd14003 175 YDGPKADVWSLGVILYAMLTGylpfdddndSKLFRK-----ILKGKYPIPSHLSPDARDLIRRMLVVDPSKRI-----TI 244


                ....*...
gi 81915001 526 SRLKSHPF 533
Cdd:cd14003 245 EEILNHPW 252
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
 381-542 2.48e-17

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: 83.39  E-value: 2.48e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQwseVEPRCSQEAVD---C---LYSAPEVgGIS 454
Cdd:cd05586  95 EDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGL---SKADLTDNKTTntfCgttEYLAPEV-LLD 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 455 E--LTEACDWWSYGSLLYELLTGMA--LSQSHPSGFQ--AHTQLQLP-EWLSHPAASLLTELLQFEPQRRLGAGGGGTsR 527
Cdd:cd05586 171 EkgYTKMVDFWSLGVLVFEMCCGWSpfYAEDTQQMYRniAFGKVRFPkDVLSDEGRSFVKGLLNRNPKHRLGAHDDAV-E 249

                       170
                ....*....|....*
gi 81915001 528 LKSHPFFSTIQWSRL 542
Cdd:cd05586 250 LKEHPFFADIDWDLL 264
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
 387-543 3.06e-17

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 83.11  E-value: 3.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001  387 WAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCLYSAPEVGGISELTEACDWWSYG 466
Cdd:PTZ00426 136 YAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVDTRTYTLCGTPEYIAPEILLNVGHGKAADWWTLG 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001  467 SLLYELLTGMALSQSHPSGFQAHTQLQ----LPEWLSHPAASLLTELLQFEPQRRLGAGGGGTSRLKSHPFFSTIQWSRL 542
Cdd:PTZ00426 216 IFIYEILVGCPPFYANEPLLIYQKILEgiiyFPKFLDNNCKHLMKKLLSHDLTKRYGNLKKGAQNVKEHPWFGNIDWVSL 295


                 .
gi 81915001  543 M 543
Cdd:PTZ00426 296 L 296
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
 379-542 3.18e-17

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: 83.91  E-value: 3.18e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEV-EPRCSQEAVDC---LYSAPEV---- 450
Cdd:cd05623 170 LPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLmEDGTVQSSVAVgtpDYISPEIlqam 249

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 451 -GGISELTEACDWWSYGSLLYELLTG------MALSQSHPSGFQAHTQLQLPEWL---SHPAASLLTELLQFEPQRrlgA 520
Cdd:cd05623 250 eDGKGKYGPECDWWSLGVCMYEMLYGetpfyaESLVETYGKIMNHKERFQFPTQVtdvSENAKDLIRRLICSREHR---L 326

                       170       180
                ....*....|....*....|..
gi 81915001 521 GGGGTSRLKSHPFFSTIQWSRL 542
Cdd:cd05623 327 GQNGIEDFKNHPFFVGIDWDNI 348
MIT pfam04212
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
 50-115 3.45e-17

MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric three-helix bundle and binds ESCRT-III (endosomal sorting complexes required for transport) substrates.


Pssm-ID: 461228  Cd Length: 66  Bit Score: 75.66  E-value: 3.45e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81915001    50 LVDAATQIHLALERDVSEDYEAAFNHYQNGVDVLLRGVHVDPNKERREAVKLKITKYLRRAEEIFN 115
Cdd:pfam04212   1 LSKALELVKKAVEEDNAGNYEEALELYKEALDYLLLALKETKNEERRELLRAKIAEYLERAEELKE 66
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
 378-542 1.27e-16

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: 81.64  E-value: 1.27e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG------------------------------ 427
Cdd:cd05627  98 TLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGlctglkkahrtefyrnlthnppsdfsfqnm 177

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 428 -------QWSEVEPRCSQEAVDCL-YSAPEVGGISELTEACDWWSYGSLLYELLTGMALSQSHPSGFQAHTQLQLPEWLS 499
Cdd:cd05627 178 nskrkaeTWKKNRRQLAYSTVGTPdYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYRKVMNWKETLV 257

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 81915001 500 HPAASLLTE-----LLQFEPQRRLGAGGGGTSRLKSHPFFSTIQWSRL 542
Cdd:cd05627 258 FPPEVPISEkakdlILRFCTDAENRIGSNGVEEIKSHPFFEGVDWEHI 305
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
 389-542 1.62e-16

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: 81.43  E-value: 1.62e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 389 AEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG------------------QWSEVEPRCSQE---AVDCL--- 444
Cdd:cd05629 108 AECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGlstgfhkqhdsayyqkllQGKSNKNRIDNRnsvAVDSInlt 187

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 445 --------------------------YSAPEVGGISELTEACDWWSYGSLLYELLTG---MALSQSHPSGFQ----AHTq 491
Cdd:cd05629 188 msskdqiatwkknrrlmaystvgtpdYIAPEIFLQQGYGQECDWWSLGAIMFECLIGwppFCSENSHETYRKiinwRET- 266

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 81915001 492 LQLPE--WLSHPAASLLTELLQfEPQRRLGAGGGgtSRLKSHPFFSTIQWSRL 542
Cdd:cd05629 267 LYFPDdiHLSVEAEDLIRRLIT-NAENRLGRGGA--HEIKSHPFFRGVDWDTI 316
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
 379-532 2.30e-16

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: 78.08  E-value: 2.30e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDC-----LYSAPEVGGI 453
Cdd:cd00180  89 LSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGgttppYYAPPELLGG 168

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81915001 454 SELTEACDWWSYGSLLYElltgmalsqshpsgfqahtqlqLPEwlshpAASLLTELLQFEPQRRLGAggggtSRLKSHP 532
Cdd:cd00180 169 RYYGPKVDIWSLGVILYE----------------------LEE-----LKDLIRRMLQYDPKKRPSA-----KELLEHL 215
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
 379-532 5.06e-16

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: 78.19  E-value: 5.06e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG--------QWSEVEPRCSQEAvdclYSAPE- 449
Cdd:cd14078  98 LSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGlcakpkggMDHHLETCCGSPA----YAAPEl 173

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 450 VGGISELTEACDWWSYGSLLYELLTG---------MALSQSHPSGfqahtQLQLPEWLSHPAASLLTELLQFEPQRRLga 520
Cdd:cd14078 174 IQGKPYIGSEADVWSMGVLLYALLCGflpfdddnvMALYRKIQSG-----KYEEPEWLSPSSKLLLDQMLQVDPKKRI-- 246

                       170
                ....*....|..
gi 81915001 521 gggGTSRLKSHP 532
Cdd:cd14078 247 ---TVKELLNHP 255
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
 378-533 6.12e-16

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: 77.90  E-value: 6.12e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLL---DQAGHIQLTYFGQWSEVEPRCSQEAVdC---LYSAPEVG 451
Cdd:cd05117  95 SFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLAKIFEEGEKLKTV-CgtpYYVAPEVL 173

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 452 GISELTEACDWWSYGSLLYELLTGmalsqSHPsgFQAHTQLQL-------------PEW--LSHPAASLLTELLQFEPQR 516
Cdd:cd05117 174 KGKGYGKKCDIWSLGVILYILLCG-----YPP--FYGETEQELfekilkgkysfdsPEWknVSEEAKDLIKRLLVVDPKK 246

                       170
                ....*....|....*..
gi 81915001 517 RLGAggggtSRLKSHPF 533
Cdd:cd05117 247 RLTA-----AEALNHPW 258
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
 374-517 1.39e-15

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: 76.86  E-value: 1.39e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 374 RAAWSLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG--QW--SEVEPRCSQEAVDCLYSAPE 449
Cdd:cd14014  92 RERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGiaRAlgDSGLTQTGSVLGTPAYMAPE 171

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 450 VGGISELTEACDWWSYGSLLYELLTG------------MALSQSHPSGFQAHTQLQLPEWLshpaASLLTELLQFEPQRR 517
Cdd:cd14014 172 QARGGPVDPRSDIYSLGVVLYELLTGrppfdgdspaavLAKHLQEAPPPPSPLNPDVPPAL----DAIILRALAKDPEER 247
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 379-534 2.59e-15

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: 75.73  E-value: 2.59e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQA-GHIQLTYFGQWSEVEPRCSQEAVDCL-YSAPEV-GGISE 455
Cdd:cd05118  98 LPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLElGQLKLADFGLARSFTSPPYTPYVATRwYRAPEVlLGAKP 177

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 456 LTEACDWWSYGSLLYELLTGMAL-SQSHPsgfqaHTQLQLPEWL--SHPAASLLTELLQFEPQRRLGAggggtSRLKSHP 532
Cdd:cd05118 178 YGSSIDIWSLGCILAELLTGRPLfPGDSE-----VDQLAKIVRLlgTPEALDLLSKMLKYDPAKRITA-----SQALAHP 247


                ..
gi 81915001 533 FF 534
Cdd:cd05118 248 YF 249
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
 379-533 3.89e-15

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: 75.79  E-value: 3.89e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGqWSEVE---------PRCSQEAVDC------ 443
Cdd:cd14010  91 LPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFG-LARREgeilkelfgQFSDEGNVNKvskkqa 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 444 -----LYSAPEVGGISELTEACDWWSYGSLLYELLTGmalsqsHPSgFQAHTQLQLPEW-LSHPA--------------- 502
Cdd:cd14010 170 krgtpYYMAPELFQGGVHSFASDLWALGCVLYEMFTG------KPP-FVAESFTELVEKiLNEDPpppppkvsskpspdf 242

                       170       180       190
                ....*....|....*....|....*....|.
gi 81915001 503 ASLLTELLQFEPQRRLgagggGTSRLKSHPF 533
Cdd:cd14010 243 KSLLKGLLEKDPAKRL-----SWDELVKHPF 268
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
 381-534 6.27e-15

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: 74.57  E-value: 6.27e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRcSQEAVDCLY-SAPEVGGISEL 456
Cdd:cd06627  98 ESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGvatKLNEVEKD-ENSVVGTPYwMAPEVIEMSGV 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 457 TEACDWWSYGSLLYELLTG---------MA-----LSQSHPSgfqahtqlqLPEWLSHPAASLLTELLQFEPQRRLGAgg 522
Cdd:cd06627 177 TTASDIWSVGCTVIELLTGnppyydlqpMAalfriVQDDHPP---------LPENISPELRDFLLQCFQKDPTLRPSA-- 245

                       170
                ....*....|..
gi 81915001 523 ggtSRLKSHPFF 534
Cdd:cd06627 246 ---KELLKHPWL 254
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
 378-534 8.14e-15

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: 74.55  E-value: 8.14e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCS-QEAVDCL-YSAPEVGGISE 455
Cdd:cd05122  94 TLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKTrNTFVGTPyWMAPEVIQGKP 173

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 456 LTEACDWWSYGSLLYELLTGMA-LSQSHPS------GFQAHTQLQLPEWLSHPAASLLTELLQFEPQRRLGAggggtSRL 528
Cdd:cd05122 174 YGFKADIWSLGITAIEMAEGKPpYSELPPMkalfliATNGPPGLRNPKKWSKEFKDFLKKCLQKDPEKRPTA-----EQL 248


                ....*.
gi 81915001 529 KSHPFF 534
Cdd:cd05122 249 LKHPFI 254
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
379-517 1.61e-14

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 75.82  E-value: 1.61e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG----QWSEVEPRCSQEAVDCLYSAPEVGGIS 454
Cdd:COG0515 104 LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGiaraLGGATLTQTGTVVGTPGYMAPEQARGE 183

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81915001 455 ELTEACDWWSYGSLLYELLTGMAL--SQSHPSGFQAHTQ----------LQLPEWLSHpaasLLTELLQFEPQRR 517
Cdd:COG0515 184 PVDPRSDVYSLGVTLYELLTGRPPfdGDSPAELLRAHLRepppppselrPDLPPALDA----IVLRALAKDPEER 254
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
 378-534 5.07e-14

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: 72.22  E-value: 5.07e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGqwseVEPRCSQEAVDCL---------YSAP 448
Cdd:cd14080  98 ALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFG----FARLCPDDDGDVLsktfcgsaaYAAP 173

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 449 EV-GGISELTEACDWWSYGSLLYELLTG-MALSQSHPSGfQAHTQLQ-------LPEWLSHPAASLLTELLQFEPQRRLG 519
Cdd:cd14080 174 EIlQGIPYDPKKYDIWSLGVILYIMLCGsMPFDDSNIKK-MLKDQQNrkvrfpsSVKKLSPECKDLIDQLLEPDPTKRAT 252

                       170
                ....*....|....*
gi 81915001 520 AGgggtsRLKSHPFF 534
Cdd:cd14080 253 IE-----EILNHPWL 262
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
 381-542 6.65e-14

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: 72.99  E-value: 6.65e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGqWSEVEPRCSQEAVDCL---------------- 444
Cdd:cd05610 103 EEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFG-LSKVTLNRELNMMDILttpsmakpkndysrtp 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 445 -----------------------------------------YSAPEVGGISELTEACDWWSYGSLLYELLTGM-ALSQSH 482
Cdd:cd05610 182 gqvlslisslgfntptpyrtpksvrrgaarvegerilgtpdYLAPELLLGKPHGPAVDWWALGVCLFEFLTGIpPFNDET 261

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81915001 483 PSG-FQAHTQLQLP-----EWLSHPAASLLTELLQFEPQRRLGAggggtSRLKSHPFFSTIQWSRL 542
Cdd:cd05610 262 PQQvFQNILNRDIPwpegeEELSVNAQNAIEILLTMDPTKRAGL-----KELKQHPLFHGVDWENL 322
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
 378-542 8.53e-14

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: 73.15  E-value: 8.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCL------------- 444
Cdd:cd05628  97 TLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKKAHRTEFYRNLnhslpsdftfqnm 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 445 -------------------------YSAPEVGGISELTEACDWWSYGSLLYELLTGMALSQSHPSGFQAHTQLQLPEWLS 499
Cdd:cd05628 177 nskrkaetwkrnrrqlafstvgtpdYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYKKVMNWKETLI 256

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 81915001 500 HPAASLLTE-----LLQF--EPQRRLGAggGGTSRLKSHPFFSTIQWSRL 542
Cdd:cd05628 257 FPPEVPISEkakdlILRFccEWEHRIGA--PGVEEIKTNPFFEGVDWEHI 304
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
 379-518 1.91e-13

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: 70.88  E-value: 1.91e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLL---DQAGHIQLTYFGQWSEVEPRCSQEAVdC---LYSAPEV-- 450
Cdd:cd14084 108 LKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLssqEEECLIKITDFGLSKILGETSLMKTL-CgtpTYLAPEVlr 186

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 451 -GGISELTEACDWWSYGSLLYELL----------TGMALSQSHPSGFQAHTQlqlPEW--LSHPAASLLTELLQFEPQRR 517
Cdd:cd14084 187 sFGTEGYTRAVDCWSLGVILFICLsgyppfseeyTQMSLKEQILSGKYTFIP---KAWknVSEEAKDLVKKMLVVDPSRR 263


                .
gi 81915001 518 L 518
Cdd:cd14084 264 P 264
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
 383-517 3.20e-13

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: 69.49  E-value: 3.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 383 QVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGqWSEVEPRCSQEAVDCLYS----APEVGGISELTE 458
Cdd:cd13999  92 LRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFG-LSRIKNSTTEKMTGVVGTprwmAPEVLRGEPYTE 170

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81915001 459 ACDWWSYGSLLYELLTGMALSQSHPSGFQA------HTQLQLPEWLSHPAASLLTELLQFEPQRR 517
Cdd:cd13999 171 KADVYSFGIVLWELLTGEVPFKELSPIQIAaavvqkGLRPPIPPDCPPELSKLIKRCWNEDPEKR 235
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
 379-534 3.86e-13

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: 69.50  E-value: 3.86e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQwSEVEPRCSQEAVDC----LYSAPEV--GG 452
Cdd:cd14008 105 LPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGV-SEMFEDGNDTLQKTagtpAFLAPELcdGD 183

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 453 ISEL-TEACDWWSYGSLLYELLTGMalsqsHPsgFQAHTQLQL-------------PEWLSHPAASLLTELLQFEPQRRL 518
Cdd:cd14008 184 SKTYsGKAADIWALGVTLYCLVFGR-----LP--FNGDNILELyeaiqnqndefpiPPELSPELKDLLRRMLEKDPEKRI 256

                       170
                ....*....|....*.
gi 81915001 519 GAggggtSRLKSHPFF 534
Cdd:cd14008 257 TL-----KEIKEHPWV 267
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
 379-534 4.38e-13

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: 69.82  E-value: 4.38e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRCSQEAVDCLYSAPEV-GGIS 454
Cdd:cd07829  95 LPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGlarAFGIPLRTYTHEVVTLWYRAPEIlLGSK 174

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 455 ELTEACDWWSYGSLLYELLTGMAL--SQSH-------------PS-----GFQA--HTQLQLPEWLSHP----------- 501
Cdd:cd07829 175 HYSTAVDIWSVGCIFAELITGKPLfpGDSEidqlfkifqilgtPTeeswpGVTKlpDYKPTFPKWPKNDlekvlprldpe 254

                       170       180       190
                ....*....|....*....|....*....|...
gi 81915001 502 AASLLTELLQFEPQRRLGAGGGgtsrLKsHPFF 534
Cdd:cd07829 255 GIDLLSKMLQYNPAKRISAKEA----LK-HPYF 282
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
 378-533 5.79e-13

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: 68.82  E-value: 5.79e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGqwseveprcSQEAVDC------------LY 445
Cdd:cd14002  95 TLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFG---------FARAMSCntlvltsikgtpLY 165

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 446 SAPEVggISE--LTEACDWWSYGSLLYELLTGmalsqSHPsgFQAHTQLQL-----------PEWLSHPAASLLTELLQF 512
Cdd:cd14002 166 MAPEL--VQEqpYDHTADLWSLGCILYELFVG-----QPP--FYTNSIYQLvqmivkdpvkwPSNMSPEFKSFLQGLLNK 236

                       170       180
                ....*....|....*....|.
gi 81915001 513 EPQRRLgagggGTSRLKSHPF 533
Cdd:cd14002 237 DPSKRL-----SWPDLLEHPF 252
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
 379-534 1.00e-12

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: 68.35  E-value: 1.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDC---LYSAPEV--GGI 453
Cdd:cd14099  98 LTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGERKKTLCgtpNYIAPEVleKKK 177

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 454 SELTEAcDWWSYGSLLYELLTGmalsqsHPSgFQA-----------HTQLQLPE--WLSHPAASLLTELLQFEPQRRLGA 520
Cdd:cd14099 178 GHSFEV-DIWSLGVILYTLLVG------KPP-FETsdvketykrikKNEYSFPShlSISDEAKDLIRSMLQPDPTKRPSL 249

                       170
                ....*....|....
gi 81915001 521 ggggtSRLKSHPFF 534
Cdd:cd14099 250 -----DEILSHPFF 258
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
 379-518 2.42e-12

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: 67.04  E-value: 2.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---------QWSEVEPRCSQEAvdclYSAPE 449
Cdd:cd14663  97 LKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGlsalseqfrQDGLLHTTCGTPN----YVAPE 172

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 450 VggiseLTE------ACDWWSYGSLLYELLTG---------MALSQSHPSGfqahtQLQLPEWLSHPAASLLTELLQFEP 514
Cdd:cd14663 173 V-----LARrgydgaKADIWSCGVILFVLLAGylpfddenlMALYRKIMKG-----EFEYPRWFSPGAKSLIKRILDPNP 242


                ....
gi 81915001 515 QRRL 518
Cdd:cd14663 243 STRI 246
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
 379-536 2.84e-12

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: 67.60  E-value: 2.84e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRCSQEAVDCLYSAPEV-GGIS 454
Cdd:cd07841  99 LTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGlarSFGSPNRKMTHQVVTRWYRAPELlFGAR 178

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 455 ELTEACDWWSYGSLLYELLTGM-----------------ALSQSHPSGFQAHTQLQLP-EWLSHP---------AAS--- 504
Cdd:cd07841 179 HYGVGVDMWSVGCIFAELLLRVpflpgdsdidqlgkifeALGTPTEENWPGVTSLPDYvEFKPFPptplkqifpAASdda 258

                       170       180       190
                ....*....|....*....|....*....|....
gi 81915001 505 --LLTELLQFEPQRRLGAggggTSRLKsHPFFST 536
Cdd:cd07841 259 ldLLQRLLTLNPNKRITA----RQALE-HPYFSN 287
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 384-534 3.16e-12

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: 67.41  E-value: 3.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 384 VKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG--QWSEVEPRC-SQEAVDCLYSAPEV-GGISELTEA 459
Cdd:cd07844 100 VRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGlaRAKSVPSKTySNEVVTLWYRPPDVlLGSTEYSTS 179

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 460 CDWWSYGSLLYELLTGMALsqsHPSGFQAHTQLQL-----------------------PEWLSHP--------------- 501
Cdd:cd07844 180 LDMWGVGCIFYEMATGRPL---FPGSTDVEDQLHKifrvlgtpteetwpgvssnpefkPYSFPFYpprplinhaprldri 256

                       170       180       190
                ....*....|....*....|....*....|....*
gi 81915001 502 --AASLLTELLQFEPQRRLGAggggtSRLKSHPFF 534
Cdd:cd07844 257 phGEELALKFLQYEPKKRISA-----AEAMKHPYF 286
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
 385-519 4.75e-12

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: 66.09  E-value: 4.75e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 385 KQWAAemllALEALHQQGVLCRDLNPQNLLLDQAGH---IQLTYFG------QWSEVEPRCSQEavdcLYSAPEVGGISE 455
Cdd:cd14009  99 QQLAS----GLKFLRSKNIIHRDLKPQNLLLSTSGDdpvLKIADFGfarslqPASMAETLCGSP----LYMAPEILQFQK 170

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81915001 456 LTEACDWWSYGSLLYELLTGmalsqsHPSgFQAHTQLQL---------------PEWLSHPAASLLTELLQFEPQRRLG 519
Cdd:cd14009 171 YDAKADLWSVGAILFEMLVG------KPP-FRGSNHVQLlrniersdavipfpiAAQLSPDCKDLLRRLLRRDPAERIS 242
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 394-534 5.39e-12

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: 66.94  E-value: 5.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 394 ALEALHQQGVLCRDLNPQNLLLDQAG---HIQLTYFGqWSEVEPRCSQEAVDCL---YSAPEV----GGISELTEACDWW 463
Cdd:cd14092 111 AVSFMHSKGVVHRDLKPENLLFTDEDddaEIKIVDFG-FARLKPENQPLKTPCFtlpYAAPEVlkqaLSTQGYDESCDLW 189

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 464 SYGSLLYELLTGMALSQSHPSGFQAHTQLQL----------PEW--LSHPAASLLTELLQFEPQRRLGAggggtSRLKSH 531
Cdd:cd14092 190 SLGVILYTMLSGQVPFQSPSRNESAAEIMKRiksgdfsfdgEEWknVSSEAKSLIQGLLTVDPSKRLTM-----SELRNH 264


                ...
gi 81915001 532 PFF 534
Cdd:cd14092 265 PWL 267
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
 379-517 6.69e-12

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: 65.95  E-value: 6.69e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGqwsevEPRCSQEAVDC--------LYSAPEV 450
Cdd:cd08215 100 FPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFG-----ISKVLESTTDLaktvvgtpYYLSPEL 174

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 451 ggiselteaC---------DWWSYGSLLYELLTGmalsqSHPsgFQAHTQLQL------------PEWLSHPAASLLTEL 509
Cdd:cd08215 175 ---------CenkpynyksDIWALGCVLYELCTL-----KHP--FEANNLPALvykivkgqyppiPSQYSSELRDLVNSM 238


                ....*...
gi 81915001 510 LQFEPQRR 517
Cdd:cd08215 239 LQKDPEKR 246
Pkinase pfam00069
Protein kinase domain;
445-534 6.81e-12

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 64.96  E-value: 6.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001   445 YSAPEVGGISELTEACDWWSYGSLLYELLTG-MALSQSHPSGFQAHTQLQLPEWLSHP------AASLLTELLQFEPQRR 517
Cdd:pfam00069 126 YMAPEVLGGNPYGPKVDVWSLGCILYELLTGkPPFPGINGNEIYELIIDQPYAFPELPsnlseeAKDLLKKLLKKDPSKR 205

                          90
                  ....*....|....*..
gi 81915001   518 LGAggggtSRLKSHPFF 534
Cdd:pfam00069 206 LTA-----TQALQHPWF 217
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
 383-534 1.81e-11

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: 64.83  E-value: 1.81e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 383 QVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG--QWSEVEPRC-SQEAVDCLYSAPEV-GGISELTE 458
Cdd:cd07860 101 LIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGlaRAFGVPVRTyTHEVVTLWYRAPEIlLGCKYYST 180

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 459 ACDWWSYGSLLYELLTGMAL-----------------SQSHPSGFQAHTQL-----QLPEW-----------LSHPAASL 505
Cdd:cd07860 181 AVDIWSLGCIFAEMVTRRALfpgdseidqlfrifrtlGTPDEVVWPGVTSMpdykpSFPKWarqdfskvvppLDEDGRDL 260

                       170       180
                ....*....|....*....|....*....
gi 81915001 506 LTELLQFEPQRRLGAGGGgtsrlKSHPFF 534
Cdd:cd07860 261 LSQMLHYDPNKRISAKAA-----LAHPFF 284
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
 384-537 1.94e-11

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: 65.02  E-value: 1.94e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 384 VKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG--QWSEVEPRC-SQEAVDCLYSAPEV-GGISELTEA 459
Cdd:cd07873 102 VKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGlaRAKSIPTKTySNEVVTLWYRPPDIlLGSTDYSTQ 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 460 CDWWSYGSLLYELLTGMALSQSHPSGFQAHTQLQL-----------------------PEW-----------LSHPAASL 505
Cdd:cd07873 182 IDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRIlgtpteetwpgilsneefksynyPKYradalhnhaprLDSDGADL 261

                       170       180       190
                ....*....|....*....|....*....|..
gi 81915001 506 LTELLQFEPQRRLGAggggtSRLKSHPFFSTI 537
Cdd:cd07873 262 LSKLLQFEGRKRISA-----EEAMKHPYFHSL 288
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
 381-534 2.16e-11

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: 65.08  E-value: 2.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQ---EAVDCLYSAPEV-GGISEL 456
Cdd:cd07845 107 ESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTYGLPAKPmtpKVVTLWYRAPELlLGCTTY 186

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 457 TEACDWWSYGSLLYELLTGMAL----SQSH-----------PS-----GFQA---HTQLQLPE-----------WLSHPA 502
Cdd:cd07845 187 TTAIDMWAVGCILAELLAHKPLlpgkSEIEqldliiqllgtPNesiwpGFSDlplVGKFTLPKqpynnlkhkfpWLSEAG 266

                       170       180       190
                ....*....|....*....|....*....|..
gi 81915001 503 ASLLTELLQFEPQRRLGAggggTSRLKsHPFF 534
Cdd:cd07845 267 LRLLNFLLMYDPKKRATA----EEALE-SSYF 293
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
 378-534 2.26e-11

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: 64.55  E-value: 2.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVdC---LYSAPEVGGIS 454
Cdd:cd14182 106 TLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLDPGEKLREV-CgtpGYLAPEIIECS 184

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 455 ELTE------ACDWWSYGSLLYELLTG---------MALSQSHPSGfqaHTQLQLPEW--LSHPAASLLTELLQFEPQRR 517
Cdd:cd14182 185 MDDNhpgygkEVDMWSTGVIMYTLLAGsppfwhrkqMLMLRMIMSG---NYQFGSPEWddRSDTVKDLISRFLVVQPQKR 261

                       170
                ....*....|....*..
gi 81915001 518 LGAggggtSRLKSHPFF 534
Cdd:cd14182 262 YTA-----EEALAHPFF 273
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
 390-534 2.72e-11

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: 63.81  E-value: 2.72e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWS-EVEPRCSQEAVDCL-YSAPEV-GGISELTEACDWWSYG 466
Cdd:cd14081 109 QIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASlQPEGSLLETSCGSPhYACPEViKGEKYDGRKADIWSCG 188

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81915001 467 SLLYELLTGmAL---SQSHPSGFQA--HTQLQLPEWLSHPAASLLTELLQFEPQRRLgagggGTSRLKSHPFF 534
Cdd:cd14081 189 VILYALLVG-ALpfdDDNLRQLLEKvkRGVFHIPHFISPDAQDLLRRMLEVNPEKRI-----TIEEIKKHPWF 255
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
 378-534 4.25e-11

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: 63.78  E-value: 4.25e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRCSQEAVDCLYSAPEV-GGI 453
Cdd:cd07843 102 PFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGlarEYGSPLKPYTQLVVTLWYRAPELlLGA 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 454 SELTEACDWWSYGSLLYELLTGMALSQSH-------------------------------PSGFQAHTQLQLPE-----W 497
Cdd:cd07843 182 KEYSTAIDMWSVGCIFAELLTKKPLFPGKseidqlnkifkllgtptekiwpgfselpgakKKTFTKYPYNQLRKkfpalS 261

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 81915001 498 LSHPAASLLTELLQFEPQRRLGAggggTSRLKsHPFF 534
Cdd:cd07843 262 LSDNGFDLLNRLLTYDPAKRISA----EDALK-HPYF 293
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
 366-517 4.99e-11

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: 63.17  E-value: 4.99e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 366 NRASLGSGRAAWS----LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAV 441
Cdd:cd13997  83 ENGSLQDALEELSpiskLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLETSGDVEEG 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 442 DCLYSAPEV-GGISELTEACDWWSYGSLLYELLTGMALSQSHPSGFQAHT-QLQLPEWLSHPA--ASLLTELLQFEPQRR 517
Cdd:cd13997 163 DSRYLAPELlNENYTHLPKADIFSLGVTVYEAATGEPLPRNGQQWQQLRQgKLPLPPGLVLSQelTRLLKVMLDPDPTRR 242
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
 378-533 5.04e-11

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: 63.32  E-value: 5.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEP----------RCS-QEAVdcLYS 446
Cdd:cd06628 102 AFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLEAnslstknngaRPSlQGSV--FWM 179

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 447 APEVGGISELTEACDWWSYGSLLYELLTGmalsqSHPsgFQAHTQLQ------------LPEWLSHPAASLLTELLQFEP 514
Cdd:cd06628 180 APEVVKQTSYTRKADIWSLGCLVVEMLTG-----THP--FPDCTQMQaifkigenasptIPSNISSEARDFLEKTFEIDH 252

                       170
                ....*....|....*....
gi 81915001 515 QRRLGAggggtSRLKSHPF 533
Cdd:cd06628 253 NKRPTA-----DELLKHPF 266
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
 379-478 5.24e-11

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: 63.50  E-value: 5.24e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQ----WSEVEPRCSQEAVDCLYSAPEV-GGI 453
Cdd:cd07832  97 LTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLarlfSEEDPRLYSHQVATRWYRAPELlYGS 176

                        90       100
                ....*....|....*....|....*
gi 81915001 454 SELTEACDWWSYGSLLYELLTGMAL 478
Cdd:cd07832 177 RKYDEGVDLWAVGCIFAELLNGSPL 201
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
 390-518 5.63e-11

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: 63.05  E-value: 5.63e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGqWSeVEPRCSQEAVDC---LYSAPEVGGISELTEACDWWSYG 466
Cdd:cd14116 113 ELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFG-WS-VHAPSSRRTTLCgtlDYLPPEMIEGRMHDEKVDLWSLG 190

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 81915001 467 SLLYELLTGMA--LSQSHPSGFQA--HTQLQLPEWLSHPAASLLTELLQFEPQRRL 518
Cdd:cd14116 191 VLCYEFLVGKPpfEANTYQETYKRisRVEFTFPDFVTEGARDLISRLLKHNPSQRP 246
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 394-535 6.46e-11

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: 63.52  E-value: 6.46e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 394 ALEALHQQGVLCRDLNPQNLLL---DQAGHIQLTYFGqWSEVEPRCSQE-AVDCL---YSAPEVGGISELTEACDWWSYG 466
Cdd:cd14179 114 AVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFG-FARLKPPDNQPlKTPCFtlhYAAPELLNYNGYDESCDLWSLG 192

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 467 SLLYELLTGMALSQSHPSGFQAHTQLQLPE-------------W--LSHPAASLLTELLQFEPQRRLGAGG-------GG 524
Cdd:cd14179 193 VILYTMLSGQVPFQCHDKSLTCTSAEEIMKkikqgdfsfegeaWknVSQEAKDLIQGLLTVDPNKRIKMSGlrynewlQD 272

                       170
                ....*....|.
gi 81915001 525 TSRLKSHPFFS 535
Cdd:cd14179 273 GSQLSSNPLMT 283
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
 378-534 6.78e-11

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: 63.07  E-value: 6.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPR------CSQEAvdclYSAPEVG 451
Cdd:cd14181 112 TLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHLEPGeklrelCGTPG----YLAPEIL 187

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 452 GIS--ELTEA----CDWWSYGSLLYELLTGmalsqSHPSG-----------FQAHTQLQLPEW--LSHPAASLLTELLQF 512
Cdd:cd14181 188 KCSmdETHPGygkeVDLWACGVILFTLLAG-----SPPFWhrrqmlmlrmiMEGRYQFSSPEWddRSSTVKDLISRLLVV 262

                       170       180
                ....*....|....*....|..
gi 81915001 513 EPQRRLGAggggtSRLKSHPFF 534
Cdd:cd14181 263 DPEIRLTA-----EQALQHPFF 279
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
 381-534 7.21e-11

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: 62.73  E-value: 7.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEV----EPRCSQEAVDCL-YSAPEV-GGIS 454
Cdd:cd14069  99 EDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFrykgKERLLNKMCGTLpYVAPELlAKKK 178

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 455 ELTEACDWWSYGSLLYELLTG-------MALSQSHpSGFQAHTQLQLPEW--LSHPAASLLTELLQFEPQRRLGAGGggt 525
Cdd:cd14069 179 YRAEPVDVWSCGIVLFAMLAGelpwdqpSDSCQEY-SDWKENKKTYLTPWkkIDTAALSLLRKILTENPNKRITIED--- 254


                ....*....
gi 81915001 526 srLKSHPFF 534
Cdd:cd14069 255 --IKKHPWY 261
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
 384-534 1.29e-10

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: 62.33  E-value: 1.29e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 384 VKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG--QWSEVEPRC-SQEAVDCLYSAPEV-GGISELTEA 459
Cdd:cd07871 105 VKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGlaRAKSVPTKTySNEVVTLWYRPPDVlLGSTEYSTP 184

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 460 CDWWSYGSLLYELLTGMAL---------------------SQSHP--SGFQAHTQLQLPEWLSHP-----------AASL 505
Cdd:cd07871 185 IDMWGVGCILYEMATGRPMfpgstvkeelhlifrllgtptEETWPgvTSNEEFRSYLFPQYRAQPlinhaprldtdGIDL 264

                       170       180
                ....*....|....*....|....*....
gi 81915001 506 LTELLQFEPQRRLGAGGGgtsrlKSHPFF 534
Cdd:cd07871 265 LSSLLLYETKSRISAEAA-----LRHSYF 288
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
 379-534 1.78e-10

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: 61.91  E-value: 1.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRCSQeAVDCLYSAPEVGGISE 455
Cdd:cd07838 104 LPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGlarIYSFEMALTSV-VVTLWYRAPEVLLQSS 182

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 456 LTEACDWWSYGSLLYEL---------------------LTGM----------ALSQSH-PSGFQAHTQLQLPEwLSHPAA 503
Cdd:cd07838 183 YATPVDMWSVGCIFAELfnrrplfrgsseadqlgkifdVIGLpseeewprnsALPRSSfPSYTPRPFKSFVPE-IDEEGL 261

                       170       180       190
                ....*....|....*....|....*....|.
gi 81915001 504 SLLTELLQFEPQRRLGAggggtSRLKSHPFF 534
Cdd:cd07838 262 DLLKKMLTFNPHKRISA-----FEALQHPYF 287
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 389-517 2.25e-10

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: 61.40  E-value: 2.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 389 AEMLLALEALH-----QQGVLCRDLNPQNLLLDQAGHIQLTYFGqWSEVEPRCSQEAVDC----LYSAPEVggISEL--T 457
Cdd:cd08217 112 TQLLLALYECHnrsvgGGKILHRDLKPANIFLDSDNNVKLGDFG-LARVLSHDSSFAKTYvgtpYYMSPEL--LNEQsyD 188

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81915001 458 EACDWWSYGSLLYELLTGmalsqSHPsgFQAHTQLQL------------PEWLSHPAASLLTELLQFEPQRR 517
Cdd:cd08217 189 EKSDIWSLGCLIYELCAL-----HPP--FQAANQLELakkikegkfpriPSRYSSELNEVIKSMLNVDPDKR 253
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
 379-534 2.25e-10

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: 61.66  E-value: 2.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAV---DCLYSAPEVGGISE 455
Cdd:cd06656 112 MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTmvgTPYWMAPEVVTRKA 191

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 456 LTEACDWWSYGSLLYELLTGM-------ALSQSHPSGFQAHTQLQLPEWLSHPAASLLTELLQFEPQRRlgaggGGTSRL 528
Cdd:cd06656 192 YGPKVDIWSLGIMAIEMVEGEppylnenPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVDRR-----GSAKEL 266


                ....*.
gi 81915001 529 KSHPFF 534
Cdd:cd06656 267 LQHPFL 272
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
 379-533 2.40e-10

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: 61.16  E-value: 2.40e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPR---CSQEAVDCL-----YSAPEV 450
Cdd:cd06626  96 LDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNtttMAPGEVNSLvgtpaYMAPEV 175

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 451 ---GGISELTEACDWWSYGSLLYELLTGMALSQSHPSGFQ------AHTQLQLPE--WLSHPAASLLTELLQFEPQRRLG 519
Cdd:cd06626 176 itgNKGEGHGRAADIWSLGCVVLEMATGKRPWSELDNEWAimyhvgMGHKPPIPDslQLSPEGKDFLSRCLESDPKKRPT 255

                       170
                ....*....|....
gi 81915001 520 AggggtSRLKSHPF 533
Cdd:cd06626 256 A-----SELLDHPF 264
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
 374-518 2.49e-10

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: 61.10  E-value: 2.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 374 RAAWSLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDC---LYSAPEV 450
Cdd:cd14189  93 KARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRKKTICgtpNYLAPEV 172

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81915001 451 GGISELTEACDWWSYGSLLYELLTG------MALSQSHPSGFQAHtqLQLPEWLSHPAASLLTELLQFEPQRRL 518
Cdd:cd14189 173 LLRQGHGPESDVWSLGCVMYTLLCGnppfetLDLKETYRCIKQVK--YTLPASLSLPARHLLAGILKRNPGDRL 244
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
 383-542 2.60e-10

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: 61.46  E-value: 2.60e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 383 QVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVE--PRCSQEAVDCLYSAPEVGGISELTEAC 460
Cdd:cd05607 105 RVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKegKPITQRAGTNGYMAPEILKEESYSYPV 184

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 461 DWWSYGSLLYELLTGMALSQSHPSG----------FQAHTQLQLPEWlSHPAASLLTELLQFEPQRRLGAGGGGTSRLKs 530
Cdd:cd05607 185 DWFAMGCSIYEMVAGRTPFRDHKEKvskeelkrrtLEDEVKFEHQNF-TEEAKDICRLFLAKKPENRLGSRTNDDDPRK- 262

                       170
                ....*....|..
gi 81915001 531 HPFFSTIQWSRL 542
Cdd:cd05607 263 HEFFKSINFPRL 274
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
 381-534 2.62e-10

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: 61.43  E-value: 2.62e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG----QWSEVEPRCSQEAVDCLYSAPEV-GGISE 455
Cdd:cd07840 103 ESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGlarpYTKENNADYTNRVITLWYRPPELlLGATR 182

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 456 LTEACDWWSYGSLLYELLTGMALsqshpsgFQAHT---QL-------------------QLP------------------ 495
Cdd:cd07840 183 YGPEVDMWSVGCILAELFTGKPI-------FQGKTeleQLekifelcgspteenwpgvsDLPwfenlkpkkpykrrlrev 255

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 81915001 496 --EWLSHPAASLLTELLQFEPQRRLGAggggTSRLkSHPFF 534
Cdd:cd07840 256 fkNVIDPSALDLLDKLLTLDPKKRISA----DQAL-QHEYF 291
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
 384-534 2.80e-10

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: 61.36  E-value: 2.80e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 384 VKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQA-GHIQLTYFG---QWSEVEPR----CSQeavdcLYSAPE-VGGIS 454
Cdd:cd14137 108 VKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPEtGVLKLCDFGsakRLVPGEPNvsyiCSR-----YYRAPElIFGAT 182

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 455 ELTEACDWWSYGSLLYELLTGMAL--------------------------SQSHPSGFQAHTQLQ-------LPEWLSHP 501
Cdd:cd14137 183 DYTTAIDIWSAGCVLAELLLGQPLfpgessvdqlveiikvlgtptreqikAMNPNYTEFKFPQIKphpwekvFPKRTPPD 262

                       170       180       190
                ....*....|....*....|....*....|...
gi 81915001 502 AASLLTELLQFEPQRRLGAggggtSRLKSHPFF 534
Cdd:cd14137 263 AIDLLSKILVYNPSKRLTA-----LEALAHPFF 290
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
 379-534 3.17e-10

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: 61.22  E-value: 3.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPrcSQEAVDCL----YSAPEV---- 450
Cdd:cd14093 106 LSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDE--GEKLRELCgtpgYLAPEVlkcs 183

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 451 --GGISELTEACDWWSYGSLLYELLTGMAlsqshPsgFQAHTQLQL-------------PEW--LSHPAASLLTELLQFE 513
Cdd:cd14093 184 myDNAPGYGKEVDMWACGVIMYTLLAGCP-----P--FWHRKQMVMlrnimegkyefgsPEWddISDTAKDLISKLLVVD 256

                       170       180
                ....*....|....*....|.
gi 81915001 514 PQRRLGAggggtSRLKSHPFF 534
Cdd:cd14093 257 PKKRLTA-----EEALEHPFF 272
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 381-517 3.65e-10

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: 60.81  E-value: 3.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLL---LDQAGHIQLTYFGqWSEVEPRCSQEAVDC---LYSAPEVGGIS 454
Cdd:cd14167 100 ERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFG-LSKIEGSGSVMSTACgtpGYVAPEVLAQK 178

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81915001 455 ELTEACDWWSYGSLLYELLTGMA--LSQSHPSGFQ----AHTQLQLPEW--LSHPAASLLTELLQFEPQRR 517
Cdd:cd14167 179 PYSKAVDCWSIGVIAYILLCGYPpfYDENDAKLFEqilkAEYEFDSPYWddISDSAKDFIQHLMEKDPEKR 249
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
 378-519 4.81e-10

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: 60.54  E-value: 4.81e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGqWSEVEPRCSQEAVDC--LY-SAPEVGGIS 454
Cdd:cd14077 109 KLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFG-LSNLYDPRRLLRTFCgsLYfAAPELLQAQ 187

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 455 ELT-EACDWWSYGSLLYELLTG-MALSQSHPSGFQAHTQ---LQLPEWLSHPAASLLTELLQFEPQRRLG 519
Cdd:cd14077 188 PYTgPEVDVWSFGVVLYVLVCGkVPFDDENMPALHAKIKkgkVEYPSYLSSECKSLISRMLVVDPKKRAT 257
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
 379-517 6.38e-10

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: 59.83  E-value: 6.38e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWS---------EVEPRCSQEAvdclYSAPE 449
Cdd:cd14070 100 LEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNcagilgysdPFSTQCGSPA----YAAPE 175

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81915001 450 VGGISELTEACDWWSYGSLLYELLTGMALSQSHPSGFQA-HTQL------QLPEWLSHPAASLLTELLQFEPQRR 517
Cdd:cd14070 176 LLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEPFSLRAlHQKMvdkemnPLPTDLSPGAISFLRSLLEPDPLKR 250
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
 379-534 6.84e-10

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: 59.94  E-value: 6.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEA--VDCLY-SAPEVGGISE 455
Cdd:cd06647 100 MDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRStmVGTPYwMAPEVVTRKA 179

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 456 LTEACDWWSYGSLLYELLTGM-------ALSQSHPSGFQAHTQLQLPEWLSHPAASLLTELLQFEPQRRlgaggGGTSRL 528
Cdd:cd06647 180 YGPKVDIWSLGIMAIEMVEGEppylnenPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKR-----GSAKEL 254


                ....*.
gi 81915001 529 KSHPFF 534
Cdd:cd06647 255 LQHPFL 260
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
 378-520 8.16e-10

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: 59.67  E-value: 8.16e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLL---DQAGHIQLTYFGQWSEVEPRCS-QEAVDCL-YSAPEVGG 452
Cdd:cd14106 104 CLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLtseFPLGDIKLCDFGISRVIGEGEEiREILGTPdYVAPEILS 183

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 453 ISELTEACDWWSYGSLLYELLTGMalsqshpSGFQAHT-----------QLQLPEWL----SHPAASLLTELLQFEPQRR 517
Cdd:cd14106 184 YEPISLATDMWSIGVLTYVLLTGH-------SPFGGDDkqetflnisqcNLDFPEELfkdvSPLAIDFIKRLLVKDPEKR 256


                ...
gi 81915001 518 LGA 520
Cdd:cd14106 257 LTA 259
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
 373-533 8.62e-10

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: 59.62  E-value: 8.62e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 373 GRAAWSLREgqvkqwAAEML----LALEALHQQGVLCRDLNPQNLLL---DQAGHIQLTYFGQWSE--VEPRCSQEAVDC 443
Cdd:cd14172  96 GDQAFTERE------ASEIMrdigTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTDFGFAKEttVQNALQTPCYTP 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 444 LYSAPEVGGISELTEACDWWSYGSLLYELL---------TGMALSQSHPSGFQ-AHTQLQLPEW--LSHPAASLLTELLQ 511
Cdd:cd14172 170 YYVAPEVLGPEKYDKSCDMWSLGVIMYILLcgfppfysnTGQAISPGMKRRIRmGQYGFPNPEWaeVSEEAKQLIRHLLK 249

                       170       180
                ....*....|....*....|..
gi 81915001 512 FEPQRRLgagggGTSRLKSHPF 533
Cdd:cd14172 250 TDPTERM-----TITQFMNHPW 266
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
 379-534 9.32e-10

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: 60.12  E-value: 9.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAV---DCLYSAPEVGGISE 455
Cdd:cd06655 112 MDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKRSTmvgTPYWMAPEVVTRKA 191

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 456 LTEACDWWSYGSLLYELLTGM-------ALSQSHPSGFQAHTQLQLPEWLSHPAASLLTELLQFEPQRRlgaggGGTSRL 528
Cdd:cd06655 192 YGPKVDIWSLGIMAIEMVEGEppylnenPLRALYLIATNGTPELQNPEKLSPIFRDFLNRCLEMDVEKR-----GSAKEL 266


                ....*.
gi 81915001 529 KSHPFF 534
Cdd:cd06655 267 LQHPFL 272
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
 378-535 9.60e-10

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: 59.15  E-value: 9.60e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWS-EVEPRCSQeaVDCLY-SAPEVGG 452
Cdd:cd06614  93 RMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGfaaQLTkEKSKRNSV--VGTPYwMAPEVIK 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 453 ISELTEACDWWSYGSLLYELLTG----------MALsqshpsgFQAHT----QLQLPEWLSHPAASLLTELLQFEPQRRL 518
Cdd:cd06614 171 RKDYGPKVDIWSLGIMCIEMAEGeppyleepplRAL-------FLITTkgipPLKNPEKWSPEFKDFLNKCLVKDPEKRP 243

                       170
                ....*....|....*..
gi 81915001 519 GAggggtSRLKSHPFFS 535
Cdd:cd06614 244 SA-----EELLQHPFLK 255
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
 379-534 1.28e-09

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: 59.42  E-value: 1.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVE---PRCSQEAVDCLYSAPEV-GGIS 454
Cdd:cd07836  97 LDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFGipvNTFSNEVVTLWYRAPDVlLGSR 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 455 ELTEACDWWSYGSLLYELLTGMALSqshpSGFQAHTQL-------------------QLPEW-----------------L 498
Cdd:cd07836 177 TYSTSIDIWSVGCIMAEMITGRPLF----PGTNNEDQLlkifrimgtptestwpgisQLPEYkptfpryppqdlqqlfpH 252

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 81915001 499 SHPAA-SLLTELLQFEPQRRLGAggggTSRLKsHPFF 534
Cdd:cd07836 253 ADPLGiDLLHRLLQLNPELRISA----HDALQ-HPWF 284
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
 378-534 1.28e-09

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: 59.23  E-value: 1.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG--QWSEVEPRC-SQEAVDCLYSAPEV--GG 452
Cdd:cd07835  95 GLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGlaRAFGVPVRTyTHEVVTLWYRAPEIllGS 174

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 453 ISELTeACDWWSYGSLLYELLTGMAL-----------------SQSHPSGFQAHTQLQ-----LPEW-----------LS 499
Cdd:cd07835 175 KHYST-PVDIWSVGCIFAEMVTRRPLfpgdseidqlfrifrtlGTPDEDVWPGVTSLPdykptFPKWarqdlskvvpsLD 253

                       170       180       190
                ....*....|....*....|....*....|....*
gi 81915001 500 HPAASLLTELLQFEPQRRLGAggggtSRLKSHPFF 534
Cdd:cd07835 254 EDGLDLLSQMLVYDPAKRISA-----KAALQHPYF 283
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
 395-533 1.35e-09

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: 59.65  E-value: 1.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 395 LEALHQQGVLCRDLNPQNLL-LDQAGH---IQLTYFGQWSEVEPRCSQEAVDCL---YSAPEVGGISELTEACDWWSYGS 467
Cdd:cd14176 126 VEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCYtanFVAPEVLERQGYDAACDIWSLGV 205

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81915001 468 LLYELLTGMALSQSHPSGFQAHTQLQLPE---------W--LSHPAASLLTELLQFEPQRRLGAggggtSRLKSHPF 533
Cdd:cd14176 206 LLYTMLTGYTPFANGPDDTPEEILARIGSgkfslsggyWnsVSDTAKDLVSKMLHVDPHQRLTA-----ALVLRHPW 277
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
 390-518 1.52e-09

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: 59.11  E-value: 1.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGqWSEVEPRCSQEAV--DCLYSAPEVGGISELTEACDWWSYGS 467
Cdd:cd14117 114 ELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFG-WSVHAPSLRRRTMcgTLDYLPPEMIEGRTHDEKVDLWCIGV 192

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 81915001 468 LLYELLTGMAL--SQSHPSGFQ--AHTQLQLPEWLSHPAASLLTELLQFEPQRRL 518
Cdd:cd14117 193 LCYELLVGMPPfeSASHTETYRriVKVDLKFPPFLSDGSRDLISKLLRYHPSERL 247
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
 384-534 1.99e-09

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: 58.43  E-value: 1.99e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 384 VKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQ--AGHIQLTYFGQWSEVEPRCSQEAVDCLYSAPEVggISEL--TEA 459
Cdd:cd14133 104 IRKIAQQILEALVFLHSLGLIHCDLKPENILLASysRCQIKIIDFGSSCFLTQRLYSYIQSRYYRAPEV--ILGLpyDEK 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 460 CDWWSYGSLLYELLTGMALSQSHPSGFQAHTQLQL----PEW-LSHPAA------SLLTELLQFEPQRRLGAggggtSRL 528
Cdd:cd14133 182 IDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTigipPAHmLDQGKAddelfvDFLKKLLEIDPKERPTA-----SQA 256


                ....*.
gi 81915001 529 KSHPFF 534
Cdd:cd14133 257 LSHPWL 262
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
 378-475 2.23e-09

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: 58.05  E-value: 2.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLD--QAGHIQLTYFGQWSEVEPRCSQeavDCLYS-----APEV 450
Cdd:cd14006  85 SLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLAdrPSPQIKIIDFGLARKLNPGEEL---KEIFGtpefvAPEI 161

                        90       100
                ....*....|....*....|....*
gi 81915001 451 GGISELTEACDWWSYGSLLYELLTG 475
Cdd:cd14006 162 VNGEPVSLATDMWSIGVLTYVLLSG 186
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
 395-520 2.83e-09

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: 58.50  E-value: 2.83e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 395 LEALHQQGVLCRDLNPQNLL-LDQAGH---IQLTYFGQWSEVEPRCSQEAVDCL---YSAPEVGGISELTEACDWWSYGS 467
Cdd:cd14175 108 VEYLHSQGVVHRDLKPSNILyVDESGNpesLRICDFGFAKQLRAENGLLMTPCYtanFVAPEVLKRQGYDEGCDIWSLGI 187

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81915001 468 LLYELLTGMALSQSHPSGF---------QAHTQLQLPEW--LSHPAASLLTELLQFEPQRRLGA 520
Cdd:cd14175 188 LLYTMLAGYTPFANGPSDTpeeiltrigSGKFTLSGGNWntVSDAAKDLVSKMLHVDPHQRLTA 251
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
 379-534 2.88e-09

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: 58.58  E-value: 2.88e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAV---DCLYSAPEVGGISE 455
Cdd:cd06654 113 MDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTmvgTPYWMAPEVVTRKA 192

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 456 LTEACDWWSYGSLLYELLTGM-------ALSQSHPSGFQAHTQLQLPEWLSHPAASLLTELLQFEPQRRlgaggGGTSRL 528
Cdd:cd06654 193 YGPKVDIWSLGIMAIEMIEGEppylnenPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKR-----GSAKEL 267


                ....*.
gi 81915001 529 KSHPFF 534
Cdd:cd06654 268 LQHQFL 273
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
 354-517 3.66e-09

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: 57.74  E-value: 3.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 354 YGRGrgrnpPSANRASLGSGRAAWSLREGQVK-----QWAAEMLLALEALHQQGV---LCRDLNPQN-LLLDQAGH---- 420
Cdd:cd14146  74 FARG-----GTLNRALAAANAAPGPRRARRIPphilvNWAVQIARGMLYLHEEAVvpiLHRDLKSSNiLLLEKIEHddic 148

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 421 ---IQLTYFG---QWSevepRCSQEAVDCLYS--APEVGGISELTEACDWWSYGSLLYELLTGM-------ALSQSHPSG 485
Cdd:cd14146 149 nktLKITDFGlarEWH----RTTKMSAAGTYAwmAPEVIKSSLFSKGSDIWSYGVLLWELLTGEvpyrgidGLAVAYGVA 224

                       170       180       190
                ....*....|....*....|....*....|..
gi 81915001 486 FQAHTqLQLPEWLSHPAASLLTELLQFEPQRR 517
Cdd:cd14146 225 VNKLT-LPIPSTCPEPFAKLMKECWEQDPHIR 255
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
 379-517 4.18e-09

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: 57.42  E-value: 4.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLL-DQAGHIQLTYFGQWSEVEP------RCSQEAvdclYSAPEV- 450
Cdd:cd14074 100 LNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPgekletSCGSLA----YSAPEIl 175

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81915001 451 GGISELTEACDWWSYGSLLYELLTGMA-LSQSHPSGFQAHT---QLQLPEWLSHPAASLLTELLQFEPQRR 517
Cdd:cd14074 176 LGDEYDAPAVDIWSLGVILYMLVCGQPpFQEANDSETLTMImdcKYTVPAHVSPECKDLIRRMLIRDPKKR 246
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
 394-533 6.69e-09

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: 56.99  E-value: 6.69e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 394 ALEALHQQGVLCRDLNPQNLLLDQAG---------HIQLTYFGqWSEVEPRCSQEAVDC---LYSAPEVGGISELTEACD 461
Cdd:cd14120 104 AMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRLKIADFG-FARFLQDGMMAATLCgspMYMAPEVIMSLQYDAKAD 182

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 462 WWSYGSLLYELLTGMAlsqshPsgFQAHTQLQL--------------PEWLSHPAASLLTELLQFEPQRRLGAGGGGtsr 527
Cdd:cd14120 183 LWSIGTIVYQCLTGKA-----P--FQAQTPQELkafyeknanlrpniPSGTSPALKDLLLGLLKRNPKDRIDFEDFF--- 252


                ....*.
gi 81915001 528 lkSHPF 533
Cdd:cd14120 253 --SHPF 256
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
 395-520 6.87e-09

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: 57.33  E-value: 6.87e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 395 LEALHQQGVLCRDLNPQNLL-LDQAGH---IQLTYFGQWSEVEPRCSQEAVDCL---YSAPEVGGISELTEACDWWSYGS 467
Cdd:cd14178 110 VEYLHSQGVVHRDLKPSNILyMDESGNpesIRICDFGFAKQLRAENGLLMTPCYtanFVAPEVLKRQGYDAACDIWSLGI 189

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81915001 468 LLYELLTGMALSQSHP------------SGFQAhtqLQLPEW--LSHPAASLLTELLQFEPQRRLGA 520
Cdd:cd14178 190 LLYTMLAGFTPFANGPddtpeeilarigSGKYA---LSGGNWdsISDAAKDIVSKMLHVDPHQRLTA 253
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
 374-534 9.26e-09

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: 56.56  E-value: 9.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 374 RAAWSLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAG---------HIQLTYFGqWSEVEPRCSQEAVDC- 443
Cdd:cd14201  97 QAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIADFG-FARYLQSNMMAATLCg 175

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 444 --LYSAPEVGGISELTEACDWWSYGSLLYELLTGMALSQSHPSG-----FQAHTQLQ--LPEWLSHPAASLLTELLQFEP 514
Cdd:cd14201 176 spMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQdlrmfYEKNKNLQpsIPRETSPYLADLLLGLLQRNQ 255

                       170       180
                ....*....|....*....|
gi 81915001 515 QRRLGAGGggtsrLKSHPFF 534
Cdd:cd14201 256 KDRMDFEA-----FFSHPFL 270
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 381-520 1.01e-08

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: 56.14  E-value: 1.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQW----SEVEPRCSQEAVDcLYSAPEVGGISEL 456
Cdd:cd08219  99 EDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSArlltSPGAYACTYVGTP-YYVPPEIWENMPY 177

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81915001 457 TEACDWWSYGSLLYELLTgmalsQSHPsgFQA----HTQLQ--------LPEWLSHPAASLLTELLQFEPQRRLGA 520
Cdd:cd08219 178 NNKSDIWSLGCILYELCT-----LKHP--FQAnswkNLILKvcqgsykpLPSHYSYELRSLIKQMFKRNPRSRPSA 246
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
 340-534 1.11e-08

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: 56.77  E-value: 1.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 340 LHWVREGADRVLGAYGRGRGRNPPSANRASLgsgraawslregqVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQA- 418
Cdd:cd07837  80 LYLVFEYLDTDLKKFIDSYGRGPHNPLPAKT-------------IQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQk 146

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 419 GHIQLTYFG---QWSEVEPRCSQEAVDCLYSAPEVG-GISELTEACDWWSYGSLLYEL---------------------L 473
Cdd:cd07837 147 GLLKIADLGlgrAFTIPIKSYTHEIVTLWYRAPEVLlGSTHYSTPVDMWSVGCIFAEMsrkqplfpgdselqqllhifrL 226

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81915001 474 TGMALSQSHPSGFQAHTQLQLPEW-----------LSHPAASLLTELLQFEPQRRLGAggggTSRLKsHPFF 534
Cdd:cd07837 227 LGTPNEEVWPGVSKLRDWHEYPQWkpqdlsravpdLEPEGVDLLTKMLAYDPAKRISA----KAALQ-HPYF 293
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
 378-518 1.30e-08

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: 56.17  E-value: 1.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAG---------HIQLTYFGqWSEVEPRCSQEAVDC---LY 445
Cdd:cd14202  97 TLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFG-FARYLQNNMMAATLCgspMY 175

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 446 SAPEVGGISELTEACDWWSYGSLLYELLTGMALSQ-SHPSG----FQAHTQL--QLPEWLSHPAASLLTELLQFEPQRRL 518
Cdd:cd14202 176 MAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQaSSPQDlrlfYEKNKSLspNIPRETSSHLRQLLLGLLQRNQKDRM 255
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
 379-475 1.35e-08

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: 56.08  E-value: 1.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQA---GHIQLTYFGQWSEVEPRCSQEAV--DCLYSAPEVGGI 453
Cdd:cd14198 107 VSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIyplGDIKIVDFGMSRKIGHACELREImgTPEYLAPEILNY 186

                        90       100
                ....*....|....*....|..
gi 81915001 454 SELTEACDWWSYGSLLYELLTG 475
Cdd:cd14198 187 DPITTATDMWNIGVIAYMLLTH 208
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
 379-519 1.40e-08

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: 55.86  E-value: 1.40e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQwSEVEPRC---SQEAVDClYSAPEVGGISE 455
Cdd:cd08530 100 FPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGI-SKVLKKNlakTQIGTPL-YAAPEVWKGRP 177

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81915001 456 LTEACDWWSYGSLLYELLTGmalsqSHPsgFQAHTQLQL------------PEWLSHPAASLLTELLQFEPQRRLG 519
Cdd:cd08530 178 YDYKSDIWSLGCLLYEMATF-----RPP--FEARTMQELrykvcrgkfppiPPVYSQDLQQIIRSLLQVNPKKRPS 246
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
 382-534 1.47e-08

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: 55.73  E-value: 1.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 382 GQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEP-----RCSQEAVDCLYSAPEV--GGIS 454
Cdd:cd14119  97 WQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALDLfaeddTCTTSQGSPAFQPPEIanGQDS 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 455 ELTEACDWWSYGSLLYELLTG---------MALSQSHPSGfqahtQLQLPEWLSHPAASLLTELLQFEPQRRLgagggGT 525
Cdd:cd14119 177 FSGFKVDIWSAGVTLYNMTTGkypfegdniYKLFENIGKG-----EYTIPDDVDPDLQDLLRGMLEKDPEKRF-----TI 246


                ....*....
gi 81915001 526 SRLKSHPFF 534
Cdd:cd14119 247 EQIRQHPWF 255
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
 383-533 1.60e-08

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: 55.83  E-value: 1.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 383 QVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGH---IQLTYFGQWSEVEPRCSQEAVD----CLYSAPEVGGIS- 454
Cdd:cd14012 105 TARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGtgiVKLTDYSLGKTLLDMCSRGSLDefkqTYWLPPELAQGSk 184

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81915001 455 ELTEACDWWSYGSLLYELLTGMALSQSHPSGFQAHTQLQLPEwlshPAASLLTELLQFEPQRRLGAggggtSRLKSHPF 533
Cdd:cd14012 185 SPTRKTDVWDLGLLFLQMLFGLDVLEKYTSPNPVLVSLDLSA----SLQDFLSKCLSLDPKKRPTA-----LELLPHEF 254
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
 379-534 1.66e-08

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: 55.53  E-value: 1.66e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRCSQEAVDCLYSAPEVggISE 455
Cdd:cd06648 100 MNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGfcaQVSKEVPRRKSLVGTPYWMAPEV--ISR 177

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 456 L---TEAcDWWSYGSLLYELLTGMALSQSHPSgFQAHTQLQ--LPEWLSHPA------ASLLTELLQFEPQRRLGAgggg 524
Cdd:cd06648 178 LpygTEV-DIWSLGIMVIEMVDGEPPYFNEPP-LQAMKRIRdnEPPKLKNLHkvsprlRSFLDRMLVRDPAQRATA---- 251

                       170
                ....*....|
gi 81915001 525 tSRLKSHPFF 534
Cdd:cd06648 252 -AELLNHPFL 260
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
 384-520 1.68e-08

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: 56.15  E-value: 1.68e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 384 VKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG--QWSEVEPRC-SQEAVDCLYSAPEV-GGISELTEA 459
Cdd:cd07872 106 VKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGlaRAKSVPTKTySNEVVTLWYRPPDVlLGSSEYSTQ 185

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 460 CDWWSYGSLLYELLTGMAL--------------------SQSHPSGFQAHTQLQ---LPEWLSHP-----------AASL 505
Cdd:cd07872 186 IDMWGVGCIFFEMASGRPLfpgstvedelhlifrllgtpTEETWPGISSNDEFKnynFPKYKPQPlinhaprldteGIEL 265

                       170
                ....*....|....*
gi 81915001 506 LTELLQFEPQRRLGA 520
Cdd:cd07872 266 LTKFLQYESKKRISA 280
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
 379-532 1.94e-08

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: 55.83  E-value: 1.94e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRCSQEAVDCLYSAPEV---GG 452
Cdd:cd14118 112 LSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFGvsnEFEGDDALLSSTAGTPAFMAPEAlseSR 191

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 453 ISELTEACDWWSYGSLLYELLTG-MALSQSHPSGFQ---AHTQLQLPE--WLSHPAASLLTELLQFEPQRRLgagggGTS 526
Cdd:cd14118 192 KKFSGKALDIWAMGVTLYCFVFGrCPFEDDHILGLHekiKTDPVVFPDdpVVSEQLKDLILRMLDKNPSERI-----TLP 266


                ....*.
gi 81915001 527 RLKSHP 532
Cdd:cd14118 267 EIKEHP 272
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 390-533 2.08e-08

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: 55.77  E-value: 2.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLLL---DQAGHIQLTYFGqWSEVEPR------CSQEAvdclYSAPEVGGISELTEAC 460
Cdd:cd14166 108 QVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFG-LSKMEQNgimstaCGTPG----YVAPEVLAQKPYSKAV 182

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 461 DWWSYGSLLYELLTGMA--LSQSHPSGF----QAHTQLQLPEW--LSHPAASLLTELLQFEPQRRLgagggGTSRLKSHP 532
Cdd:cd14166 183 DCWSIGVITYILLCGYPpfYEETESRLFekikEGYYEFESPFWddISESAKDFIRHLLEKNPSKRY-----TCEKALSHP 257


                .
gi 81915001 533 F 533
Cdd:cd14166 258 W 258
MIT cd02656
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
 50-113 2.09e-08

MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain is found in sorting nexins, the nuclear thiol protease PalBH, the AAA protein spastin and archaebacterial proteins with similar domain architecture, vacuolar sorting proteins and others. The molecular function of the MIT domain is unclear.


Pssm-ID: 239121  Cd Length: 75  Bit Score: 51.16  E-value: 2.09e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81915001  50 LVDAATQ-IHLALERDVSEDYEAAFNHYQNGVDVLLRGVHVDPNKERREAVKLKITKYLRRAEEI 113
Cdd:cd02656   2 LLQQAKElIKQAVKEDEDGNYEEALELYKEALDYLLQALKAEKEPKLRKLLRKKVKEYLDRAEFL 66
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
 384-534 2.13e-08

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: 55.74  E-value: 2.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 384 VKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG--QWSEVEPRCSQEAVDCLYSAPEVGGISELTEACD 461
Cdd:cd07863 110 IKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGlaRIYSCQMALTPVVVTLWYRAPEVLLQSTYATPVD 189

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 462 WWSYGSLLYEL---------------------LTGMALSQSHP-------SGFQAHTQLQL----PEwLSHPAASLLTEL 509
Cdd:cd07863 190 MWSVGCIFAEMfrrkplfcgnseadqlgkifdLIGLPPEDDWPrdvtlprGAFSPRGPRPVqsvvPE-IEESGAQLLLEM 268

                       170       180
                ....*....|....*....|....*
gi 81915001 510 LQFEPQRRLGAggggtSRLKSHPFF 534
Cdd:cd07863 269 LTFNPHKRISA-----FRALQHPFF 288
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
 379-518 2.25e-08

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: 55.37  E-value: 2.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTY--FGQWSEVEPRCSQEAV--DCLYSAPEVGGIS 454
Cdd:cd14121  92 LPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPVLKLadFGFAQHLKPNDEAHSLrgSPLYMAPEMILKK 171

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81915001 455 ELTEACDWWSYGSLLYELLTGMALSQShpSGF-------QAHTQLQLPEW--LSHPAASLLTELLQFEPQRRL 518
Cdd:cd14121 172 KYDARVDLWSVGVILYECLFGRAPFAS--RSFeeleekiRSSKPIEIPTRpeLSADCRDLLLRLLQRDPDRRI 242
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
 384-478 2.36e-08

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: 56.29  E-value: 2.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 384 VKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGH--IQLTYFGQWSEVEPRCSQEAVDCLYSAPEVGGISELTEACD 461
Cdd:cd14224 170 VRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEHQRIYTYIQSRFYRAPEVILGARYGMPID 249

                        90
                ....*....|....*..
gi 81915001 462 WWSYGSLLYELLTGMAL 478
Cdd:cd14224 250 MWSFGCILAELLTGYPL 266
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
 378-520 2.71e-08

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: 55.33  E-value: 2.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQA---GHIQLTYFGQWSEVepRCSQEAVDCL----YSAPEV 450
Cdd:cd14197 107 AFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGLSRIL--KNSEELREIMgtpeYVAPEI 184

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81915001 451 GGISELTEACDWWSYGSLLYELLTGMA--LSQSHPSGFQAHTQLQLP------EWLSHPAASLLTELLQFEPQRRLGA 520
Cdd:cd14197 185 LSYEPISTATDMWSIGVLAYVMLTGISpfLGDDKQETFLNISQMNVSyseeefEHLSESAIDFIKTLLIKKPENRATA 262
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
 378-534 2.76e-08

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: 55.12  E-value: 2.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQ------VKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG--QWSEVEPRC-SQEAVDCLYSAP 448
Cdd:cd07861  91 SLPKGKymdaelVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGlaRAFGIPVRVyTHEVVTLWYRAP 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 449 EV-GGISELTEACDWWSYGSLLYELLTGMALSQSHPSGFQAH-----------------TQLQ-----LPEW-------- 497
Cdd:cd07861 171 EVlLGSPRYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFrifrilgtptediwpgvTSLPdykntFPKWkkgslrta 250

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 81915001 498 ---LSHPAASLLTELLQFEPQRRLGAggggtSRLKSHPFF 534
Cdd:cd07861 251 vknLDEDGLDLLEKMLIYDPAKRISA-----KKALVHPYF 285
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
 384-520 3.42e-08

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: 55.52  E-value: 3.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 384 VKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCS----QEAVDCLYSAPEV-GGISELTE 458
Cdd:cd07853 105 VKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEEPDESkhmtQEVVTQYYRAPEIlMGSRHYTS 184

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 459 ACDWWSYGSLLYELLTGMALSQSH---------------PS---------GFQAHTqLQLPEW-------------LSHP 501
Cdd:cd07853 185 AVDIWSVGCIFAELLGRRILFQAQspiqqldlitdllgtPSleamrsaceGARAHI-LRGPHKppslpvlytlssqATHE 263

                       170
                ....*....|....*....
gi 81915001 502 AASLLTELLQFEPQRRLGA 520
Cdd:cd07853 264 AVHLLCRMLVFDPDKRISA 282
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
 379-493 3.87e-08

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: 54.97  E-value: 3.87e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGH------IQLTYFGQWSEVEpRCSQEAVDCLYSAPEVGG 452
Cdd:cd14038  98 LREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQrlihkiIDLGYAKELDQGS-LCTSFVGTLQYLAPELLE 176

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 81915001 453 ISELTEACDWWSYGSLLYELLTGMA--LSQSHPsgFQAHTQLQ 493
Cdd:cd14038 177 QQKYTVTVDYWSFGTLAFECITGFRpfLPNWQP--VQWHGKVR 217
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
 379-537 5.05e-08

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: 54.70  E-value: 5.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRCSQEAVDCLYSAPEV-GGIS 454
Cdd:cd07869 100 LHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGlarAKSVPSHTYSNEVVTLWYRPPDVlLGST 179

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 455 ELTEACDWWSYGSLLYELLTGMA--------------------------------LSQSHPSGFQAHTQLQLPE------ 496
Cdd:cd07869 180 EYSTCLDMWGVGCIFVEMIQGVAafpgmkdiqdqleriflvlgtpnedtwpgvhsLPHFKPERFTLYSPKNLRQawnkls 259

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 81915001 497 WLSHpAASLLTELLQFEPQRRLGAGGGgtsrlKSHPFFSTI 537
Cdd:cd07869 260 YVNH-AEDLASKLLQCFPKNRLSAQAA-----LSHEYFSDL 294
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
 379-517 5.29e-08

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: 54.19  E-value: 5.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG------QWSEVEPRCSQEavdcLYSAPE-VG 451
Cdd:cd14161  99 LSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGlsnlynQDKFLQTYCGSP----LYASPEiVN 174

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81915001 452 GISELTEACDWWSYGSLLYELLTGmalsqSHPsgFQAHTQLQLPEWLS--------HP--AASLLTELLQFEPQRR 517
Cdd:cd14161 175 GRPYIGPEVDSWSLGVLLYILVHG-----TMP--FDGHDYKILVKQISsgayreptKPsdACGLIRWLLMVNPERR 243
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
 390-475 5.36e-08

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: 54.58  E-value: 5.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRC---SQEAVDCLYSAPEV-GGISELTEACDWWSY 465
Cdd:cd07870 106 QLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSqtySSEVVTLWYRPPDVlLGATDYSSALDIWGA 185

                        90
                ....*....|
gi 81915001 466 GSLLYELLTG 475
Cdd:cd07870 186 GCIFIEMLQG 195
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 381-474 5.39e-08

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: 54.05  E-value: 5.39e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGqWSEVEPRCSQEAVDCL----YSAPEVGGISEL 456
Cdd:cd08218 100 EDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFG-IARVLNSTVELARTCIgtpyYLSPEICENKPY 178

                        90
                ....*....|....*...
gi 81915001 457 TEACDWWSYGSLLYELLT 474
Cdd:cd08218 179 NNKSDIWALGCVLYEMCT 196
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
 393-517 5.58e-08

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: 53.93  E-value: 5.58e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 393 LALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCL-YSAPEV-GGISELTEACDWWSYGSLLY 470
Cdd:cd14004 120 DAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSAAYIKSGPFDTFVGTIdYAAPEVlRGNPYGGKEQDIWALGVLLY 199

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 81915001 471 ELLTGMALSQSHPSGFQAhtQLQLPEWLSHPAASLLTELLQFEPQRR 517
Cdd:cd14004 200 TLVFKENPFYNIEEILEA--DLRIPYAVSEDLIDLISRMLNRDVGDR 244
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
 394-535 6.64e-08

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: 54.27  E-value: 6.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 394 ALEALHQQGVLCRDLNPQNLLLDQA---GHIQLTYFGQWSEVEPRCSQeAVDCL---YSAPEVGGISELTEACDWWSYGS 467
Cdd:cd14170 113 AIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGFAKETTSHNSL-TTPCYtpyYVAPEVLGPEKYDKSCDMWSLGV 191

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 468 LLYELLT---------GMALSQSHPSGFQ-AHTQLQLPEW--LSHPAASLLTELLQFEPQRRLgagggGTSRLKSHPFFS 535
Cdd:cd14170 192 IMYILLCgyppfysnhGLAISPGMKTRIRmGQYEFPNPEWseVSEEVKMLIRNLLKTEPTQRM-----TITEFMNHPWIM 266
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
 381-535 7.12e-08

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: 54.18  E-value: 7.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRCSQEAVDCLYSAPEV---GGIS 454
Cdd:cd14200 123 EDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIADFGvsnQFEGNDALLSSTAGTPAFMAPETlsdSGQS 202

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 455 ELTEACDWWSYGSLLYELLTG---------MALS---QSHPSGFQAHTQlqlpewLSHPAASLLTELLQFEPQRRLgagg 522
Cdd:cd14200 203 FSGKALDVWAMGVTLYCFVYGkcpfidefiLALHnkiKNKPVEFPEEPE------ISEELKDLILKMLDKNPETRI---- 272

                       170
                ....*....|...
gi 81915001 523 gGTSRLKSHPFFS 535
Cdd:cd14200 273 -TVPEIKVHPWVT 284
MIT_VPS4 cd02678
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 60-113 8.01e-08

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in intracellular protein transport proteins of the AAA-ATPase family. The molecular function of the MIT domain is unclear.


Pssm-ID: 239141  Cd Length: 75  Bit Score: 49.57  E-value: 8.01e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 81915001  60 ALERDVSEDYEAAFNHYQNGVDVLLRGVHVDPNKERREAVKLKITKYLRRAEEI 113
Cdd:cd02678  13 AIEEDNAGNYEEALRLYQHALEYFMHALKYEKNPKSKESIRAKCTEYLDRAEKL 66
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
 379-475 8.03e-08

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: 53.45  E-value: 8.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG------QWSEVEPRCSQEAvdC---LYSAPE 449
Cdd:cd14162  97 LPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGfargvmKTKDGKPKLSETY--CgsyAYASPE 174

                        90       100
                ....*....|....*....|....*..
gi 81915001 450 V-GGISELTEACDWWSYGSLLYELLTG 475
Cdd:cd14162 175 IlRGIPYDPFLSDIWSMGVVLYTMVYG 201
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
 394-517 8.12e-08

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: 53.68  E-value: 8.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 394 ALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVdC---LYSAPEV-GGISELTEACDWWSYGSLL 469
Cdd:cd14072 111 AVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPGNKLDTF-CgspPYAAPELfQGKKYDGPEVDVWSLGVIL 189

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 81915001 470 YELLTGmalsqSHPSGFQAHTQL---------QLPEWLSHPAASLLTELLQFEPQRR 517
Cdd:cd14072 190 YTLVSG-----SLPFDGQNLKELrervlrgkyRIPFYMSTDCENLLKKFLVLNPSKR 241
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
 379-517 8.56e-08

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: 53.48  E-value: 8.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAG--HIQLTYFGQwseveprcsQEAVDCL---------YSA 447
Cdd:cd13987  88 LPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDcrRVKLCDFGL---------TRRVGSTvkrvsgtipYTA 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 448 PEVGGISE-----LTEACDWWSYGSLLYELLTGM---ALSQSHPSGFQAHTQLQ------LP-EW--LSHPAASLLTELL 510
Cdd:cd13987 159 PEVCEAKKnegfvVDPSIDVWAFGVLLFCCLTGNfpwEKADSDDQFYEEFVRWQkrkntaVPsQWrrFTPKALRMFKKLL 238


                ....*..
gi 81915001 511 QFEPQRR 517
Cdd:cd13987 239 APEPERR 245
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
 390-483 1.07e-07

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: 53.40  E-value: 1.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCS--QEAVDCLY-SAPEVGGISELTEACDWWSYG 466
Cdd:cd06609 106 EVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTMSkrNTFVGTPFwMAPEVIKQSGYDEKADIWSLG 185

                        90
                ....*....|....*...
gi 81915001 467 SLLYELLTGMA-LSQSHP 483
Cdd:cd06609 186 ITAIELAKGEPpLSDLHP 203
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
 379-478 1.16e-07

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 53.61  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001  379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG------------QWSEVEPRCSQE-----AV 441
Cdd:PTZ00024 116 LTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGlarrygyppysdTLSKDETMQRREemtskVV 195

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 81915001  442 DCLYSAPE-VGGISELTEACDWWSYGSLLYELLTGMAL 478
Cdd:PTZ00024 196 TLWYRAPElLMGAEKYHFAVDMWSVGCIFAELLTGKPL 233
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
 379-518 1.30e-07

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: 53.26  E-value: 1.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRCSQEAVD--ClYSAPEVGGI 453
Cdd:cd14076 103 LKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGfanTFDHFNGDLMSTSCGspC-YAAPELVVS 181

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81915001 454 SELTEA--CDWWSYGSLLYELLTG-MALSQSH--PSG--------FQAHTQLQLPEWLSHPAASLLTELLQFEPQRRL 518
Cdd:cd14076 182 DSMYAGrkADIWSCGVILYAMLAGyLPFDDDPhnPNGdnvprlyrYICNTPLIFPEYVTPKARDLLRRILVPNPRKRI 259
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 390-474 1.41e-07

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: 52.89  E-value: 1.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQ-GVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRCSQEAVDCLYSAPEVGGISELTEACDWWSY 465
Cdd:cd08528 121 QMVLALRYLHKEkQIVHRDLKPNNIMLGEDDKVTITDFGlakQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWAL 200


                ....*....
gi 81915001 466 GSLLYELLT 474
Cdd:cd08528 201 GCILYQMCT 209
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
 379-517 1.56e-07

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: 52.71  E-value: 1.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDC---LYSAPEVggISE 455
Cdd:cd14188  98 LTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRTICgtpNYLSPEV--LNK 175

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 456 LTEAC--DWWSYGSLLYELLTG------MALSQSHPSGFQAhtQLQLPEWLSHPAASLLTELLQFEPQRR 517
Cdd:cd14188 176 QGHGCesDIWALGCVMYTMLLGrppfetTNLKETYRCIREA--RYSLPSSLLAPAKHLIASMLSKNPEDR 243
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
 392-535 1.59e-07

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: 53.33  E-value: 1.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 392 LLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCL--------YSAPEV-GGISELTEACDW 462
Cdd:cd07852 117 LKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARSLSQLEEDDENPVLtdyvatrwYRAPEIlLGSTRYTKGVDM 196

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 463 WSYGSLLYELLTGMAL----S--------------------QSHPSGFqAHTQLQ---------LPEWL---SHPAASLL 506
Cdd:cd07852 197 WSVGCILGEMLLGKPLfpgtStlnqlekiievigrpsaediESIQSPF-AATMLEslppsrpksLDELFpkaSPDALDLL 275

                       170       180
                ....*....|....*....|....*....
gi 81915001 507 TELLQFEPQRRLGAggggTSRLKsHPFFS 535
Cdd:cd07852 276 KKLLVFNPNKRLTA----EEALR-HPYVA 299
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
 384-534 1.81e-07

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: 52.70  E-value: 1.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 384 VKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSE-VEPRCSQEAVDCLYSAPEV-GGISELTE 458
Cdd:cd07833 102 VRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGfarALTArPASPLTDYVATRWYRAPELlVGDTNYGK 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 459 ACDWWSYGSLLYELLTGMAL--------------------SQSHPSGFQAHT----------------QLQLPEWLSHPA 502
Cdd:cd07833 182 PVDVWAIGCIMAELLDGEPLfpgdsdidqlyliqkclgplPPSHQELFSSNPrfagvafpepsqpeslERRYPGKVSSPA 261

                       170       180       190
                ....*....|....*....|....*....|..
gi 81915001 503 ASLLTELLQFEPQRRLGAggggtSRLKSHPFF 534
Cdd:cd07833 262 LDFLKACLRMDPKERLTC-----DELLQHPYF 288
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
 384-518 2.06e-07

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 53.50  E-value: 2.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001  384 VKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGH-IQLTYFGQ-------WSEVEPRCSQeavdcLYSAPEVG-GIS 454
Cdd:PTZ00036 172 VKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHtLKLCDFGSaknllagQRSVSYICSR-----FYRAPELMlGAT 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001  455 ELTEACDWWSYGSLLYELLTGMALSQSHPS-----------GFQAHTQLQ----------------------LPEWLSHP 501
Cdd:PTZ00036 247 NYTTHIDLWSLGCIIAEMILGYPIFSGQSSvdqlvriiqvlGTPTEDQLKemnpnyadikfpdvkpkdlkkvFPKGTPDD 326

                        170
                 ....*....|....*..
gi 81915001  502 AASLLTELLQFEPQRRL 518
Cdd:PTZ00036 327 AINFISQFLKYEPLKRL 343
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
 387-475 2.15e-07

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: 52.11  E-value: 2.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 387 WAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRCSQeAVDCLYSAPEVGGISELTEACDWW 463
Cdd:cd14059  86 WSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGtskELSEKSTKMSF-AGTVAWMAPEVIRNEPCSEKVDIW 164

                        90
                ....*....|..
gi 81915001 464 SYGSLLYELLTG 475
Cdd:cd14059 165 SFGVVLWELLTG 176
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
 381-533 2.45e-07

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: 52.17  E-value: 2.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDC---LYSAPEVGGISELT 457
Cdd:cd14186 101 EDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHEKHFTMCgtpNYISPEIATRSAHG 180

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 458 EACDWWSYGSLLYELLTGmalsqsHPSgFQAHT-----------QLQLPEWLSHPAASLLTELLQFEPQRRLgagggGTS 526
Cdd:cd14186 181 LESDVWSLGCMFYTLLVG------RPP-FDTDTvkntlnkvvlaDYEMPAFLSREAQDLIHQLLRKNPADRL-----SLS 248


                ....*..
gi 81915001 527 RLKSHPF 533
Cdd:cd14186 249 SVLDHPF 255
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
 381-519 2.71e-07

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: 52.01  E-value: 2.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWaaEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG------------QWSEVEPrcsqeavdclYSAP 448
Cdd:cd14071 100 EARKKFW--QILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGfsnffkpgellkTWCGSPP----------YAAP 167

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 449 EV-GGISELTEACDWWSYGSLLYELLTGM---------ALSQSHPSGfqahtQLQLPEWLSHPAASLLTELLQFEPQRRL 518
Cdd:cd14071 168 EVfEGKEYEGPQLDIWSLGVVLYVLVCGAlpfdgstlqTLRDRVLSG-----RFRIPFFMSTDCEHLIRRMLVLDPSKRL 242


                .
gi 81915001 519 G 519
Cdd:cd14071 243 T 243
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
 388-518 2.82e-07

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: 51.91  E-value: 2.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 388 AAEML----LALEALHQQGVLCRDLNPQNLLLDQAGH---IQLTYFGQWSEVEPRCSQEAVDC--LYSAPEVGGISELTE 458
Cdd:cd14089 102 AAEIMrqigSAVAHLHSMNIAHRDLKPENLLYSSKGPnaiLKLTDFGFAKETTTKKSLQTPCYtpYYVAPEVLGPEKYDK 181

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81915001 459 ACDWWSYGSLLYELL---------TGMALSQSHPSGF-QAHTQLQLPEW--LSHPAASLLTELLQFEPQRRL 518
Cdd:cd14089 182 SCDMWSLGVIMYILLcgyppfysnHGLAISPGMKKRIrNGQYEFPNPEWsnVSEEAKDLIRGLLKTDPSERL 253
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
 378-533 2.94e-07

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: 52.02  E-value: 2.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAV--DCLYSAPEV--GGI 453
Cdd:cd06632  98 AFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFSFAKSFkgSPYWMAPEVimQKN 177

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 454 SELTEACDWWSYGSLLYELLTGmALSQSHPSGFQAHTQL-------QLPEWLSHPAASLLTELLQFEPQRRLGAggggtS 526
Cdd:cd06632 178 SGYGLAVDIWSLGCTVLEMATG-KPPWSQYEGVAAIFKIgnsgelpPIPDHLSPDAKDFIRLCLQRDPEDRPTA-----S 251


                ....*..
gi 81915001 527 RLKSHPF 533
Cdd:cd06632 252 QLLEHPF 258
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
 391-537 3.15e-07

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: 52.53  E-value: 3.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 391 MLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPrcsQEAVDCL--------YSAPEV-GGISELTEACD 461
Cdd:cd07834 112 ILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLARGVDP---DEDKGFLteyvvtrwYRAPELlLSSKKYTKAID 188

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 462 WWSYGSLLYELLTGMALsqshpsgFQAHT---QLQL---------------------PEWLSH-------------PAAS 504
Cdd:cd07834 189 IWSVGCIFAELLTRKPL-------FPGRDyidQLNLivevlgtpseedlkfissekaRNYLKSlpkkpkkplsevfPGAS 261

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 81915001 505 -----LLTELLQFEPQRRLGAggggtSRLKSHPFFSTI 537
Cdd:cd07834 262 peaidLLEKMLVFNPKKRITA-----DEALAHPYLAQL 294
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
 366-527 3.21e-07

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: 52.07  E-value: 3.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 366 NRASLGSGraawsLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGH------IQLTYFGQWSEVEpRCSQE 439
Cdd:cd13989  91 NQPENCCG-----LKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGrviyklIDLGYAKELDQGS-LCTSF 164

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 440 AVDCLYSAPEVGGISELTEACDWWSYGSLLYELLTG------------------------MALSQSHPSGFQAHTQLQLP 495
Cdd:cd13989 165 VGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGyrpflpnwqpvqwhgkvkqkkpehICAYEDLTGEVKFSSELPSP 244

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 81915001 496 EWLSHPAA----SLLTELLQFEPQRRlGAGGGGTSR 527
Cdd:cd13989 245 NHLSSILKeyleSWLQLMLRWDPRQR-GGGPQNNPG 279
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
 387-517 3.40e-07

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: 51.95  E-value: 3.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 387 WAAEMLLALEALHQQG---VLCRDLNPQNLLLDQAGH--------IQLTYFG---QWSevepRCSQEAVDCLYS--APEV 450
Cdd:cd14147 106 WAVQIARGMHYLHCEAlvpVIHRDLKSNNILLLQPIEnddmehktLKITDFGlarEWH----KTTQMSAAGTYAwmAPEV 181

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81915001 451 GGISELTEACDWWSYGSLLYELLTGMA-------LSQSHPSGFQAHTqLQLPEWLSHPAASLLTELLQFEPQRR 517
Cdd:cd14147 182 IKASTFSKGSDVWSFGVLLWELLTGEVpyrgidcLAVAYGVAVNKLT-LPIPSTCPEPFAQLMADCWAQDPHRR 254
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 381-518 3.42e-07

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: 52.18  E-value: 3.42e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGH---IQLTYFGqWSEVEPRCSQE-AVDCL---YSAPEVGGI 453
Cdd:cd14180 100 ESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFG-FARLRPQGSRPlQTPCFtlqYAAPELFSN 178

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 454 SELTEACDWWSYGSLLYELLTGMALSQSHPS-GFQAHT------------QLQLPEW--LSHPAASLLTELLQFEPQRRL 518
Cdd:cd14180 179 QGYDESCDLWSLGVILYTMLSGQVPFQSKRGkMFHNHAadimhkikegdfSLEGEAWkgVSEEAKDLVRGLLTVDPAKRL 258
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
 374-475 3.86e-07

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: 51.54  E-value: 3.86e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 374 RAAWSLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG-------QWSEVEPR----CSQEAvd 442
Cdd:cd13994  90 EKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGtaevfgmPAEKESPMsaglCGSEP-- 167

                        90       100       110
                ....*....|....*....|....*....|....
gi 81915001 443 clYSAPEV-GGISELTEACDWWSYGSLLYELLTG 475
Cdd:cd13994 168 --YMAPEVfTSGSYDGRAVDVWSCGIVLFALFTG 199
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
 384-472 4.12e-07

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: 51.66  E-value: 4.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 384 VKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSE--VEPRC-SQEAVDCLYSAPEV-GGISELTEA 459
Cdd:cd07839 101 VKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAfgIPVRCySAEVVTLWYRPPDVlFGAKLYSTS 180

                        90
                ....*....|...
gi 81915001 460 CDWWSYGSLLYEL 472
Cdd:cd07839 181 IDMWSAGCIFAEL 193
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
 390-520 4.18e-07

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: 51.71  E-value: 4.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEA--VDCLY-SAPEV--GGISELTEAcDWWS 464
Cdd:cd06917 109 EVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSKRStfVGTPYwMAPEVitEGKYYDTKA-DIWS 187

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81915001 465 YGSLLYELLTGmalsqSHP-SGFQAHTQLQL------PEWLSHPAASLLTEL----LQFEPQRRLGA 520
Cdd:cd06917 188 LGITTYEMATG-----NPPySDVDALRAVMLipkskpPRLEGNGYSPLLKEFvaacLDEEPKDRLSA 249
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
 378-517 4.33e-07

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: 51.47  E-value: 4.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDC---LYSAPEVGGIS 454
Cdd:cd14187 103 ALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGERKKTLCgtpNYIAPEVLSKK 182

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81915001 455 ELTEACDWWSYGSLLYELLTGM------ALSQSHPSgfQAHTQLQLPEWLSHPAASLLTELLQFEPQRR 517
Cdd:cd14187 183 GHSFEVDIWSIGCIMYTLLVGKppfetsCLKETYLR--IKKNEYSIPKHINPVAASLIQKMLQTDPTAR 249
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
 379-534 4.64e-07

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: 51.60  E-value: 4.64e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSqEAVDCL----YSAPE-VGGI 453
Cdd:cd07847  97 VPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPGD-DYTDYVatrwYRAPElLVGD 175

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 454 SELTEACDWWSYGSLLYELLTGMAL--SQS------------------HPSGFQAH---TQLQLPE------------WL 498
Cdd:cd07847 176 TQYGPPVDVWAIGCVFAELLTGQPLwpGKSdvdqlylirktlgdliprHQQIFSTNqffKGLSIPEpetrepleskfpNI 255

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 81915001 499 SHPAASLLTELLQFEPQRRLGAggggtSRLKSHPFF 534
Cdd:cd07847 256 SSPALSFLKGCLQMDPTERLSC-----EELLEHPYF 286
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
 380-518 4.78e-07

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: 51.36  E-value: 4.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 380 REGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLdQAGHIQLTYFGQWSEVEpRCSQEAVDC---LYSAPEVGGISEL 456
Cdd:cd14109  97 TERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILL-QDDKLKLADFGQSRRLL-RGKLTTLIYgspEFVSPEIVNSYPV 174

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 457 TEACDWWSYGSLLYELLTGMAL------SQSHPSGFQAHTQLQLPEW--LSHPAASLLTELLQFEPQRRL 518
Cdd:cd14109 175 TLATDMWSVGVLTYVLLGGISPflgdndRETLTNVRSGKWSFDSSPLgnISDDARDFIKKLLVYIPESRL 244
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
 395-520 5.09e-07

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: 51.55  E-value: 5.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 395 LEALHQQGVLCRDLNPQNLL-LDQAGH---IQLTYFGQWSEVEPRCSQEAVDCL---YSAPEVGGISELTEACDWWSYGS 467
Cdd:cd14177 111 VDYLHCQGVVHRDLKPSNILyMDDSANadsIRICDFGFAKQLRGENGLLLTPCYtanFVAPEVLMRQGYDAACDIWSLGV 190

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81915001 468 LLYELLTGMALSQSHPSGFQAHTQLQLPE---------W--LSHPAASLLTELLQFEPQRRLGA 520
Cdd:cd14177 191 LLYTMLAGYTPFANGPNDTPEEILLRIGSgkfslsggnWdtVSDAAKDLLSHMLHVDPHQRYTA 254
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
 377-477 5.25e-07

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: 51.13  E-value: 5.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 377 W-SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGH---IQLTYFGQWSEVE--PRCSQEAVDCLYSAPEV 450
Cdd:cd14113  97 WgNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFGDAVQLNttYYIHQLLGSPEFAAPEI 176

                        90       100
                ....*....|....*....|....*....
gi 81915001 451 --GGISELTEacDWWSYGSLLYELLTGMA 477
Cdd:cd14113 177 ilGNPVSLTS--DLWSIGVLTYVLLSGVS 203
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
 383-521 5.58e-07

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: 51.01  E-value: 5.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 383 QVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAG-HIQLTYFGQWSEVEPR-------CSQEAvdclYSAPEV-GGI 453
Cdd:cd14164 101 LARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVEDYpelsttfCGSRA----YTPPEViLGT 176

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81915001 454 SELTEACDWWSYGSLLYELLTGMALSQSHPSGFQAHTQ--LQLPE--WLSHPAASLLTELLQFEPQRRLGAG 521
Cdd:cd14164 177 PYDPKKYDVWSLGVVLYVMVTGTMPFDETNVRRLRLQQrgVLYPSgvALEEPCRALIRTLLQFNPSTRPSIQ 248
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 390-517 5.58e-07

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: 51.59  E-value: 5.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLLL---DQAGHIQLTYFGqWSEVEPRCSQEAVDC---LYSAPEVGGISELTEACDWW 463
Cdd:cd14168 116 QVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFG-LSKMEGKGDVMSTACgtpGYVAPEVLAQKPYSKAVDCW 194

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81915001 464 SYGSLLYELLTGMAL------SQSHPSGFQAHTQLQLPEW--LSHPAASLLTELLQFEPQRR 517
Cdd:cd14168 195 SIGVIAYILLCGYPPfydendSKLFEQILKADYEFDSPYWddISDSAKDFIRNLMEKDPNKR 256
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
 378-517 5.67e-07

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: 50.77  E-value: 5.67e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEV--EPRCSQEAVDCLYSAPEV-GGIs 454
Cdd:cd14050  96 SLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELdkEDIHDAQEGDPRYMAPELlQGS- 174

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 455 eLTEACDWWSYGSLLYELLTGMALsqshPSGFQAHTQL---QLPE----WLSHPAASLLTELLQFEPQRR 517
Cdd:cd14050 175 -FTKAADIFSLGITILELACNLEL----PSGGDGWHQLrqgYLPEeftaGLSPELRSIIKLMMDPDPERR 239
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 381-517 7.29e-07

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: 50.73  E-value: 7.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHI-QLTYFGQwSEVEPRCSQEAVDCL----YSAPEVGGISE 455
Cdd:cd08225 100 EDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGI-ARQLNDSMELAYTCVgtpyYLSPEICQNRP 178

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81915001 456 LTEACDWWSYGSLLYELLT------GMALSQSHPSGFQAHTQLQLPEWlSHPAASLLTELLQFEPQRR 517
Cdd:cd08225 179 YNNKTDIWSLGCVLYELCTlkhpfeGNNLHQLVLKICQGYFAPISPNF-SRDLRSLISQLFKVSPRDR 245
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
 379-534 7.41e-07

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: 51.16  E-value: 7.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG----------QWSEVEPRCSQEAVDCL---- 444
Cdd:cd07866 112 LTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGlarpydgpppNPKGGGGGGTRKYTNLVvtrw 191

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 445 YSAPE-VGGISELTEACDWWSYGSLLYELLTGMALSQSHPSGFQAH---------TQLQLPEWLSHPA------------ 502
Cdd:cd07866 192 YRPPElLLGERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLHlifklcgtpTEETWPGWRSLPGcegvhsftnypr 271

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 81915001 503 -------------ASLLTELLQFEPQRRLGAGGGgtsrlKSHPFF 534
Cdd:cd07866 272 tleerfgklgpegLDLLSKLLSLDPYKRLTASDA-----LEHPYF 311
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
 375-520 9.77e-07

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: 50.55  E-value: 9.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 375 AAW-SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAG--HIQLTYFG------QWSEVEPRCSQEAvdclY 445
Cdd:cd14098  93 MAWgAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGlakvihTGTFLVTFCGTMA----Y 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 446 SAPEV---------GGISELTeacDWWSYGSLLYELLTGmAL---SQSHPSGFQAHTQLQLPEW------LSHPAASLLT 507
Cdd:cd14098 169 LAPEIlmskeqnlqGGYSNLV---DMWSVGCLVYVMLTG-ALpfdGSSQLPVEKRIRKGRYTQPplvdfnISEEAIDFIL 244

                       170
                ....*....|...
gi 81915001 508 ELLQFEPQRRLGA 520
Cdd:cd14098 245 RLLDVDPEKRMTA 257
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
 384-473 1.06e-06

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: 50.42  E-value: 1.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 384 VKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG--QWSEVEPRCSQEAVDCLYSAPEVGGISELTEACD 461
Cdd:cd07862 112 IKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGlaRIYSFQMALTSVVVTLWYRAPEVLLQSSYATPVD 191

                        90
                ....*....|..
gi 81915001 462 WWSYGSLLYELL 473
Cdd:cd07862 192 LWSVGCIFAEMF 203
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
 387-517 1.13e-06

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: 50.08  E-value: 1.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 387 WAAEMLLALEALHQQG---VLCRDLNPQNLLLDQA---GHIQ-----LTYFGQWSEVE--PRCSQeAVDCLYSAPEVGGI 453
Cdd:cd14061  97 WAIQIARGMNYLHNEApvpIIHRDLKSSNILILEAienEDLEnktlkITDFGLAREWHktTRMSA-AGTYAWMAPEVIKS 175

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81915001 454 SELTEACDWWSYGSLLYELLTGM-------ALSQSHPSGFQAHTqLQLPEWLSHPAASLLTELLQFEPQRR 517
Cdd:cd14061 176 STFSKASDVWSYGVLLWELLTGEvpykgidGLAVAYGVAVNKLT-LPIPSTCPEPFAQLMKDCWQPDPHDR 245
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
 381-499 1.16e-06

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: 50.57  E-value: 1.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQ---WSEVEPRCSQEAVDCL-YSAPE-VGGISE 455
Cdd:cd07864 115 EDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLarlYNSEESRPYTNKVITLwYRPPElLLGEER 194

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 81915001 456 LTEACDWWSYGSLLYELLTGMALsqshpsgFQAHTQLQLPEWLS 499
Cdd:cd07864 195 YGPAIDVWSCGCILGELFTKKPI-------FQANQELAQLELIS 231
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
 381-475 1.35e-06

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: 49.90  E-value: 1.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQ-GVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPR--CSQEAV-DCLYSAPEVGGISEL 456
Cdd:cd06623  98 EPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGEVKIADFGISKVLENTldQCNTFVgTVTYMSPERIQGESY 177

                        90
                ....*....|....*....
gi 81915001 457 TEACDWWSYGSLLYELLTG 475
Cdd:cd06623 178 SYAADIWSLGLTLLECALG 196
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
 378-477 1.41e-06

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: 49.90  E-value: 1.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAG--HIQLTYFGQWSEVEPrcsQEAVDCLYS-----APEV 450
Cdd:cd14108  93 TVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKtdQVRICDFGNAQELTP---NEPQYCKYGtpefvAPEI 169

                        90       100
                ....*....|....*....|....*..
gi 81915001 451 GGISELTEACDWWSYGSLLYELLTGMA 477
Cdd:cd14108 170 VNQSPVSKVTDIWPVGVIAYLCLTGIS 196
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
 387-517 1.43e-06

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: 49.99  E-value: 1.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 387 WAAEMLLALEALHQQG---VLCRDLNPQNLLLDQAGH--------IQLTYFGQWSEVEPRCSQEAVDCL-YSAPEVGGIS 454
Cdd:cd14148  97 WAVQIARGMNYLHNEAivpIIHRDLKSSNILILEPIEnddlsgktLKITDFGLAREWHKTTKMSAAGTYaWMAPEVIRLS 176

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 455 ELTEACDWWSYGSLLYELLTGM-------ALSQSHPSGFQAHTqLQLPEWLSHPAASLLTELLQFEPQRR 517
Cdd:cd14148 177 LFSKSSDVWSFGVLLWELLTGEvpyreidALAVAYGVAMNKLT-LPIPSTCPEPFARLLEECWDPDPHGR 245
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
 379-533 1.45e-06

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: 49.96  E-value: 1.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVeprcsqEAVDCLYS---------APE 449
Cdd:cd14199 123 LSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGEDGHIKIADFGVSNEF------EGSDALLTntvgtpafmAPE 196

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 450 VggISELT-----EACDWWSYGSLLYELLTG---------MALSQshpsgfQAHTQ-LQLPEW--LSHPAASLLTELLQF 512
Cdd:cd14199 197 T--LSETRkifsgKALDVWAMGVTLYCFVFGqcpfmderiLSLHS------KIKTQpLEFPDQpdISDDLKDLLFRMLDK 268

                       170       180
                ....*....|....*....|.
gi 81915001 513 EPQRRLgagggGTSRLKSHPF 533
Cdd:cd14199 269 NPESRI-----SVPEIKLHPW 284
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
 379-478 1.55e-06

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: 50.29  E-value: 1.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCLYSAPEV-GGISELT 457
Cdd:cd07879 114 LSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHADAEMTGYVVTRWYRAPEViLNWMHYN 193

                        90       100
                ....*....|....*....|.
gi 81915001 458 EACDWWSYGSLLYELLTGMAL 478
Cdd:cd07879 194 QTVDIWSVGCIMAEMLTGKTL 214
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 390-517 1.55e-06

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: 49.68  E-value: 1.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLL---LDQAGHIQLTYFGqWSEVEPRcSQEAVDC---LYSAPEVGGISELTEACDWW 463
Cdd:cd14083 109 QVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFG-LSKMEDS-GVMSTACgtpGYVAPEVLAQKPYGKAVDCW 186

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81915001 464 SYGSLLYELLTGMA--LSQSHPSGFQ----AHTQLQLPEW--LSHPAASLLTELLQFEPQRR 517
Cdd:cd14083 187 SIGVISYILLCGYPpfYDENDSKLFAqilkAEYEFDSPYWddISDSAKDFIRHLMEKDPNKR 248
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
 379-534 1.58e-06

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: 50.04  E-value: 1.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRCSQEAVDCLYSAPEVggISE 455
Cdd:cd06658 115 MNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGfcaQVSKEVPKRKSLVGTPYWMAPEV--ISR 192

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 456 L---TEAcDWWSYGSLLYELLTGMALSQSHPSgFQAHTQLQ--LPEWL--SHPAASLLTELLQF----EPQRRLGAgggg 524
Cdd:cd06658 193 LpygTEV-DIWSLGIMVIEMIDGEPPYFNEPP-LQAMRRIRdnLPPRVkdSHKVSSVLRGFLDLmlvrEPSQRATA---- 266

                       170
                ....*....|
gi 81915001 525 tSRLKSHPFF 534
Cdd:cd06658 267 -QELLQHPFL 275
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
 383-478 1.78e-06

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: 49.85  E-value: 1.78e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 383 QVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGH--IQLTYFGqwseveprCSqeavdCL-------------YSA 447
Cdd:cd14210 117 LIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKssIKVIDFG--------SS-----CFegekvytyiqsrfYRA 183

                        90       100       110
                ....*....|....*....|....*....|...
gi 81915001 448 PEVggISEL--TEACDWWSYGSLLYELLTGMAL 478
Cdd:cd14210 184 PEV--ILGLpyDTAIDMWSLGCILAELYTGYPL 214
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
 379-518 1.85e-06

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: 49.26  E-value: 1.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGqWSEVEPRcsQEAVDCL-----YSAPE---- 449
Cdd:cd14075  98 LSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFG-FSTHAKR--GETLNTFcgsppYAAPElfkd 174

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 450 ---VGgiseltEACDWWSYGSLLYELLTGMAlsqshPsgFQAHT-----------QLQLPEWLSHPAASLLTELLQFEPQ 515
Cdd:cd14075 175 ehyIG------IYVDIWALGVLLYFMVTGVM-----P--FRAETvaklkkcilegTYTIPSYVSEPCQELIRGILQPVPS 241


                ...
gi 81915001 516 RRL 518
Cdd:cd14075 242 DRY 244
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
 374-534 1.98e-06

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: 49.35  E-value: 1.98e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 374 RAAWSLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYfgqwSEVEPRCSQEAVD--------C-L 444
Cdd:cd13976  76 RSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEERTKLRL----ESLEDAVILEGEDdslsdkhgCpA 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 445 YSAPEV--GGISELTEACDWWSYGSLLYELLTG-MALSQSHPSGFQA---HTQLQLPEWLSHPAASLLTELLQFEPQRRL 518
Cdd:cd13976 152 YVSPEIlnSGATYSGKAADVWSLGVILYTMLVGrYPFHDSEPASLFAkirRGQFAIPETLSPRARCLIRSLLRREPSERL 231

                       170
                ....*....|....*.
gi 81915001 519 GAggggtSRLKSHPFF 534
Cdd:cd13976 232 TA-----EDILLHPWL 242
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
 390-520 2.09e-06

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: 49.88  E-value: 2.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCLYSAPEVggisELT-----EACDWWS 464
Cdd:cd07856 116 QILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEI----MLTwqkydVEVDIWS 191

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 465 YGSLLYELLTGMAL--SQSHPSGFQAHTQL----------------------QLPEWLSHP-----------AASLLTEL 509
Cdd:cd07856 192 AGCIFAEMLEGKPLfpGKDHVNQFSIITELlgtppddvinticsentlrfvqSLPKRERVPfsekfknadpdAIDLLEKM 271

                       170
                ....*....|.
gi 81915001 510 LQFEPQRRLGA 520
Cdd:cd07856 272 LVFDPKKRISA 282
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
 390-520 2.17e-06

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: 49.29  E-value: 2.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG----QWSEVE----------PRCSQEAVD-------CLYSAP 448
Cdd:cd14046 112 QILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGlatsNKLNVElatqdinkstSAALGSSGDltgnvgtALYVAP 191

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 449 EV--GGISELTEACDWWSYGSLLYELL----TGM----------ALSQSHPSGFqahtqlqlpEWLSHP-AASLLTELLQ 511
Cdd:cd14046 192 EVqsGTKSTYNEKVDMYSLGIIFFEMCypfsTGMervqiltalrSVSIEFPPDF---------DDNKHSkQAKLIRWLLN 262


                ....*....
gi 81915001 512 FEPQRRLGA 520
Cdd:cd14046 263 HDPAKRPSA 271
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
 388-520 2.31e-06

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: 49.18  E-value: 2.31e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 388 AAEMLL----ALEALHQQGVLCRDLNPQNLLL----DQAGHIQLTYFGQWSEVEPRCSQEAVDCLYSAPEVGGISELTEA 459
Cdd:cd14185 100 AALMIIdlceALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKYVTGPIFTVCGTPTYVAPEILSEKGYGLE 179

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81915001 460 CDWWSYGSLLYELLTGMALSQSHPSG----FQ----AHTQLQLPEW--LSHPAASLLTELLQFEPQRRLGA 520
Cdd:cd14185 180 VDMWAAGVILYILLCGFPPFRSPERDqeelFQiiqlGHYEFLPPYWdnISEAAKDLISRLLVVDPEKRYTA 250
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
 381-534 2.63e-06

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: 49.07  E-value: 2.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPR------CSQEavdcLYSAPEVggis 454
Cdd:cd07830  98 ESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREIRSRppytdyVSTR----WYRAPEI---- 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 455 eL------TEACDWWSYGSLLYELLT-------------------------------GMALSQSHPSGFQAHTQLQLPEW 497
Cdd:cd07830 170 -LlrstsySSPVDIWALGCIMAELYTlrplfpgsseidqlykicsvlgtptkqdwpeGYKLASKLGFRFPQFAPTSLHQL 248

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 81915001 498 LSHP---AASLLTELLQFEPQRRLGAggggtSRLKSHPFF 534
Cdd:cd07830 249 IPNAspeAIDLIKDMLRWDPKKRPTA-----SQALQHPYF 283
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 378-518 3.02e-06

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: 49.12  E-value: 3.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLD---QAGHIQLTYFGqWSEVEPR------CSQEAvdclYSAP 448
Cdd:cd14169  97 SYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFG-LSKIEAQgmlstaCGTPG----YVAP 171

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81915001 449 EVGGISELTEACDWWSYGSLLYELLTGMA--LSQSHPSGF----QAHTQLQLPEW--LSHPAASLLTELLQFEPQRRL 518
Cdd:cd14169 172 ELLEQKPYGKAVDVWAIGVISYILLCGYPpfYDENDSELFnqilKAEYEFDSPYWddISESAKDFIRHLLERDPEKRF 249
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
 379-534 3.23e-06

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: 48.81  E-value: 3.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQaGHIQLTYFGqwseveprcSQEAVDC-----------LYSA 447
Cdd:cd07831  97 LPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKD-DILKLADFG---------SCRGIYSkppyteyistrWYRA 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 448 PEVggisELTE-----ACDWWSYGSLLYELLTGMAL--------------------------------------SQSHPS 484
Cdd:cd07831 167 PEC----LLTDgyygpKMDIWAVGCVFFEILSLFPLfpgtneldqiakihdvlgtpdaevlkkfrksrhmnynfPSKKGT 242

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 81915001 485 GFQAHTQLqlpewLSHPAASLLTELLQFEPQRRLGAggggtSRLKSHPFF 534
Cdd:cd07831 243 GLRKLLPN-----ASAEGLDLLKKLLAYDPDERITA-----KQALRHPYF 282
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
 390-474 3.34e-06

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 49.63  E-value: 3.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001  390 EMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCL-----YSAPEVGGISELTEACDWWS 464
Cdd:PTZ00267 177 QIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSLDVASSFcgtpyYLAPELWERKRYSKKADMWS 256

                         90
                 ....*....|
gi 81915001  465 YGSLLYELLT 474
Cdd:PTZ00267 257 LGVILYELLT 266
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
 387-475 3.47e-06

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: 48.89  E-value: 3.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 387 WAAEMLLALEALHQQG---VLCRDLNPQNLLLDQAGH--------IQLTYFG---QWSevepRCSQEAVDCLYS--APEV 450
Cdd:cd14145 109 WAVQIARGMNYLHCEAivpVIHRDLKSSNILILEKVEngdlsnkiLKITDFGlarEWH----RTTKMSAAGTYAwmAPEV 184

                        90       100
                ....*....|....*....|....*
gi 81915001 451 GGISELTEACDWWSYGSLLYELLTG 475
Cdd:cd14145 185 IRSSMFSKGSDVWSYGVLLWELLTG 209
MIT_2 cd02684
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 60-116 4.01e-06

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in proteins with an n-terminal serine/threonine kinase domain. The molecular function of the MIT domain is unclear.


Pssm-ID: 239147  Cd Length: 75  Bit Score: 44.81  E-value: 4.01e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 81915001  60 ALERDVSEDYEAAFNHYQNGVDVLLRGVHVDPNKERREAVKLKITKYLRRAEEIFNC 116
Cdd:cd02684  13 AVKKDQRGDAAAALSLYCSALQYFVPALHYETDAQRKEALRQKVLQYVSRAEELKAL 69
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 390-533 4.06e-06

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: 48.57  E-value: 4.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLLL---DQAGHIQLTYFGQWSEVE---PRCSQEAVDCLYSAPEVGGISELTEACDWW 463
Cdd:cd14086 108 QILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQgdqQAWFGFAGTPGYLSPEVLRKDPYGKPVDIW 187

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 464 SYGSLLYELLTGmalsqsHPSgFQAHTQLQL-------------PEW--LSHPAASLLTELLQFEPQRRLGAggggTSRL 528
Cdd:cd14086 188 ACGVILYILLVG------YPP-FWDEDQHRLyaqikagaydypsPEWdtVTPEAKDLINQMLTVNPAKRITA----AEAL 256


                ....*
gi 81915001 529 KsHPF 533
Cdd:cd14086 257 K-HPW 260
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
 383-534 4.27e-06

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: 48.72  E-value: 4.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 383 QVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAG-------------------HIQLTYFGQ---WSE-----VEPR 435
Cdd:cd14134 116 HVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDyvkvynpkkkrqirvpkstDIKLIDFGSatfDDEyhssiVSTR 195

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 436 csqeavdcLYSAPEVggISEL--TEACDWWSYGSLLYELLTGMALSQSH----------------PS------------G 485
Cdd:cd14134 196 --------HYRAPEV--ILGLgwSYPCDVWSIGCILVELYTGELLFQTHdnlehlammerilgplPKrmirrakkgakyF 265

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81915001 486 FQAHTQLQLPEWLSHPAAS-----------------------LLTELLQFEPQRRLGAggggtSRLKSHPFF 534
Cdd:cd14134 266 YFYHGRLDWPEGSSSGRSIkrvckplkrlmllvdpehrllfdLIRKMLEYDPSKRITA-----KEALKHPFF 332
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
 379-534 5.18e-06

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: 48.44  E-value: 5.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRCSQEAVDCLYSAPEVGGISE 455
Cdd:cd06659 114 LNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGfcaQISKDVPKRKSLVGTPYWMAPEVISRCP 193

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 456 LTEACDWWSYGSLLYELLTGMALSQSHpSGFQAHTQLQ--LPEWL--SHPAASLLTELLQF----EPQRRLGAggggtSR 527
Cdd:cd06659 194 YGTEVDIWSLGIMVIEMVDGEPPYFSD-SPVQAMKRLRdsPPPKLknSHKASPVLRDFLERmlvrDPQERATA-----QE 267


                ....*..
gi 81915001 528 LKSHPFF 534
Cdd:cd06659 268 LLDHPFL 274
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
 394-521 6.17e-06

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: 47.71  E-value: 6.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 394 ALEALHQQGVLCRDLNPQNLLL--DQAG--HIQLTYFGQWSEVEPRCSQEAVDCLYSAPEVggISELTEAC--DWWSYGS 467
Cdd:cd14095 110 ALKYLHSLSIVHRDIKPENLLVveHEDGskSLKLADFGLATEVKEPLFTVCGTPTYVAPEI--LAETGYGLkvDIWAAGV 187

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81915001 468 LLYELLTGMALSQShPSGFQ---------AHTQLQLPEW--LSHPAASLLTELLQFEPQRRLGAG 521
Cdd:cd14095 188 ITYILLCGFPPFRS-PDRDQeelfdlilaGEFEFLSPYWdnISDSAKDLISRMLVVDPEKRYSAG 251
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
 380-533 6.85e-06

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: 47.76  E-value: 6.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 380 REGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGqwseVEPRcSQEAVD----------CLYSAPE 449
Cdd:cd06629 106 EEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFG----ISKK-SDDIYGnngatsmqgsVFWMAPE 180

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 450 VggISELTEA----CDWWSYGSLLYELLTG----------------MALSQSHPsgfqahtqlqLPE--WLSHPAASLLT 507
Cdd:cd06629 181 V--IHSQGQGysakVDIWSLGCVVLEMLAGrrpwsddeaiaamfklGNKRSAPP----------VPEdvNLSPEALDFLN 248

                       170       180
                ....*....|....*....|....*.
gi 81915001 508 ELLQFEPQRRLGAggggtSRLKSHPF 533
Cdd:cd06629 249 ACFAIDPRDRPTA-----AELLSHPF 269
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
 391-534 7.31e-06

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: 47.72  E-value: 7.31e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 391 MLLALEALHQQ-GVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDC-LYSAPEVGGISELTEACDWWSYGSL 468
Cdd:cd06605 108 VVKGLIYLHEKhKIIHRDVKPSNILVNSRGQVKLCDFGVSGQLVDSLAKTFVGTrSYMAPERISGGKYTVKSDIWSLGLS 187

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81915001 469 LYELLTG---MALSQSHPSG--FQAHTQL------QLP-EWLSHPAASLLTELLQFEPQRRLGAggggtSRLKSHPFF 534
Cdd:cd06605 188 LVELATGrfpYPPPNAKPSMmiFELLSYIvdepppLLPsGKFSPDFQDFVSQCLQKDPTERPSY-----KELMEHPFI 260
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
 390-536 8.92e-06

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: 47.75  E-value: 8.92e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG------QWSEVEPRCSQEAVDCL-YSAPEVG-GISELTEACD 461
Cdd:cd07855 117 QLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGmarglcTSPEEHKYFMTEYVATRwYRAPELMlSLPEYTQAID 196

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 462 WWSYGSLLYELLTGMAL----SQSH-----------PSG--------------FQAHTQLQLPEW------LSHPAASLL 506
Cdd:cd07855 197 MWSVGCIFAEMLGRRQLfpgkNYVHqlqliltvlgtPSQavinaigadrvrryIQNLPNKQPVPWetlypkADQQALDLL 276

                       170       180       190
                ....*....|....*....|....*....|
gi 81915001 507 TELLQFEPQRRLGAggggtSRLKSHPFFST 536
Cdd:cd07855 277 SQMLRFDPSERITV-----AEALQHPFLAK 301
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
 344-475 9.11e-06

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: 47.45  E-value: 9.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 344 REGADRVLGAYGRGRGRNP--------PSANRASL---GSGRAAWSLRegqvKQWAAEMLLALEALH--QQGVLCRDLNP 410
Cdd:cd13978  48 RARHSYVLPLLGVCVERRSlglvmeymENGSLKSLlerEIQDVPWSLR----FRIIHEIALGMNFLHnmDPPLLHHDLKP 123

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81915001 411 QNLLLDQAGHIQLTYFG-----QWSEVEPRCSQEAVD---CLYSAPEV--GGISELTEACDWWSYGSLLYELLTG 475
Cdd:cd13978 124 ENILLDNHFHVKISDFGlsklgMKSISANRRRGTENLggtPIYMAPEAfdDFNKKPTSKSDVYSFAIVIWAVLTR 198
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
 379-535 1.18e-05

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: 47.47  E-value: 1.18e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHI-QLTYFGQWSEVEPR------CSQEAVDCLYSAPE-V 450
Cdd:cd07854 111 LSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVlKIGDFGLARIVDPHyshkgyLSEGLVTKWYRSPRlL 190

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 451 GGISELTEACDWWSYGSLLYELLTG-MALSQSH---------------------------PS-----GFQAHTQLQ--LP 495
Cdd:cd07854 191 LSPNNYTKAIDMWAAGCIFAEMLTGkPLFAGAHeleqmqlilesvpvvreedrnellnviPSfvrndGGEPRRPLRdlLP 270

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 81915001 496 EwLSHPAASLLTELLQFEPQRRLGAGGGgtsrlKSHPFFS 535
Cdd:cd07854 271 G-VNPEALDFLEQILTFNPMDRLTAEEA-----LMHPYMS 304
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 379-472 1.18e-05

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: 47.03  E-value: 1.18e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHI-QLTYFGQWSEVEPRCSQEAV---DClYSAPEVGGIS 454
Cdd:cd08220  98 LSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVvKIGDFGISKILSSKSKAYTVvgtPC-YISPELCEGK 176

                        90
                ....*....|....*...
gi 81915001 455 ELTEACDWWSYGSLLYEL 472
Cdd:cd08220 177 PYNQKSDIWALGCVLYEL 194
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
 379-489 1.49e-05

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: 46.96  E-value: 1.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAV---DCLYSAPEVGGISE 455
Cdd:cd06645 105 LSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKRKSfigTPYWMAPEVAAVER 184

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 81915001 456 ---LTEACDWWSYGsllyelLTGMALSQSHPSGFQAH 489
Cdd:cd06645 185 kggYNQLCDIWAVG------ITAIELAELQPPMFDLH 215
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
 381-534 1.49e-05

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: 46.65  E-value: 1.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAG-HIQLTYFGQWSEVEPRCS-------QEAVDCLYSAPEVGG 452
Cdd:cd06630 102 ENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGqRLRIADFGAAARLASKGTgagefqgQLLGTIAFMAPEVLR 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 453 ISELTEACDWWSYGSLLYELLTGmalsqSHPSGFQAHT-QLQL-------------PEWLSHPAASLLTELLQFEPQRRL 518
Cdd:cd06630 182 GEQYGRSCDVWSVGCVIIEMATA-----KPPWNAEKISnHLALifkiasattpppiPEHLSPGLRDVTLRCLELQPEDRP 256

                       170
                ....*....|....*.
gi 81915001 519 GAggggtSRLKSHPFF 534
Cdd:cd06630 257 PA-----RELLKHPVF 267
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
 379-473 1.60e-05

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: 46.52  E-value: 1.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLdQAGHIQLTYFGqWSEVEPRCSQEAVDCL-----YSAPEV-GG 452
Cdd:cd14163  98 LPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFG-FAKQLPKGGRELSQTFcgstaYAAPEVlQG 175

                        90       100
                ....*....|....*....|.
gi 81915001 453 ISELTEACDWWSYGSLLYELL 473
Cdd:cd14163 176 VPHDSRKGDIWSMGVVLYVML 196
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
 394-517 1.88e-05

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: 46.52  E-value: 1.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 394 ALEALHQQGVLCRDLNPQNLLLDQ-AGHIQLTYFG-----------QWSEVEP---RCSQEAVDC---LYSAPEVGGISE 455
Cdd:cd13996 119 GVSYIHSKGIVHRDLKPSNIFLDNdDLQVKIGDFGlatsignqkreLNNLNNNnngNTSNNSVGIgtpLYASPEQLDGEN 198

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81915001 456 LTEACDWWSYGSLLYELL----TGMALSQShpsgFQAHTQLQLPEWL--SHPA-ASLLTELLQFEPQRR 517
Cdd:cd13996 199 YNEKADIYSLGIILFEMLhpfkTAMERSTI----LTDLRNGILPESFkaKHPKeADLIQSLLSKNPEER 263
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
 370-509 1.94e-05

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: 46.58  E-value: 1.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 370 LGSGRAAWSLREG-----QVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRCSQEAV 441
Cdd:cd06640  84 LGGGSALDLLRAGpfdefQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGvagQLTDTQIKRNTFVG 163

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81915001 442 DCLYSAPEVGGISELTEACDWWSYGsllyelLTGMALSQSHPSGFQAHTQLQLPEWLSHPAASLLTEL 509
Cdd:cd06640 164 TPFWMAPEVIQQSAYDSKADIWSLG------ITAIELAKGEPPNSDMHPMRVLFLIPKNNPPTLVGDF 225
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
 373-496 2.03e-05

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: 46.39  E-value: 2.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 373 GRAAWSLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLL--DQAGHIQLTYFGQWSEVEP--RCSQEAVDCLYSAP 448
Cdd:cd14104  88 TTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYctRRGSYIKIIEFGQSRQLKPgdKFRLQYTSAEFYAP 167

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 81915001 449 EVGGISELTEACDWWSYGSLLYELLTGMalsqshpSGFQAHTQLQLPE 496
Cdd:cd14104 168 EVHQHESVSTATDMWSLGCLVYVLLSGI-------NPFEAETNQQTIE 208
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
 390-478 2.24e-05

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: 46.58  E-value: 2.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCLYSAPEVG-GISELTEACDWWSYGSL 468
Cdd:cd07878 126 QLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQADDEMTGYVATRWYRAPEIMlNWMHYNQTVDIWSVGCI 205

                        90
                ....*....|
gi 81915001 469 LYELLTGMAL 478
Cdd:cd07878 206 MAELLKGKAL 215
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
 378-517 2.30e-05

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: 46.23  E-value: 2.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSE---VEPRCSQEavdcLYSAPE-V 450
Cdd:cd14073  97 RLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGlsnLYSKdklLQTFCGSP----LYASPEiV 172

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81915001 451 GGISELTEACDWWSYGSLLYELLTGmalsqSHPSGFQAHTQL--QL-------PEWLSHpAASLLTELLQFEPQRR 517
Cdd:cd14073 173 NGTPYQGPEVDCWSLGVLLYTLVYG-----TMPFDGSDFKRLvkQIssgdyrePTQPSD-ASGLIRWMLTVNPKRR 242
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
 374-522 2.42e-05

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: 46.03  E-value: 2.42e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 374 RAAWSLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGqwseVEPRCSQEAVD--------C-L 444
Cdd:cd14024  76 RRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVLVN----LEDSCPLNGDDdsltdkhgCpA 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 445 YSAPEV--GGISELTEACDWWSYGSLLYELLTGMALSQ-SHPSGFQAHTQ---LQLPEWLSHPAASLLTELLQFEPQRRL 518
Cdd:cd14024 152 YVGPEIlsSRRSYSGKAADVWSLGVCLYTMLLGRYPFQdTEPAALFAKIRrgaFSLPAWLSPGARCLVSCMLRRSPAERL 231


                ....
gi 81915001 519 GAGG 522
Cdd:cd14024 232 KASE 235
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
 378-534 2.52e-05

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: 45.93  E-value: 2.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAV-------DCLYSAPEV 450
Cdd:cd14165  98 ALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDENGRIVlsktfcgSAAYAAPEV 177

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 451 -GGISELTEACDWWSYGSLLYELLTG-MALSQSHPSGF---QAHTQLQLPEW--LSHPAASLLTELLQFEPQRRLgaggg 523
Cdd:cd14165 178 lQGIPYDPRIYDIWSLGVILYIMVCGsMPYDDSNVKKMlkiQKEHRVRFPRSknLTSECKDLIYRLLQPDVSQRL----- 252

                       170
                ....*....|.
gi 81915001 524 GTSRLKSHPFF 534
Cdd:cd14165 253 CIDEVLSHPWL 263
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
 390-509 2.68e-05

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: 46.57  E-value: 2.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCLYSAPEVG-GISELTEACDWWSYGSL 468
Cdd:cd07877 128 QILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMlNWMHYNQTVDIWSVGCI 207

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 81915001 469 LYELLTGMALSqshpSGFQAHTQLQLPEWLS-HPAASLLTEL 509
Cdd:cd07877 208 MAELLTGRTLF----PGTDHIDQLKLILRLVgTPGAELLKKI 245
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
 390-533 2.81e-05

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: 46.05  E-value: 2.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLLLDQaGHIQLTYFGQWSEVEP------RCSQ---------EAVDCLYSAPEVGGIS 454
Cdd:cd14131 111 QMLEAVHTIHEEGIVHSDLKPANFLLVK-GRLKLIDFGIAKAIQNdttsivRDSQvgtlnymspEAIKDTSASGEGKPKS 189

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 455 ELTEACDWWSYGSLLYELLTGMALSQSHPSGFQAHTQLQLP----EWLSHPAASLLTEL---LQFEPQRRLgagggGTSR 527
Cdd:cd14131 190 KIGRPSDVWSLGCILYQMVYGKTPFQHITNPIAKLQAIIDPnheiEFPDIPNPDLIDVMkrcLQRDPKKRP-----SIPE 264


                ....*.
gi 81915001 528 LKSHPF 533
Cdd:cd14131 265 LLNHPF 270
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
 379-534 2.97e-05

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: 45.76  E-value: 2.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEA--VDCLY-SAPEVGGI-- 453
Cdd:cd06613  94 LSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATIAKRKsfIGTPYwMAPEVAAVer 173

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 454 -SELTEACDWWSYGSLLYELLTGM-ALSQSHP---------SGFQAHTqLQLPEWLSHPAASLLTELLQFEPQRRLGAGg 522
Cdd:cd06613 174 kGGYDGKCDIWALGITAIELAELQpPMFDLHPmralflipkSNFDPPK-LKDKEKWSPDFHDFIKKCLTKNPKKRPTAT- 251

                       170
                ....*....|..
gi 81915001 523 ggtsRLKSHPFF 534
Cdd:cd06613 252 ----KLLQHPFV 259
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
 386-486 3.17e-05

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: 45.78  E-value: 3.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 386 QWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGqWSEVEPRCSQE-------AVDCLYSAPEVGGISELTE 458
Cdd:cd14205 112 QYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFG-LTKVLPQDKEYykvkepgESPIFWYAPESLTESKFSV 190

                        90       100
                ....*....|....*....|....*...
gi 81915001 459 ACDWWSYGSLLYELLTGMALSQSHPSGF 486
Cdd:cd14205 191 ASDVWSFGVVLYELFTYIEKSKSPPAEF 218
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
 388-472 3.28e-05

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: 45.88  E-value: 3.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 388 AAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGqwseveprCSQEAVDCL---------YSAPE--VGGISEL 456
Cdd:cd06621 111 AESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFG--------VSGELVNSLagtftgtsyYMAPEriQGGPYSI 182

                        90
                ....*....|....*.
gi 81915001 457 TeaCDWWSYGSLLYEL 472
Cdd:cd06621 183 T--SDVWSLGLTLLEV 196
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
 383-517 3.33e-05

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: 45.33  E-value: 3.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 383 QVKQWAAEMLLALEALHQQG---VLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCL-YSAPEVGGISELTE 458
Cdd:cd14060  85 QIMTWATDIAKGMHYLHMEApvkVIHRDLKSRNVVIAADGVLKICDFGASRFHSHTTHMSLVGTFpWMAPEVIQSLPVSE 164

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81915001 459 ACDWWSYGSLLYELLT------GMALSQSHPSGFQAHTQLQLPEWLSHPAASLLTELLQFEPQRR 517
Cdd:cd14060 165 TCDTYSYGVVLWEMLTrevpfkGLEGLQVAWLVVEKNERPTIPSSCPRSFAELMRRCWEADVKER 229
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
 381-520 3.63e-05

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: 46.00  E-value: 3.63e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLL---DQAGHIQLTYFG---QWSEVEPRCSQEAVDCLYSAPEVGGIS 454
Cdd:cd14094 108 EAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGvaiQLGESGLVAGGRVGTPHFMAPEVVKRE 187

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81915001 455 ELTEACDWWSYGSLLYELLTGM-----ALSQSHPSGFQAHTQLQLPEW--LSHPAASLLTELLQFEPQRRLGA 520
Cdd:cd14094 188 PYGKPVDVWGCGVILFILLSGClpfygTKERLFEGIIKGKYKMNPRQWshISESAKDLVRRMLMLDPAERITV 260
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
 366-517 3.68e-05

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 46.40  E-value: 3.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001  366 NRAslgsgRAAWSLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGqWSEVEPRCSQEAVD--- 442
Cdd:PTZ00283 132 SRA-----KTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFG-FSKMYAATVSDDVGrtf 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001  443 C---LYSAPEVGGISELTEACDWWSYGSLLYELLTgmalsQSHP-SGFQAHTQLQ---------LPEWLSHPAASLLTEL 509
Cdd:PTZ00283 206 CgtpYYVAPEIWRRKPYSKKADMFSLGVLLYELLT-----LKRPfDGENMEEVMHktlagrydpLPPSISPEMQEIVTAL 280


                 ....*...
gi 81915001  510 LQFEPQRR 517
Cdd:PTZ00283 281 LSSDPKRR 288
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
 379-478 3.98e-05

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: 45.49  E-value: 3.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEP---RCSQEAVDCLYSAPE-VGGIS 454
Cdd:cd07846  97 LDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAApgeVYTDYVATRWYRAPElLVGDT 176

                        90       100
                ....*....|....*....|....
gi 81915001 455 ELTEACDWWSYGSLLYELLTGMAL 478
Cdd:cd07846 177 KYGKAVDVWAVGCLVTEMLTGEPL 200
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
 390-478 4.31e-05

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: 45.93  E-value: 4.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQ-------------WSE-VEPRcsqeavdcLYSAPEVGG--I 453
Cdd:cd07859 111 QLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLarvafndtptaifWTDyVATR--------WYRAPELCGsfF 182

                        90       100
                ....*....|....*....|....*
gi 81915001 454 SELTEACDWWSYGSLLYELLTGMAL 478
Cdd:cd07859 183 SKYTPAIDIWSIGCIFAEVLTGKPL 207
MIT_1 cd02683
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 53-113 4.35e-05

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in proteins with unknown function, co-occuring with an as yet undescribed domain. The molecular function of the MIT domain is unclear.


Pssm-ID: 239146  Cd Length: 77  Bit Score: 42.03  E-value: 4.35e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81915001  53 AATQIHLALERDVSEDYEAAFNHYQNGVDVLLRGVHVDPNKERREAVKLKITKYLRRAEEI 113
Cdd:cd02683   6 AKEVLKRAVELDQEGRFQEALVCYQEGIDLLMQVLKGTKDEAKKKNLRQKISEYMDRAEAI 66
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
 379-530 4.51e-05

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: 45.29  E-value: 4.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAG----H--IQLTY---FGQWSevepRCSQEAVDCLYSAPE 449
Cdd:cd14039  96 LKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINgkivHkiIDLGYakdLDQGS----LCTSFVGTLQYLAPE 171

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 450 VGGISELTEACDWWSYGSLLYELLTGMALSQSHPSGFQAHTQLQ----------------------LPE------WLSHP 501
Cdd:cd14039 172 LFENKSYTVTVDYWSFGTMVFECIAGFRPFLHNLQPFTWHEKIKkkdpkhifaveemngevrfsthLPQpnnlcsLIVEP 251

                       170       180
                ....*....|....*....|....*....
gi 81915001 502 AASLLTELLQFEPQRRlgaGGGGTSRLKS 530
Cdd:cd14039 252 MEGWLQLMLNWDPVQR---GGGLDTDSKQ 277
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
 374-478 4.66e-05

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: 45.82  E-value: 4.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 374 RAAWSLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRCSQEAVDCLYSAPEV 450
Cdd:cd07858 100 RSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGlarTTSEKGDFMTEYVVTRWYRAPEL 179

                        90       100
                ....*....|....*....|....*....
gi 81915001 451 -GGISELTEACDWWSYGSLLYELLTGMAL 478
Cdd:cd07858 180 lLNCSEYTTAIDVWSVGCIFAELLGRKPL 208
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
 394-475 4.85e-05

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: 45.44  E-value: 4.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 394 ALEALH----QQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSE-VEPRCSQEAVDC-LYSAPEVGGISELTE---ACDWWS 464
Cdd:cd06618 123 IVKALHylkeKHGVIHRDVKPSNILLDESGNVKLCDFGISGRlVDSKAKTRSAGCaAYMAPERIDPPDNPKydiRADVWS 202

                        90
                ....*....|.
gi 81915001 465 YGSLLYELLTG 475
Cdd:cd06618 203 LGISLVELATG 213
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
 378-533 5.07e-05

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: 45.37  E-value: 5.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEpRCSQEAVDCL----YSAPEVGGI 453
Cdd:cd06608 109 RLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSAQLD-STLGRRNTFIgtpyWMAPEVIAC 187

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 454 SELTEA-----CDWWSYGsllyelLTGMALSQSHPSGFQAHTQLQL-------PEWLSHPAA------SLLTELLQFEPQ 515
Cdd:cd06608 188 DQQPDAsydarCDVWSLG------ITAIELADGKPPLCDMHPMRALfkiprnpPPTLKSPEKwskefnDFISECLIKNYE 261

                       170
                ....*....|....*...
gi 81915001 516 RRlgaggGGTSRLKSHPF 533
Cdd:cd06608 262 QR-----PFTEELLEHPF 274
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
 395-517 5.21e-05

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: 44.83  E-value: 5.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 395 LEALHQ--QGVLCRDLNPQNLLLDQAGHIQLTYFGQ----WSEVEPRCSQEAVDCLYSAPEV-GGISELTEACDWWSYGS 467
Cdd:cd14064 106 MEYLHNltQPIIHRDLNSHNILLYEDGHAVVADFGEsrflQSLDEDNMTKQPGNLRWMAPEVfTQCTRYSIKADVFSYAL 185

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 81915001 468 LLYELLTG-MALSQSHPSGFQA-----HTQLQLPEWLSHPAASLLTELLQFEPQRR 517
Cdd:cd14064 186 CLWELLTGeIPFAHLKPAAAAAdmayhHIRPPIGYSIPKPISSLLMRGWNAEPESR 241
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
 394-475 5.26e-05

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: 45.41  E-value: 5.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 394 ALEALHQQGVLCRDLNPQNLLL---DQAGHIQLTYFGQWSEVE----------PRCSQEAVDCLYSAPEVggISELTEA- 459
Cdd:cd14174 112 ALDFLHTKGIAHRDLKPENILCespDKVSPVKICDFDLGSGVKlnsactpittPELTTPCGSAEYMAPEV--VEVFTDEa 189

                        90       100
                ....*....|....*....|..
gi 81915001 460 ------CDWWSYGSLLYELLTG 475
Cdd:cd14174 190 tfydkrCDLWSLGVILYIMLSG 211
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
 379-475 5.40e-05

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: 45.40  E-value: 5.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRCSQEAVDCLYSAPEVGGISE 455
Cdd:cd06657 113 MNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGfcaQVSKEVPRRKSLVGTPYWMAPELISRLP 192

                        90       100
                ....*....|....*....|
gi 81915001 456 LTEACDWWSYGSLLYELLTG 475
Cdd:cd06657 193 YGPEVDIWSLGIMVIEMVDG 212
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 381-521 5.42e-05

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: 45.11  E-value: 5.42e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQaGHIQLTYFGQwSEVEPRCSQEAVDC----LYSAPEVGGISEL 456
Cdd:cd08222 105 ENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKN-NVIKVGDFGI-SRILMGTSDLATTFtgtpYYMSPEVLKHEGY 182

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81915001 457 TEACDWWSYGSLLYELLTgmalsQSHpsGFQAHTQL------------QLPEWLSHPAASLLTELLQFEPQRRLGAG 521
Cdd:cd08222 183 NSKSDIWSLGCILYEMCC-----LKH--AFDGQNLLsvmykivegetpSLPDKYSKELNAIYSRMLNKDPALRPSAA 252
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
 374-535 5.54e-05

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: 45.47  E-value: 5.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 374 RAAWSLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG-------QWSEVEPRCSQEAVDCLYS 446
Cdd:cd07857  97 RSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGlargfseNPGENAGFMTEYVATRWYR 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 447 APEVG-GISELTEACDWWSYGSLLYELLTG------------------------------MALSQSHPSGFQAHTQLQLP 495
Cdd:cd07857 177 APEIMlSFQSYTKAIDVWSVGCILAELLGRkpvfkgkdyvdqlnqilqvlgtpdeetlsrIGSPKAQNYIRSLPNIPKKP 256

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 81915001 496 -EWL----SHPAASLLTELLQFEPQRRLgagggGTSRLKSHPFFS 535
Cdd:cd07857 257 fESIfpnaNPLALDLLEKLLAFDPTKRI-----SVEEALEHPYLA 296
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
 384-517 5.55e-05

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: 45.03  E-value: 5.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 384 VKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQaGHIQLTYFGQWS--EVEPRCSQEavDCL--------YSAPEV--- 450
Cdd:cd14063  99 TVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLEN-GRVVITDFGLFSlsGLLQPGRRE--DTLvipngwlcYLAPEIira 175

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 451 -------GGISELTEACDWWSYGSLLYELLTG-MALSQSHP--------SGF-QAHTQLQLPEWLShpaaSLLTELLQFE 513
Cdd:cd14063 176 lspdldfEESLPFTKASDVYAFGTVWYELLAGrWPFKEQPAesiiwqvgCGKkQSLSQLDIGREVK----DILMQCWAYD 251


                ....
gi 81915001 514 PQRR 517
Cdd:cd14063 252 PEKR 255
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
 394-475 5.73e-05

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: 45.07  E-value: 5.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 394 ALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEV-EPRCSQEAVD-----CLYSAPEVGGISELTEACDWWSYGS 467
Cdd:cd13979 115 ALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLgEGNEVGTPRShiggtYTYRAPELLKGERVTPKADIYSFGI 194


                ....*...
gi 81915001 468 LLYELLTG 475
Cdd:cd13979 195 TLWQMLTR 202
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
 394-517 5.85e-05

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: 44.91  E-value: 5.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 394 ALEALHQQGVLCRDLNPQNLLL-----DQAGHIQLTYFGqwseVEPRCSQEAVDCL-----YSAPEVG-GISELTEACDW 462
Cdd:cd14000 124 GLRYLHSAMIIYRDLKSHNVLVwtlypNSAIIIKIADYG----ISRQCCRMGAKGSegtpgFRAPEIArGNVIYNEKVDV 199

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81915001 463 WSYGSLLYELLTGMALSQSH---PSGFQAHTQLQLPewLSHPAAS-------LLTELLQFEPQRR 517
Cdd:cd14000 200 FSFGMLLYEILSGGAPMVGHlkfPNEFDIHGGLRPP--LKQYECApwpevevLMKKCWKENPQQR 262
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
 390-534 6.25e-05

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: 44.91  E-value: 6.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLLLD-QAGHIQLTYFGQWSEVEPRCSQEAvDCL----YSAPEVggiseL------TE 458
Cdd:cd14019 109 NLFKALKHVHSFGIIHRDVKPGNFLYNrETGKGVLVDFGLAQREEDRPEQRA-PRAgtrgFRAPEV-----LfkcphqTT 182

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 459 ACDWWSYGSLLYELLTGmalsqSHPSGFQAHTQLQLPEWLS----HPAASLLTELLQFEPQRRLGAggggtSRLKSHPFF 534
Cdd:cd14019 183 AIDIWSAGVILLSILSG-----RFPFFFSSDDIDALAEIATifgsDEAYDLLDKLLELDPSKRITA-----EEALKHPFF 252
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
 398-522 6.60e-05

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: 44.95  E-value: 6.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 398 LHQQGVLCRDLNPQNLL-LDQAGH-IQLTYFGQWSEVEPRcsqEAVDCLYS-----APEVGGISELTEACDWWSYGSLLY 470
Cdd:cd14192 118 LHQHYILHLDLKPENILcVNSTGNqIKIIDFGLARRYKPR---EKLKVNFGtpeflAPEVVNYDFVSFPTDMWSVGVITY 194

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 471 ELLTG----MALSQSHPSGFQAHTQLQLP----EWLSHPAASLLTELLQFEPQRRLGAGG 522
Cdd:cd14192 195 MLLSGlspfLGETDAETMNNIVNCKWDFDaeafENLSEEAKDFISRLLVKEKSCRMSATQ 254
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
 379-538 6.92e-05

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: 44.74  E-value: 6.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQwSEVEPRCSQEAVDCL------YSAPEVGG 452
Cdd:cd05041  91 LTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGM-SREEEDGEYTVSDGLkqipikWTAPEALN 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 453 ISELTEACDWWSYGSLLYELLTGMALSQSHPSGFQAHTQ------LQLPEWLSHPAASLLTELLQFEPQRRlgaggggts 526
Cdd:cd05041 170 YGRYTSESDVWSFGILLWEIFSLGATPYPGMSNQQTREQiesgyrMPAPELCPEAVYRLMLQCWAYDPENR--------- 240

                       170
                ....*....|..
gi 81915001 527 rlkshPFFSTIQ 538
Cdd:cd05041 241 -----PSFSEIY 247
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
 379-483 7.03e-05

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: 44.68  E-value: 7.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRCSQEAVDCLYSAPEVGGISE 455
Cdd:cd06641  98 LDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGvagQLTDTQIKRN*FVGTPFWMAPEVIKQSA 177

                        90       100
                ....*....|....*....|....*....
gi 81915001 456 LTEACDWWSYGSLLYELLTGM-ALSQSHP 483
Cdd:cd06641 178 YDSKADIWSLGITAIELARGEpPHSELHP 206
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 379-494 7.16e-05

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: 44.73  E-value: 7.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRcSQEAVDCL----YSAPEVGGIS 454
Cdd:cd08221  98 FPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSE-SSMAESIVgtpyYMSPELVQGV 176

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 81915001 455 ELTEACDWWSYGSLLYELLTgmaLSQShpsgFQAHTQLQL 494
Cdd:cd08221 177 KYNFKSDIWAVGCVLYELLT---LKRT----FDATNPLRL 209
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
 394-533 8.37e-05

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: 44.25  E-value: 8.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 394 ALEALHQQGVLCRDLNPQNLLL----DQAGHIQLTYFGQWSEVEPRCSQEAVDCLYSAPEVGGISELTEACDWWSYGSLL 469
Cdd:cd14184 111 ALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATVVEGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVIT 190

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81915001 470 YELLTGMALSQSHpSGFQ---------AHTQLQLPEW--LSHPAASLLTELLQFEPQRRLGAGgggtsRLKSHPF 533
Cdd:cd14184 191 YILLCGFPPFRSE-NNLQedlfdqillGKLEFPSPYWdnITDSAKELISHMLQVNVEARYTAE-----QILSHPW 259
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
 378-475 8.99e-05

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: 44.56  E-value: 8.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQN-LLLDQAG---HIQLTYFGQWSEVEPRCSQEAV--DCLYSAPEVG 451
Cdd:cd14196 104 SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIpipHIKLIDFGLAHEIEDGVEFKNIfgTPEFVAPEIV 183

                        90       100
                ....*....|....*....|....
gi 81915001 452 GISELTEACDWWSYGSLLYELLTG 475
Cdd:cd14196 184 NYEPLGLEADMWSIGVITYILLSG 207
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
 378-486 9.16e-05

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: 44.51  E-value: 9.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEP-----RCSQEAVD-CLYSAPEVG 451
Cdd:cd05080 103 SIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVPEgheyyRVREDGDSpVFWYAPECL 182

                        90       100       110
                ....*....|....*....|....*....|....*
gi 81915001 452 GISELTEACDWWSYGSLLYELLTGMALSQSHPSGF 486
Cdd:cd05080 183 KEYKFYYASDVWSFGVTLYELLTHCDSSQSPPTKF 217
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
 390-483 1.05e-04

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: 44.23  E-value: 1.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRCSQEAVDCLYSAPEVGGI-----SELTEACD 461
Cdd:cd06638 132 EALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGvsaQLTSTRLRRNTSVGTPFWMAPEVIACeqqldSTYDARCD 211

                        90       100
                ....*....|....*....|...
gi 81915001 462 WWSYGSLLYELLTG-MALSQSHP 483
Cdd:cd06638 212 VWSLGITAIELGDGdPPLADLHP 234
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
386-475 1.12e-04

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 44.79  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001  386 QWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG-----------QWSEVeprcsqeavdcL----YSAPEV 450
Cdd:NF033483 111 EIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGiaralssttmtQTNSV-----------LgtvhYLSPEQ 179

                         90       100
                 ....*....|....*....|....*..
gi 81915001  451 --GGISelTEACDWWSYGSLLYELLTG 475
Cdd:NF033483 180 arGGTV--DARSDIYSLGIVLYEMLTG 204
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
 382-474 1.17e-04

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: 43.96  E-value: 1.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 382 GQVKQWAAEMLLALEALHQ---QGVLCRDLNPQNLLL-DQAGHIQLTYFGQWSEVEPRCSQEAVDCLYSAPEVGGISELT 457
Cdd:cd14058  89 AHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLtNGGTVLKICDFGTACDISTHMTNNKGSAAWMAPEVFEGSKYS 168

                        90
                ....*....|....*..
gi 81915001 458 EACDWWSYGSLLYELLT 474
Cdd:cd14058 169 EKCDVFSWGIILWEVIT 185
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
 395-476 1.21e-04

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: 43.85  E-value: 1.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 395 LEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG------QWSEVEPrCSQEAVDCLYSAPEVGGISE---LTEACDWWSY 465
Cdd:cd14150 109 MDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGlatvktRWSGSQQ-VEQPSGSILWMAPEVIRMQDtnpYSFQSDVYAY 187

                        90
                ....*....|.
gi 81915001 466 GSLLYELLTGM 476
Cdd:cd14150 188 GVVLYELMSGT 198
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
 379-521 1.28e-04

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: 44.26  E-value: 1.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDcLYSAPEVggISELTE 458
Cdd:cd06633 118 LQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPANSFVGTP-YWMAPEV--ILAMDE 194

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 459 A-----CDWWSYGsllyelLTGMALSQSHPSGFQAHTQ-------------LQLPEWlSHPAASLLTELLQFEPQRRLGA 520
Cdd:cd06633 195 GqydgkVDIWSLG------ITCIELAERKPPLFNMNAMsalyhiaqndsptLQSNEW-TDSFRGFVDYCLQKIPQERPSS 267


                .
gi 81915001 521 G 521
Cdd:cd06633 268 A 268
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
 394-533 1.33e-04

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: 43.69  E-value: 1.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 394 ALEALHQQGVLCRDLNPQNLLLDQAG-------HIQLTYFG----QWSEVEPRCSQEAVDCLYSAPEVGGISELTEACDW 462
Cdd:cd14097 112 AVAYLHKNDIVHRDLKLENILVKSSIidnndklNIKVTDFGlsvqKYGLGEDMLQETCGTPIYMAPEVISAHGYSQQCDI 191

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81915001 463 WSYGSLLYELLTGMA--LSQSHPSGFQAHTQLQL----PEW--LSHPAASLLTELLQFEPQRRLGAggggtSRLKSHPF 533
Cdd:cd14097 192 WSIGVIMYMLLCGEPpfVAKSEEKLFEEIRKGDLtftqSVWqsVSDAAKNVLQQLLKVDPAHRMTA-----SELLDNPW 265
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
 394-510 1.41e-04

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: 43.80  E-value: 1.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 394 ALEALHQQG---VLCRDLNPQNLLLDQAGHIQLTYFG-----QWSEVEPRCSQEAVDCLYSAPEVGGISELTEACDWWSY 465
Cdd:cd14066 105 GLEYLHEECpppIIHGDIKSSNILLDEDFEPKLTDFGlarliPPSESVSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSF 184

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 81915001 466 GSLLYELLTGMALSQSHPSGFQAhtqLQLPEWLSHPAASLLTELL 510
Cdd:cd14066 185 GVVLLELLTGKPAVDENRENASR---KDLVEWVESKGKEELEDIL 226
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
 394-475 1.57e-04

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: 43.86  E-value: 1.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 394 ALEALHQQGVLCRDLNPQNLLL---DQAGHIQLTYF--GQWSEVEPRCSQEAVDCL--------YSAPEVggISELTEA- 459
Cdd:cd14173 112 ALDFLHNKGIAHRDLKPENILCehpNQVSPVKICDFdlGSGIKLNSDCSPISTPELltpcgsaeYMAPEV--VEAFNEEa 189

                        90       100
                ....*....|....*....|..
gi 81915001 460 ------CDWWSYGSLLYELLTG 475
Cdd:cd14173 190 siydkrCDLWSLGVILYIMLSG 211
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 379-474 1.58e-04

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: 43.58  E-value: 1.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAV---DCLYSAPEVGGISE 455
Cdd:cd08223  99 LEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDMATTligTPYYMSPELFSNKP 178

                        90
                ....*....|....*....
gi 81915001 456 LTEACDWWSYGSLLYELLT 474
Cdd:cd08223 179 YNHKSDVWALGCCVYEMAT 197
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
 377-477 1.72e-04

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: 43.45  E-value: 1.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 377 WSLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLL-LDQAG-HIQLTYFGQWSEVEPRCSQEAV--DCLYSAPEVGG 452
Cdd:cd14191  95 FELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtKIKLIDFGLARRLENAGSLKVLfgTPEFVAPEVIN 174

                        90       100
                ....*....|....*....|....*
gi 81915001 453 ISELTEACDWWSYGSLLYELLTGMA 477
Cdd:cd14191 175 YEPIGYATDMWSIGVICYILVSGLS 199
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
 388-475 1.73e-04

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: 43.29  E-value: 1.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 388 AAEMLL-ALEALHQQGVLCRDLNPQNLLLDQAGH---IQLTYFGQWSEveprcSQEAVDCL---------YSAPEVGGIS 454
Cdd:cd14087 102 VLQMVLdGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLAST-----RKKGPNCLmkttcgtpeYIAPEILLRK 176

                        90       100
                ....*....|....*....|.
gi 81915001 455 ELTEACDWWSYGSLLYELLTG 475
Cdd:cd14087 177 PYTQSVDMWAVGVIAYILLSG 197
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
 378-534 1.83e-04

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: 43.50  E-value: 1.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCL-----YSAPEVGG 452
Cdd:cd06625  98 ALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRLQTICSSTGMKSVtgtpyWMSPEVIN 177

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 453 ISELTEACDWWSYGSLLYELLT---------GMAlsqshpSGFQAHTQ---LQLPEWLSHPAASLLTELLQFEPQRRLGA 520
Cdd:cd06625 178 GEGYGRKADIWSVGCTVVEMLTtkppwaefePMA------AIFKIATQptnPQLPPHVSEDARDFLSLIFVRNKKQRPSA 251

                       170
                ....*....|....
gi 81915001 521 ggggtSRLKSHPFF 534
Cdd:cd06625 252 -----EELLSHSFV 260
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
 374-534 1.86e-04

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: 43.11  E-value: 1.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 374 RAAWSLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYfgqWSEVEPRCSQEAVDCL--------Y 445
Cdd:cd14023  76 RSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEERTQLRL---ESLEDTHIMKGEDDALsdkhgcpaY 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 446 SAPEV----GGISelTEACDWWSYGSLLYELLTG-MALSQSHPSGFQAHT---QLQLPEWLSHPAASLLTELLQFEPQRR 517
Cdd:cd14023 153 VSPEIlnttGTYS--GKSADVWSLGVMLYTLLVGrYPFHDSDPSALFSKIrrgQFCIPDHVSPKARCLIRSLLRREPSER 230

                       170
                ....*....|....*..
gi 81915001 518 LGAggggtSRLKSHPFF 534
Cdd:cd14023 231 LTA-----PEILLHPWF 242
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
 390-475 2.25e-04

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: 43.26  E-value: 2.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQ-----LTYFGQWSEV--EPRCSQEAVD---------CLYSAPE-VGG 452
Cdd:cd14027  98 EIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKiadlgLASFKMWSKLtkEEHNEQREVDgtakknagtLYYMAPEhLND 177

                        90       100
                ....*....|....*....|....
gi 81915001 453 I-SELTEACDWWSYGSLLYELLTG 475
Cdd:cd14027 178 VnAKPTEKSDVYSFAIVLWAIFAN 201
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
 374-534 2.32e-04

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: 43.10  E-value: 2.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 374 RAAWSLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQaghiqltyfGQWSEVEPRCSQEAV------DCL--- 444
Cdd:cd14022  76 RTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKD---------EERTRVKLESLEDAYilrghdDSLsdk 146

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 445 -----YSAPEV----GGISelTEACDWWSYGSLLYELLTG-MALSQSHPSGFQAHT---QLQLPEWLSHPAASLLTELLQ 511
Cdd:cd14022 147 hgcpaYVSPEIlntsGSYS--GKAADVWSLGVMLYTMLVGrYPFHDIEPSSLFSKIrrgQFNIPETLSPKAKCLIRSILR 224

                       170       180
                ....*....|....*....|....
gi 81915001 512 FEPQRRLgaggggTSR-LKSHPFF 534
Cdd:cd14022 225 REPSERL------TSQeILDHPWF 242
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
 384-538 2.39e-04

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 43.27  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001  384 VKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGH-IQLTYFG--QWSEVEPRC-SQEAVDCLYSAPEV-GGISELTE 458
Cdd:PLN00009 104 IKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNaLKLADFGlaRAFGIPVRTfTHEVVTLWYRAPEIlLGSRHYST 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001  459 ACDWWSYGSLLYELLTGMALSQSHPSGFQAHTQLQL----------------------PEW-----------LSHPAASL 505
Cdd:PLN00009 184 PVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRIlgtpneetwpgvtslpdyksafPKWppkdlatvvptLEPAGVDL 263

                        170       180       190
                 ....*....|....*....|....*....|...
gi 81915001  506 LTELLQFEPQRRLGAggggtSRLKSHPFFSTIQ 538
Cdd:PLN00009 264 LSKMLRLDPSKRITA-----RAALEHEYFKDLG 291
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
 386-474 2.71e-04

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: 42.87  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001   386 QWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG----QWSEVEPRCSQEAVDCL-YSAPEVggISE--LTE 458
Cdd:pfam07714 106 SMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGlsrdIYDDDYYRKRGGGKLPIkWMAPES--LKDgkFTS 183

                          90
                  ....*....|....*.
gi 81915001   459 ACDWWSYGSLLYELLT 474
Cdd:pfam07714 184 KSDVWSFGVLLWEIFT 199
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
 378-534 2.84e-04

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: 42.95  E-value: 2.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGH--IQLTYFGQWSEV---EPRCSQEAVDcLYSAPEVGG 452
Cdd:cd14107  94 VVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTRedIKICDFGFAQEItpsEHQFSKYGSP-EFVAPEIVH 172

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 453 ISELTEACDWWSYGSLLYelltgMALSQSHPSGFQAH--TQLQLPE----W-------LSHPAASLLTELLQFEPQRRLG 519
Cdd:cd14107 173 QEPVSAATDIWALGVIAY-----LSLTCHSPFAGENDraTLLNVAEgvvsWdtpeithLSEDAKDFIKRVLQPDPEKRPS 247

                       170
                ....*....|....*
gi 81915001 520 AggggtSRLKSHPFF 534
Cdd:cd14107 248 A-----SECLSHEWF 257
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
 394-475 3.05e-04

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: 42.60  E-value: 3.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 394 ALEALHQQGVLCRDLNPQNLL-LDQAGH-IQLTYFGQWSEVEPRcsqEAVDCLYS-----APEVGGISELTEACDWWSYG 466
Cdd:cd14103 103 GVQYMHKQGILHLDLKPENILcVSRTGNqIKIIDFGLARKYDPD---KKLKVLFGtpefvAPEVVNYEPISYATDMWSVG 179


                ....*....
gi 81915001 467 SLLYELLTG 475
Cdd:cd14103 180 VICYVLLSG 188
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
 373-517 4.20e-04

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: 42.17  E-value: 4.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 373 GRAAWSLreGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGqWSEVEPRCSQEA-VDCLYSAPEVG 451
Cdd:cd05083  93 GRALVPV--IQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFG-LAKVGSMGVDNSrLPVKWTAPEAL 169

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81915001 452 GISELTEACDWWSYGSLLYELLT-------GMALSQSHPSGFQAHtQLQLPEWLSHPAASLLTELLQFEPQRR 517
Cdd:cd05083 170 KNKKFSSKSDVWSYGVLLWEVFSygrapypKMSVKEVKEAVEKGY-RMEPPEGCPPDVYSIMTSCWEAEPGKR 241
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
 378-533 4.47e-04

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: 42.40  E-value: 4.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAV---DCLYSAPEVGGIS 454
Cdd:cd06637 107 TLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTfigTPYWMAPEVIACD 186

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 455 ELTEAC-----DWWSYGSLLYELLTGM-ALSQSHPSGF------QAHTQLQLPEWLSHPAASLLTELLQFEPQRrlgagg 522
Cdd:cd06637 187 ENPDATydfksDLWSLGITAIEMAEGApPLCDMHPMRAlfliprNPAPRLKSKKWSKKFQSFIESCLVKNHSQR------ 260

                       170
                ....*....|.
gi 81915001 523 GGTSRLKSHPF 533
Cdd:cd06637 261 PSTEQLMKHPF 271
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
 392-506 4.66e-04

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: 42.29  E-value: 4.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 392 LLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRCSQEAVDCLYSAPEVGGISELTEA-----CDWW 463
Cdd:cd06639 138 LLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGvsaQLTSARLRRNTSVGTPFWMAPEVIACEQQYDYsydarCDVW 217

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 81915001 464 SYGsllyelLTGMALSQSHPSGFQAHTQLQLPEWLSHPAASLL 506
Cdd:cd06639 218 SLG------ITAIELADGDPPLFDMHPVKALFKIPRNPPPTLL 254
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
 394-475 5.63e-04

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: 42.02  E-value: 5.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 394 ALEALHQQGVLCRDLNPQNLL---LDQAGHIQLTYFGQWSEVE----------------PRCSQEavdclYSAPEV---- 450
Cdd:cd14090 112 ALDFLHDKGIAHRDLKPENILcesMDKVSPVKICDFDLGSGIKlsstsmtpvttpelltPVGSAE-----YMAPEVvdaf 186

                        90       100
                ....*....|....*....|....*.
gi 81915001 451 -GGISELTEACDWWSYGSLLYELLTG 475
Cdd:cd14090 187 vGEALSYDKRCDLWSLGVILYIMLCG 212
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
 381-475 6.28e-04

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: 41.73  E-value: 6.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEP----RCSQEAVDCLYSAPEVGGISEL 456
Cdd:cd14111  98 EDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPlslrQLGRRTGTLEYMAPEMVKGEPV 177

                        90
                ....*....|....*....
gi 81915001 457 TEACDWWSYGSLLYELLTG 475
Cdd:cd14111 178 GPPADIWSIGVLTYIMLSG 196
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
 381-475 6.67e-04

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: 41.90  E-value: 6.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 381 EGQVKQWAAEMLLALEALHQQ---GVLCRDLNPQNLLLDQAGHIQLTYFGQWSE--VEPRCSQEAV--------DC--LY 445
Cdd:cd13986 105 EDRILHIFLGICRGLKAMHEPelvPYAHRDIKPGNVLLSEDDEPILMDLGSMNParIEIEGRREALalqdwaaeHCtmPY 184

                        90       100       110
                ....*....|....*....|....*....|...
gi 81915001 446 SAPE---VGGISELTEACDWWSYGSLLYELLTG 475
Cdd:cd13986 185 RAPElfdVKSHCTIDEKTDIWSLGCTLYALMYG 217
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 390-520 8.77e-04

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: 41.35  E-value: 8.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLLLDQAGH---IQLTYFGQWSEVEPRCSQEAVdC---LYSAPEVGGISELTEACDWW 463
Cdd:cd14085 106 QILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLSKIVDQQVTMKTV-CgtpGYCAPEILRGCAYGPEVDMW 184

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81915001 464 SYGSLLYELLTGM-------ALSQSHPSGFQAHTQLQLPEW--LSHPAASLLTELLQFEPQRRLGA 520
Cdd:cd14085 185 SVGVITYILLCGFepfyderGDQYMFKRILNCDYDFVSPWWddVSLNAKDLVKKLIVLDPKKRLTT 250
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
 390-478 9.95e-04

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: 41.57  E-value: 9.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG--QWSEVEPRCSQEAVDCLYSAPEVGGISELTEACDWWSYGS 467
Cdd:cd07875 134 QMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGlaRTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGC 213

                        90
                ....*....|.
gi 81915001 468 LLYELLTGMAL 478
Cdd:cd07875 214 IMGEMIKGGVL 224
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
 379-475 1.09e-03

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: 40.89  E-value: 1.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREgQVKQWAAEMLL--------ALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEV---EPRCSQEA-VDCLYS 446
Cdd:cd05059  90 LRE-RRGKFQTEQLLemckdvceAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVlddEYTSSVGTkFPVKWS 168

                        90       100
                ....*....|....*....|....*....
gi 81915001 447 APEVGGISELTEACDWWSYGSLLYELLTG 475
Cdd:cd05059 169 PPEVFMYSKFSSKSDVWSFGVLMWEVFSE 197
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
 387-486 1.10e-03

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: 41.03  E-value: 1.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 387 WAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGqWSEVEPRCSQEAV-------DCLYSAPEVGGISELTEA 459
Cdd:cd05081 113 YSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFG-LAKLLPLDKDYYVvrepgqsPIFWYAPESLSDNIFSRQ 191

                        90       100
                ....*....|....*....|....*..
gi 81915001 460 CDWWSYGSLLYELLTGMALSQSHPSGF 486
Cdd:cd05081 192 SDVWSFGVVLYELFTYCDKSCSPSAEF 218
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
 395-475 1.11e-03

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: 40.84  E-value: 1.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 395 LEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG------QWSeVEPRCSQEAVDCLYSAPEV---GGISELTEACDWWSY 465
Cdd:cd14062 102 MDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGlatvktRWS-GSQQFEQPTGSILWMAPEVirmQDENPYSFQSDVYAF 180

                        90
                ....*....|
gi 81915001 466 GSLLYELLTG 475
Cdd:cd14062 181 GIVLYELLTG 190
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
 378-533 1.19e-03

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: 40.88  E-value: 1.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRCSQEavDCLYS-------- 446
Cdd:cd06631  99 ALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGcakRLCINLSSGSQS--QLLKSmrgtpywm 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 447 APEVGGISELTEACDWWSYGSLLYELLTGM-ALSQSHPSG----FQAHTQL--QLPEWLSHPAASLLTELLQFEPQRRLG 519
Cdd:cd06631 177 APEVINETGHGRKSDIWSIGCTVFEMATGKpPWADMNPMAaifaIGSGRKPvpRLPDKFSPEARDFVHACLTRDQDERPS 256

                       170
                ....*....|....
gi 81915001 520 AggggtSRLKSHPF 533
Cdd:cd06631 257 A-----EQLLKHPF 265
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
 373-471 1.22e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 41.42  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001  373 GRAAWSLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG-------QWSEVEPRCSQEAVDCly 445
Cdd:PHA03211 251 GARLRPLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGaacfargSWSTPFHYGIAGTVDT-- 328

                         90       100
                 ....*....|....*....|....*.
gi 81915001  446 SAPEVGGISELTEACDWWSYGSLLYE 471
Cdd:PHA03211 329 NAPEVLAGDPYTPSVDIWSAGLVIFE 354
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
 388-520 1.48e-03

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. 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 LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 40.72  E-value: 1.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 388 AAEMLLALEALHQQGVLCRDLNPQNLL---LDQAGHI--QLTYFG--QWSEVEPRCSQEAVDClYSAPEVGGISELTEAC 460
Cdd:cd14067 120 AYQIAAGLAYLHKKNIIFCDLKSDNILvwsLDVQEHIniKLSDYGisRQSFHEGALGVEGTPG-YQAPEIRPRIVYDEKV 198

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81915001 461 DWWSYGSLLYELLTGmalsqSHPSgfQAHTQLQLPEWLS--------HPA-------ASLLTELLQFEPQRRLGA 520
Cdd:cd14067 199 DMFSYGMVLYELLSG-----QRPS--LGHHQLQIAKKLSkgirpvlgQPEevqffrlQALMMECWDTKPEKRPLA 266
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
 390-480 1.48e-03

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: 41.17  E-value: 1.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG--QWSEVEPRCSQEAVDCLYSAPEVGGISELTEACDWWSYGS 467
Cdd:cd07876 131 QMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGlaRTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGC 210

                        90
                ....*....|...
gi 81915001 468 LLYELLTGMALSQ 480
Cdd:cd07876 211 IMGELVKGSVIFQ 223
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
 374-500 2.05e-03

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: 40.07  E-value: 2.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 374 RAAWSLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRC-SQEAVDCL-----YSA 447
Cdd:cd06651 103 KAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICmSGTGIRSVtgtpyWMS 182

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 81915001 448 PEVGGISELTEACDWWSYGSLLYELLTGM---ALSQSHPSGFQAHTQLQLPEWLSH 500
Cdd:cd06651 183 PEVISGEGYGRKADVWSLGCTVVEMLTEKppwAEYEAMAAIFKIATQPTNPQLPSH 238
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
 398-477 2.06e-03

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: 40.29  E-value: 2.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 398 LHQQGVLCRDLNPQNLLL-DQAGH-IQLTYFGQWSEVEPRcsqEAVDCLYS-----APEVGGISELTEACDWWSYGSLLY 470
Cdd:cd14190 118 MHQMRVLHLDLKPENILCvNRTGHqVKIIDFGLARRYNPR---EKLKVNFGtpeflSPEVVNYDQVSFPTDMWSMGVITY 194


                ....*..
gi 81915001 471 ELLTGMA 477
Cdd:cd14190 195 MLLSGLS 201
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
 389-521 2.12e-03

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: 40.09  E-value: 2.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 389 AEMLLALEALHQQGVLCRDLNPQNLLLDQAG---HIQLTYFGQWSEVEPRCSQEAV--DCLYSAPEVGGISELTEACDWW 463
Cdd:cd14082 110 TQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFARIIGEKSFRRSVvgTPAYLAPEVLRNKGYNRSLDMW 189

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81915001 464 SYGSLLYELLTGM--------ALSQSHPSGFQAHTQlqlpEW--LSHPAASLLTELLQFEPQRRLGAG 521
Cdd:cd14082 190 SVGVIIYVSLSGTfpfnededINDQIQNAAFMYPPN----PWkeISPDAIDLINNLLQVKMRKRYSVD 253
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
 394-493 2.21e-03

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: 40.01  E-value: 2.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 394 ALEALHQQG--VLCRDLNPQNLLLDQAGHIQLTYFG----QWSEVEPRCSQEAVD--------CLYSAPE---VGGISEL 456
Cdd:cd13985 115 AVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGsattEHYPLERAEEVNIIEeeiqknttPMYRAPEmidLYSKKPI 194

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 81915001 457 TEACDWWSYGSLLYELLTgmalsQSHPsgFQAHTQLQ 493
Cdd:cd13985 195 GEKADIWALGCLLYKLCF-----FKLP--FDESSKLA 224
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
 394-520 2.27e-03

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: 39.98  E-value: 2.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 394 ALEALHQQGVLCRDLNPQNLLL----DQAGHIQLTYFGQWSEVEPRCSQEAVDCLYSAPEVGGISELTEACDWWSYGSLL 469
Cdd:cd14183 116 AIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLATVVDGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVIT 195

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81915001 470 YELLTGMALSQSHPSGFQA--------HTQLQLPEW--LSHPAASLLTELLQFEPQRRLGA 520
Cdd:cd14183 196 YILLCGFPPFRGSGDDQEVlfdqilmgQVDFPSPYWdnVSDSAKELITMMLQVDVDQRYSA 256
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
 378-475 2.36e-03

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: 39.99  E-value: 2.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQN-LLLDQAG---HIQLTYFGQWSEVEprCSQEAVDCL----YSAPE 449
Cdd:cd14195 104 SLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENiMLLDKNVpnpRIKLIDFGIAHKIE--AGNEFKNIFgtpeFVAPE 181

                        90       100
                ....*....|....*....|....*.
gi 81915001 450 VGGISELTEACDWWSYGSLLYELLTG 475
Cdd:cd14195 182 IVNYEPLGLEADMWSIGVITYILLSG 207
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
 384-475 2.41e-03

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: 40.03  E-value: 2.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 384 VKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQA-GHIQLTYFGqWSEVEPRCSQEAVDCL-YSAPE----VGGISEL- 456
Cdd:cd13993 109 IKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCDFG-LATTEKISMDFGVGSEfYMAPEcfdeVGRSLKGy 187

                        90       100
                ....*....|....*....|
gi 81915001 457 -TEACDWWSYGSLLYELLTG 475
Cdd:cd13993 188 pCAAGDIWSLGIILLNLTFG 207
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
 385-517 2.41e-03

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: 39.86  E-value: 2.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 385 KQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---------------QWSEVEPRCSQEAVDCLYSAPE 449
Cdd:cd14048 121 LNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGlvtamdqgepeqtvlTPMPAYAKHTGQVGTRLYMSPE 200

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81915001 450 VGGISELTEACDWWSYGSLLYELLTGMALSQSHPSGFQAHTQLQLPEWL--SHPAASLLT-ELLQFEPQRR 517
Cdd:cd14048 201 QIHGNQYSEKVDIFALGLILFELIYSFSTQMERIRTLTDVRKLKFPALFtnKYPEERDMVqQMLSPSPSER 271
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
 383-478 2.50e-03

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: 39.98  E-value: 2.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 383 QVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG---QWSEVEPRCSQEAVDC-LYSAPEVGGISELTE 458
Cdd:cd07848 101 KVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGfarNLSEGSNANYTEYVATrWYRSPELLLGAPYGK 180

                        90       100
                ....*....|....*....|
gi 81915001 459 ACDWWSYGSLLYELLTGMAL 478
Cdd:cd07848 181 AVDMWSVGCILGELSDGQPL 200
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
 379-478 2.52e-03

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: 40.35  E-value: 2.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCLYSAPEVggI---SE 455
Cdd:cd07851 115 LSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEI--MlnwMH 192

                        90       100
                ....*....|....*....|...
gi 81915001 456 LTEACDWWSYGSLLYELLTGMAL 478
Cdd:cd07851 193 YNQTVDIWSVGCIMAELLTGKTL 215
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
 377-477 2.73e-03

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: 39.90  E-value: 2.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 377 WSLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLL--DQAGHIQLTYFGQWSEVEPRcsqEAVDCLYS-----APE 449
Cdd:cd14193  97 YNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCvsREANQVKIIDFGLARRYKPR---EKLRVNFGtpeflAPE 173

                        90       100
                ....*....|....*....|....*...
gi 81915001 450 VGGISELTEACDWWSYGSLLYELLTGMA 477
Cdd:cd14193 174 VVNYEFVSFPTDMWSLGVIAYMLLSGLS 201
PK_MviN-like cd13973
Pseudokinase domain of the peptidoglycan biosynthetic protein MviN; The pseudokinase domain ...
 365-475 2.99e-03

Pseudokinase domain of the peptidoglycan biosynthetic protein MviN; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This family is composed of the mycobacterial protein MviN and similar proteins. MviN is an integral membrane protein that is essential for growth and is required for cell wall integrity and peptidogylcan (PG) biosynthesis. It comprises of 14 predicted transmembrane (TM) helices at the N-terminus, followed by an intracellular pseudokinase domain linked through a single TM helix to a carbohydrate binding extracellular domain. Phosphorylation of the MviN pseudokinase domain by the PG-sensitive serine/threonine protein kinase PknB recruits a forkhead associated (FHA) domain protein FhaA, which modulates local PG synthesis at cell poles and the septum. The MviN pseudokinase forms a canonical receptor kinase dimer.


Pssm-ID: 270875 [Multi-domain]  Cd Length: 236  Bit Score: 39.62  E-value: 2.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 365 ANRASLGSGRAAWSLREgqvkqwAAEmllALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGqwseVEPrcsqeavdcl 444
Cdd:cd13973  92 AESGPLDPEAAARAVAE------LAE---ALAAAHRAGLALGIDHPDRVRISSDGRVVLAFPA----VLA---------- 148

                        90       100       110
                ....*....|....*....|....*....|.
gi 81915001 445 ysapevggisELTEACDWWSYGSLLYELLTG 475
Cdd:cd13973 149 ----------ALSPATDVRALGALLYALLTG 169
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
 366-474 3.13e-03

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. 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 CDK8 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 40.04  E-value: 3.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 366 NRASLGSGRAAwSLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLL----DQAGHIQLTYFGQW----SEVEPRCS 437
Cdd:cd07868 109 HRASKANKKPV-QLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFArlfnSPLKPLAD 187

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 81915001 438 QE--AVDCLYSAPE-VGGISELTEACDWWSYGSLLYELLT 474
Cdd:cd07868 188 LDpvVVTFWYRAPElLLGARHYTKAIDIWAIGCIFAELLT 227
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
 371-517 3.23e-03

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: 39.83  E-value: 3.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 371 GSGRAAWSLREGQVKQWAAEMLLALEALHQQ-GVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVDCL-YSAP 448
Cdd:cd06622  91 AGGVATEGIPEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLVASLAKTNIGCQsYMAP 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 449 E---VGGISE---LTEACDWWSYGSLLYELLTGmalsqSHPSGFQAHT----QLQ---------LPEWLSHPAASLLTEL 509
Cdd:cd06622 171 ErikSGGPNQnptYTVQSDVWSLGLSILEMALG-----RYPYPPETYAnifaQLSaivdgdpptLPSGYSDDAQDFVAKC 245


                ....*...
gi 81915001 510 LQFEPQRR 517
Cdd:cd06622 246 LNKIPNRR 253
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
 387-474 3.32e-03

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 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: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 39.66  E-value: 3.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 387 WAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG-----QWSEVEPRCSQEAVDCLYSAPEVGGISELTEACD 461
Cdd:cd05110 114 WCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGlarllEGDEKEYNADGGKMPIKWMALECIHYRKFTHQSD 193

                        90
                ....*....|...
gi 81915001 462 WWSYGSLLYELLT 474
Cdd:cd05110 194 VWSYGVTIWELMT 206
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
 390-473 4.25e-03

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: 39.41  E-value: 4.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 390 EMLLALEALHQQGVLCRDLNPQNLLLD-QAGHIQLTYFG-----------QWSEVEPRCSQEAVD----CLYSAPEVGGI 453
Cdd:cd14049 128 QLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHVRIGDFGlacpdilqdgnDSTTMSRLNGLTHTSgvgtCLYAAPEQLEG 207

                        90       100
                ....*....|....*....|
gi 81915001 454 SELTEACDWWSYGSLLYELL 473
Cdd:cd14049 208 SHYDFKSDMYSIGVILLELF 227
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
 383-482 4.28e-03

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: 39.24  E-value: 4.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 383 QVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFG------QWSEVEpRCSQEAVDCLYSAPEVGGISE- 455
Cdd:cd14149 109 QLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGlatvksRWSGSQ-QVEQPTGSILWMAPEVIRMQDn 187

                        90       100
                ....*....|....*....|....*....
gi 81915001 456 --LTEACDWWSYGSLLYELLTGmALSQSH 482
Cdd:cd14149 188 npFSFQSDVYSYGIVLYELMTG-ELPYSH 215
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
 379-517 4.44e-03

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: 39.14  E-value: 4.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQwseveprcSQEAVDCLYS------------ 446
Cdd:cd05084  92 LKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGM--------SREEEDGVYAatggmkqipvkw 163

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81915001 447 -APEVGGISELTEACDWWSYGSLLYELLTGMALSQSHPSGFQAH------TQLQLPEWLSHPAASLLTELLQFEPQRR 517
Cdd:cd05084 164 tAPEALNYGRYSSESDVWSFGILLWETFSLGAVPYANLSNQQTReaveqgVRLPCPENCPDEVYRLMEQCWEYDPRKR 241
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
 378-483 4.57e-03

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: 39.22  E-value: 4.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAV---DCLYSAPEVGGIS 454
Cdd:cd06636 117 ALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTfigTPYWMAPEVIACD 196

                        90       100       110
                ....*....|....*....|....*....|....*
gi 81915001 455 ELTEA-----CDWWSYGSLLYELLTGM-ALSQSHP 483
Cdd:cd06636 197 ENPDAtydyrSDIWSLGITAIEMAEGApPLCDMHP 231
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
 384-475 5.37e-03

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: 39.13  E-value: 5.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 384 VKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGH-IQLTYFGQWSEVEprcSQEAVDCL----YSAPEVggISELT- 457
Cdd:cd14135 107 VRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNtLKLCDFGSASDIG---ENEITPYLvsrfYRAPEI--ILGLPy 181

                        90
                ....*....|....*....
gi 81915001 458 -EACDWWSYGSLLYELLTG 475
Cdd:cd14135 182 dYPIDMWSVGCTLYELYTG 200
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
 391-473 5.76e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 39.06  E-value: 5.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001  391 MLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVE-----PRCSQEAVDCLYSAPEVGGISELTEACDWWSY 465
Cdd:PHA03207 194 LLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACKLDahpdtPQCYGWSGTLETNSPELLALDPYCAKTDIWSA 273


                 ....*...
gi 81915001  466 GSLLYELL 473
Cdd:PHA03207 274 GLVLFEMS 281
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
 369-474 6.37e-03

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 38.59  E-value: 6.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 369 SLGSGRAAWSLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPrcsqEAVDCL---- 444
Cdd:cd05043 103 RLSEANNPQALSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALSRDLFP----MDYHCLgdne 178

                        90       100       110
                ....*....|....*....|....*....|....*
gi 81915001 445 -----YSAPEVGGISELTEACDWWSYGSLLYELLT 474
Cdd:cd05043 179 nrpikWMSLESLVNKEYSSASDVWSFGVLLWELMT 213
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
 383-474 7.71e-03

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: 38.37  E-value: 7.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 383 QVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQEAVD------CLYSAPEVGGISEL 456
Cdd:cd05079 110 QQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKddldspVFWYAPECLIQSKF 189

                        90
                ....*....|....*...
gi 81915001 457 TEACDWWSYGSLLYELLT 474
Cdd:cd05079 190 YIASDVWSFGVTLYELLT 207
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
 378-477 9.02e-03

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: 38.24  E-value: 9.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 378 SLREGQVKQWAAEMLLALEALHQQGVLCRDLNPQNLLLDQAG----HIQLTYFGQWSEVEPrcSQEAVDCL----YSAPE 449
Cdd:cd14105 104 SLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNvpipRIKLIDFGLAHKIED--GNEFKNIFgtpeFVAPE 181

                        90       100
                ....*....|....*....|....*...
gi 81915001 450 VGGISELTEACDWWSYGSLLYELLTGMA 477
Cdd:cd14105 182 IVNYEPLGLEADMWSIGVITYILLSGAS 209
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 47-96 9.23e-03

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT domain sub-family is found in the AAA protein spastin, a probable ATPase involved in the assembly or function of nuclear protein complexes; spastins might also be involved in microtubule dynamics. The molecular function of the MIT domain is unclear.


Pssm-ID: 239142  Cd Length: 79  Bit Score: 35.33  E-value: 9.23e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 81915001  47 RDYLVDAATQIHLALERDVSEDYEAAFNHYQNGVDVLLRGVHVDPNKERR 96
Cdd:cd02679   2 RGYYKQAFEEISKALRADEWGDKEQALAHYRKGLRELEEGIAVPVPSAGV 51
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
 406-475 9.25e-03

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: 38.11  E-value: 9.25e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81915001 406 RDLNPQNLLLDQAGHIQLTYFGQWSEVEPRCSQ-EAVDCL-YSAPEVGGISELTEA----CDWWSYGSLLYELLTG 475
Cdd:cd06616 134 RDVKPSNILLDRNGNIKLCDFGISGQLVDSIAKtRDAGCRpYMAPERIDPSASRDGydvrSDVWSLGITLYEVATG 209
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
 379-474 9.59e-03

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: 37.92  E-value: 9.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81915001 379 LREGQvKQWAAEMLL--------ALEALHQQGVLCRDLNPQNLLLDQAGHIQLTYFGQWSEV---EPRCSQEA-VDCLYS 446
Cdd:cd05114  90 LRQRR-GKLSRDMLLsmcqdvceGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVlddQYTSSSGAkFPVKWS 168

                        90       100
                ....*....|....*....|....*...
gi 81915001 447 APEVGGISELTEACDWWSYGSLLYELLT 474
Cdd:cd05114 169 PPEVFNYSKFSSKSDVWSFGVLMWEVFT 196
 
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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