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Conserved domains on  [gi|189011594|ref|NP_001121027|]
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interleukin-1 receptor-associated kinase 1 [Rattus norvegicus]

Protein Classification

interleukin-1 receptor-associated kinase 1( domain architecture ID 10172023)

interleukin-1 receptor-associated kinase 1 (IRAK1) is a serine/threonine-protein kinase that catalyzes 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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
218-521 0e+00

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd14159:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 296  Bit Score: 530.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLE 297
Cdd:cd14159    1 IGEGGFGCVYQAVMRNTEYAVKRLKEDSELDWSVVKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLPNGSLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 298 DQLHLQTqACSPLSWPQRLDILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAgANPSQSST 377
Cdd:cd14159   81 DRLHCQV-SCPCLSWSQRLHVLLGTARAIQYLHSDSPSLIHGDVKSSNILLDAALNPKLGDFGLARFSRRP-KQPGMSST 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 378 VARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGA-KTKYLKDLIEDEAEEVGVTLKstqptl 456
Cdd:cd14159  159 LARTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAMEVDSCsPTKYLKDLVKEEEEAQHTPTT------ 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 457 wMGVATDAWTAPIAAQIYKKHLDSRPGPCPPQLGLALAQLACCCMHRRAKKRPPMTQVYKRLEGL 521
Cdd:cd14159  233 -MTHSAEAQAAQLATSICQKHLDPQAGPCPPELGIEISQLACRCLHRRAKKRPPMTEVFQELERL 296
Death_IRAK1 cd08794
Death domain of Interleukin 1 Receptor Associated Kinase-1; Death Domain (DD) of Interleukin-1 ...
17-100 8.33e-49

Death domain of Interleukin 1 Receptor Associated Kinase-1; Death Domain (DD) of Interleukin-1 Receptor-Associated Kinase 1 (IRAK1). IRAKs are essential components of innate immunity and inflammation in mammals and other vertebrates. They are involved in signal transduction pathways involving IL-1 and IL-18 receptors, Toll-like receptors, nuclear factor-kappaB (NF-kB), and mitogen-activated protein kinases (MAPKs). IRAKs contain an N-terminal DD domain and a C-terminal kinase domain. IRAK1 is an active kinase and also plays adaptor functions. It binds to the MyD88-IRAK4 complex via its DD, which facilitates its phosphorylation by IRAK4, activating it for further auto-phosphorylation. Hyper-phosphorylated IRAK1 forms a cytosolic complex with TRAF6, leading to the activation of NF-kB and MAPK pathways. IRAK1 is involved in autoimmunity and may be associated with lupus pathogenesis. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260061  Cd Length: 84  Bit Score: 165.73  E-value: 8.33e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594  17 HFLYEVPPWVMCRFYKVMDALEPADWCQFAALIVRDQTELRLCERSEQRTASVLWPWINRNARVADLVHILTHLQLLRAR 96
Cdd:cd08794    1 EFLYELPPSVMWRFCLVMDSLSDLDWTRFASEIIKDQTELRLLERSGRRTDWVMWRWENRNGRVGELVDILERLQLLRPR 80

                 ....
gi 189011594  97 DIIT 100
Cdd:cd08794   81 DVIL 84
 
Name Accession Description Interval E-value
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
218-521 0e+00

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 530.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLE 297
Cdd:cd14159    1 IGEGGFGCVYQAVMRNTEYAVKRLKEDSELDWSVVKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLPNGSLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 298 DQLHLQTqACSPLSWPQRLDILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAgANPSQSST 377
Cdd:cd14159   81 DRLHCQV-SCPCLSWSQRLHVLLGTARAIQYLHSDSPSLIHGDVKSSNILLDAALNPKLGDFGLARFSRRP-KQPGMSST 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 378 VARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGA-KTKYLKDLIEDEAEEVGVTLKstqptl 456
Cdd:cd14159  159 LARTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAMEVDSCsPTKYLKDLVKEEEEAQHTPTT------ 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 457 wMGVATDAWTAPIAAQIYKKHLDSRPGPCPPQLGLALAQLACCCMHRRAKKRPPMTQVYKRLEGL 521
Cdd:cd14159  233 -MTHSAEAQAAQLATSICQKHLDPQAGPCPPELGIEISQLACRCLHRRAKKRPPMTEVFQELERL 296
Death_IRAK1 cd08794
Death domain of Interleukin 1 Receptor Associated Kinase-1; Death Domain (DD) of Interleukin-1 ...
17-100 8.33e-49

Death domain of Interleukin 1 Receptor Associated Kinase-1; Death Domain (DD) of Interleukin-1 Receptor-Associated Kinase 1 (IRAK1). IRAKs are essential components of innate immunity and inflammation in mammals and other vertebrates. They are involved in signal transduction pathways involving IL-1 and IL-18 receptors, Toll-like receptors, nuclear factor-kappaB (NF-kB), and mitogen-activated protein kinases (MAPKs). IRAKs contain an N-terminal DD domain and a C-terminal kinase domain. IRAK1 is an active kinase and also plays adaptor functions. It binds to the MyD88-IRAK4 complex via its DD, which facilitates its phosphorylation by IRAK4, activating it for further auto-phosphorylation. Hyper-phosphorylated IRAK1 forms a cytosolic complex with TRAF6, leading to the activation of NF-kB and MAPK pathways. IRAK1 is involved in autoimmunity and may be associated with lupus pathogenesis. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260061  Cd Length: 84  Bit Score: 165.73  E-value: 8.33e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594  17 HFLYEVPPWVMCRFYKVMDALEPADWCQFAALIVRDQTELRLCERSEQRTASVLWPWINRNARVADLVHILTHLQLLRAR 96
Cdd:cd08794    1 EFLYELPPSVMWRFCLVMDSLSDLDWTRFASEIIKDQTELRLLERSGRRTDWVMWRWENRNGRVGELVDILERLQLLRPR 80

                 ....
gi 189011594  97 DIIT 100
Cdd:cd08794   81 DVIL 84
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
218-518 7.55e-38

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


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 141.53  E-value: 7.55e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594   218 IGEGGFGCVYRAVMRNTTY------AVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFL 291
Cdd:smart00221   7 LGEGAFGEVYKGTLKGKGDgkevevAVKTLKEDASEQ---QIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVMEYM 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594   292 PNGSLEDqlHLQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRfagan 371
Cdd:smart00221  84 PGGDLLD--YLRKNRPKELSLSDLLSFALQIARGMEYLE--SKNFIHRDLAARNCLVGENLVVKISDFGLSRDLY----- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594   372 psqSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLagqravrTQGAKTKYLKDLIEdeaeevgvtlks 451
Cdd:smart00221 155 ---DDDYYKVKGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIF-------TLGEEPYPGMSNAE------------ 212
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594   452 tqptlwmgvatdawtapIAAQIYKKHLDSRPGPCPPqlglALAQLACCCMHRRAKKRPPMTQVYKRL 518
Cdd:smart00221 213 -----------------VLEYLKKGYRLPKPPNCPP----ELYKLMLQCWAEDPEDRPTFSELVEIL 258
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
217-594 2.36e-37

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 145.93  E-value: 2.36e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEWTVVKQsFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNG 294
Cdd:COG0515   14 LLGRGGMGVVYLARDLRLgrPVALKVLRPELAADPEARER-FRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEGE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEDQLHLQtqacSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFSRfaganpsq 374
Cdd:COG0515   93 SLADLLRRR----GPLPPAEALRILAQLAEALAAAHAAG--IVHRDIKPANILLTPDGRVKLIDFGIARALG-------- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 375 SSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRavrtqgaktkylkdliedeaeevgvtlkstqp 454
Cdd:COG0515  159 GATLTQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRP-------------------------------- 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 455 tlwmgvatdAWTAPIAAQIYKKHLDSRPGPCP---PQLGLALAQLACCCMHRRAKKRPP-MTQVYKRLEGLQAVPPWKLE 530
Cdd:COG0515  207 ---------PFDGDSPAELLRAHLREPPPPPSelrPDLPPALDAIVLRALAKDPEERYQsAAELAAALRAVLRSLAAAAA 277
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594 531 VAGHGSPSPQENSYMSTTGSAQSGDEPWQPLVVTTRAPAQAAQQLQRSPNQPVESDESVPGLSA 594
Cdd:COG0515  278 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAAAAA 341
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
217-518 3.66e-35

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: 134.16  E-value: 3.66e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594  217 RIGEGGFGCVYRAVMR------NTTYAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGF 290
Cdd:pfam07714   6 KLGEGAFGEVYKGTLKgegentKIKVAVKTLKEGADEE---EREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594  291 LPNGSLEDQLHLQTQacsPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFsrfagA 370
Cdd:pfam07714  83 MPGGDLLDFLRKHKR---KLTLKDLLSMALQIAKGMEYLE--SKNFVHRDLAARNCLVSENLVVKISDFGLSRD-----I 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594  371 NPSQSSTVARTCTVRgtLAYLPEEYIKTGRLAVDTDTFSFGVVILETLagqravrTQGAKTKYLKDLIEdeaeevgvtlk 450
Cdd:pfam07714 153 YDDDYYRKRGGGKLP--IKWMAPESLKDGKFTSKSDVWSFGVLLWEIF-------TLGEQPYPGMSNEE----------- 212
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594  451 stqptlwmgvatdawtapIAAQIYKKHLDSRPGPCPPQlglaLAQLACCCMHRRAKKRPPMTQVYKRL 518
Cdd:pfam07714 213 ------------------VLEFLEDGYRLPQPENCPDE----LYDLMKQCWAYDPEDRPTFSELVEDL 258
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
159-421 1.59e-14

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 75.63  E-value: 1.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 159 LQVPLSD-SLGPPLQSSAPSSIKPSPESPVSGLQRARPSPfcwPFCEISQGTcnfseelRIGEGGFGCVYRAVMRNTT-- 235
Cdd:PLN00034  32 LPLPQRDpSLAVPLPLPPPSSSSSSSSSSSASGSAPSAAK---SLSELERVN-------RIGSGAGGTVYKVIHRPTGrl 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 236 YAVKRLKEEADlewTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLEDQLHLQTQACSPLSwpqr 315
Cdd:PLN00034 102 YALKVIYGNHE---DTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLEGTHIADEQFLADVA---- 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 316 LDILLGtaraIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFSRfAGANPSQSSTvartctvrGTLAYLPEEY 395
Cdd:PLN00034 175 RQILSG----IAYLHRRH--IVHRDIKPSNLLINSAKNVKIADFGVSRILA-QTMDPCNSSV--------GTIAYMSPER 239
                        250       260       270
                 ....*....|....*....|....*....|.
gi 189011594 396 IKT----GRL-AVDTDTFSFGVVILETLAGQ 421
Cdd:PLN00034 240 INTdlnhGAYdGYAGDIWSLGVSILEFYLGR 270
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
217-421 5.68e-12

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 68.67  E-value: 5.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAV-MR-NTTYAVKRLKeeADLewtVVKQSFLTeveqlsRFR----------HPNIV---DfAGycAES 281
Cdd:NF033483  14 RIGRGGMAEVYLAKdTRlDRDVAVKVLR--PDL---ARDPEFVA------RFRreaqsaaslsHPNIVsvyD-VG--EDG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 282 GFYCLVYGFLPNGSLEDQLHLQtqacSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGL 361
Cdd:NF033483  80 GIPYIVMEYVDGRTLKDYIREH----GPLSPEEAVEIMIQILSALEHAHRNG--IVHRDIKPQNILITKDGRVKVTDFGI 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189011594 362 AR-FSrfaganpsqSSTVARTCTVRGTLAYLPEEYIKTGrlAVD--TDTFSFGVVILETLAGQ 421
Cdd:NF033483 154 ARaLS---------STTMTQTNSVLGTVHYLSPEQARGG--TVDarSDIYSLGIVLYEMLTGR 205
Death pfam00531
Death domain;
27-102 8.59e-12

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 61.61  E-value: 8.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594   27 MCRFYKVMDALEP--ADWCQFAALIVRDQTELRLCERSEQRTAS----VLWPWINR---NARVADLVHILTHLQLLRARD 97
Cdd:pfam00531   1 RKQLDRLLDPPPPlgKDWRELARKLGLSENEIDEIESENPRLRSqtyeLLRLWEQRegkNATVGTLLEALRKLGRRDAAE 80

                  ....*
gi 189011594   98 IITAW 102
Cdd:pfam00531  81 KIQSI 85
 
Name Accession Description Interval E-value
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
218-521 0e+00

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 530.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLE 297
Cdd:cd14159    1 IGEGGFGCVYQAVMRNTEYAVKRLKEDSELDWSVVKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLPNGSLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 298 DQLHLQTqACSPLSWPQRLDILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAgANPSQSST 377
Cdd:cd14159   81 DRLHCQV-SCPCLSWSQRLHVLLGTARAIQYLHSDSPSLIHGDVKSSNILLDAALNPKLGDFGLARFSRRP-KQPGMSST 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 378 VARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGA-KTKYLKDLIEDEAEEVGVTLKstqptl 456
Cdd:cd14159  159 LARTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAMEVDSCsPTKYLKDLVKEEEEAQHTPTT------ 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 457 wMGVATDAWTAPIAAQIYKKHLDSRPGPCPPQLGLALAQLACCCMHRRAKKRPPMTQVYKRLEGL 521
Cdd:cd14159  233 -MTHSAEAQAAQLATSICQKHLDPQAGPCPPELGIEISQLACRCLHRRAKKRPPMTEVFQELERL 296
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
218-521 1.79e-101

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: 311.90  E-value: 1.79e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMR-NTTYAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSL 296
Cdd:cd14066    1 IGSGGFGTVYKGVLEnGTVVAVKRLNEMNCAA---SKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 297 EDQLHLQTqACSPLSWPQRLDILLGTARAIQFLHQD-SPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAGANPSQS 375
Cdd:cd14066   78 EDRLHCHK-GSPPLPWPQRLKIAKGIARGLEYLHEEcPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSESVSKTS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 376 StvartctVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRT--QGAKTKYLKDLIEDEAEEvgvtlkstq 453
Cdd:cd14066  157 A-------VKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDEnrENASRKDLVEWVESKGKE--------- 220
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189011594 454 ptlwmgvatdawtapiaaqIYKKHLDSRPGPCPPQ---LGLALAQLACCCMHRRAKKRPPMTQVYKRLEGL 521
Cdd:cd14066  221 -------------------ELEDILDKRLVDDDGVeeeEVEALLRLALLCTRSDPSLRPSMKEVVQMLEKL 272
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
218-521 4.05e-74

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 240.94  E-value: 4.05e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLE 297
Cdd:cd14160    1 IGEGEIFEVYRVRIGNRSYAVKLFKQEKKMQWKKHWKRFLSELEVLLLFQHPNILELAAYFTETEKFCLVYPYMQNGTLF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 298 DQLHlQTQACSPLSWPQRLDILLGTARAIQFLHQDSP-SLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAganPSQSS 376
Cdd:cd14160   81 DRLQ-CHGVTKPLSWHERINILIGIAKAIHYLHNSQPcTVICGNISSANILLDDQMQPKLTDFALAHFRPHL---EDQSC 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 377 TVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRaVRTQGAKTKYLKDLIEDEAEEVGVtlkstqptl 456
Cdd:cd14160  157 TINMTTALHKHLWYMPEEYIRQGKLSVKTDVYSFGIVIMEVLTGCK-VVLDDPKHLQLRDLLHELMEKRGL--------- 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 457 wmgvatDAWTapiaaqiykKHLDSRPGPCPPQLGLALAQLACCCMHRRAKKRPPMTQVYKRLEGL 521
Cdd:cd14160  227 ------DSCL---------SFLDLKFPPCPRNFSAKLFRLAGRCTATKAKLRPDMDEVLQRLEST 276
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
218-519 1.50e-63

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK2 plays a role in mediating NFkB activation by TLR3, TLR4, and TLR8. It is specifically targeted by the viral protein A52, which is important for virulence, to inhibit all IL-1/TLR pathways, indicating that IRAK2 has a predominant role in NFkB activation. It is redundant with IRAK1 in early signaling but is critical for late and sustained activation. The IRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271059 [Multi-domain]  Cd Length: 289  Bit Score: 213.16  E-value: 1.50e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLE 297
Cdd:cd14157    1 ISEGTFADIYKGYRHGKQYVIKRLKETECESPKSTERFFQTEVQICFRCCHPNILPLLGFCVESDCHCLIYPYMPNGSLQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 298 DQLHLQTQAcSPLSWPQRLDILLGTARAIQFLHQDspSLIHGDIKSSNVLLDERLMPKLGDFGLarfsRFAGANPSQSST 377
Cdd:cd14157   81 DRLQQQGGS-HPLPWEQRLSISLGLLKAVQHLHNF--GILHGNIKSSNVLLDGNLLPKLGHSGL----RLCPVDKKSVYT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 378 VARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVrTQGAKTKYLKDLIEDEAEEVGVTLKSTQPTLw 457
Cdd:cd14157  154 MMKTKVLQISLAYLPEDFVRHGQLTEKVDIFSCGVVLAEILTGIKAM-DEFRSPVYLKDLLLEEIQRAKEGSQSKHKSP- 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189011594 458 mgvatdawTAPIAAQIYKKHLDSRPGPCPPQLGLALAQLACCCMHrraKKRPPMTQVYKRLE 519
Cdd:cd14157  232 --------ESLAAKEICSKYLDKRAGLLPENVAFSLAFAACLCLR---KKNPLLPEVYEIVE 282
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
202-521 1.35e-57

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 196.95  E-value: 1.35e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 202 FCEISQGTCNFSEE------LRIGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFA 275
Cdd:cd14158    1 FHELKNMTNNFDERpisvggNKLGEGGFGVVFKGYINDKNVAVKKLAAMVDISTEDLTKQFEQEIQVMAKCQHENLVELL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 276 GYCAESGFYCLVYGFLPNGSLEDQLhlqtqACS----PLSWPQRLDILLGTARAIQFLHQDspSLIHGDIKSSNVLLDER 351
Cdd:cd14158   81 GYSCDGPQLCLVYTYMPNGSLLDRL-----ACLndtpPLSWHMRCKIAQGTANGINYLHEN--NHIHRDIKSANILLDET 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 352 LMPKLGDFGLARfsrfagANPSQSSTVaRTCTVRGTLAYL-PEEYikTGRLAVDTDTFSFGVVILETLAGQRAVrTQGAK 430
Cdd:cd14158  154 FVPKISDFGLAR------ASEKFSQTI-MTERIVGTTAYMaPEAL--RGEITPKSDIFSFGVVLLEIITGLPPV-DENRD 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 431 TKYLKDLIEDEAEEVgvtlkstqptlwmgvatdawtapiaAQIYkKHLDSRPGPCPPQLGLALAQLACCCMHRRAKKRPP 510
Cdd:cd14158  224 PQLLLDIKEEIEDEE-------------------------KTIE-DYVDKKMGDWDSTSIEAMYSVASQCLNDKKNRRPD 277
                        330
                 ....*....|.
gi 189011594 511 MTQVYKRLEGL 521
Cdd:cd14158  278 IAKVQQLLQEL 288
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
218-518 2.92e-55

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: 189.29  E-value: 2.92e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLE 297
Cdd:cd13999    1 IGSGSFGEVYKGKWRGTDVAIKKLKVEDDNDEL--LKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 298 DQLHLQTqacSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFsrfaganpsQSST 377
Cdd:cd13999   79 DLLHKKK---IPLSWSLRLKIALDIARGMNYLH--SPPIIHRDLKSLNILLDENFTVKIADFGLSRI---------KNST 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 378 VARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVrtqgaktkylkDLIEDEAEEVGVTLKSTQPTLw 457
Cdd:cd13999  145 TEKMTGVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPF-----------KELSPIQIAAAVVQKGLRPPI- 212
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189011594 458 mgvatdawtapiaaqiykkhldsrPGPCPPQlglaLAQLACCCMHRRAKKRPPMTQVYKRL 518
Cdd:cd13999  213 ------------------------PPDCPPE----LSKLIKRCWNEDPEKRPSFSEIVKRL 245
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
218-520 1.77e-52

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 182.70  E-value: 1.77e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRN-TTYAVKRLKEEADLEWtvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSL 296
Cdd:cd14664    1 IGRGGAGTVYKGVMPNgTLVAVKRLKGEGTQGG---DHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 297 EDQLHLQTQACSPLSWPQRLDILLGTARAIQFLHQD-SPSLIHGDIKSSNVLLDERLMPKLGDFGLARFsrfagANPSQS 375
Cdd:cd14664   78 GELLHSRPESQPPLDWETRQRIALGSARGLAYLHHDcSPLIIHRDVKSNNILLDEEFEAHVADFGLAKL-----MDDKDS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 376 STVArtcTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAK-----TKYLKDLIEDEAEEVGVtlk 450
Cdd:cd14664  153 HVMS---SVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPFDEAFLDdgvdiVDWVRGLLEEKKVEALV--- 226
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 451 stQPTLwMGVATDawtapiaaqiykkhldsrpgpcppQLGLALAQLACCCMHRRAKKRPPMTQVYKRLEG 520
Cdd:cd14664  227 --DPDL-QGVYKL------------------------EEVEQVFQVALLCTQSSPMERPTMREVVRMLEG 269
Death_IRAK1 cd08794
Death domain of Interleukin 1 Receptor Associated Kinase-1; Death Domain (DD) of Interleukin-1 ...
17-100 8.33e-49

Death domain of Interleukin 1 Receptor Associated Kinase-1; Death Domain (DD) of Interleukin-1 Receptor-Associated Kinase 1 (IRAK1). IRAKs are essential components of innate immunity and inflammation in mammals and other vertebrates. They are involved in signal transduction pathways involving IL-1 and IL-18 receptors, Toll-like receptors, nuclear factor-kappaB (NF-kB), and mitogen-activated protein kinases (MAPKs). IRAKs contain an N-terminal DD domain and a C-terminal kinase domain. IRAK1 is an active kinase and also plays adaptor functions. It binds to the MyD88-IRAK4 complex via its DD, which facilitates its phosphorylation by IRAK4, activating it for further auto-phosphorylation. Hyper-phosphorylated IRAK1 forms a cytosolic complex with TRAF6, leading to the activation of NF-kB and MAPK pathways. IRAK1 is involved in autoimmunity and may be associated with lupus pathogenesis. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260061  Cd Length: 84  Bit Score: 165.73  E-value: 8.33e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594  17 HFLYEVPPWVMCRFYKVMDALEPADWCQFAALIVRDQTELRLCERSEQRTASVLWPWINRNARVADLVHILTHLQLLRAR 96
Cdd:cd08794    1 EFLYELPPSVMWRFCLVMDSLSDLDWTRFASEIIKDQTELRLLERSGRRTDWVMWRWENRNGRVGELVDILERLQLLRPR 80

                 ....
gi 189011594  97 DIIT 100
Cdd:cd08794   81 DVIL 84
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
218-416 6.78e-43

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: 154.35  E-value: 6.78e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT--YAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd00180    1 LGKGSFGKVYKARDKETGkkVAVKVIPKEKLKK---LLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLHLQTQacsPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFSrfaganpSQS 375
Cdd:cd00180   78 LKDLLKENKG---PLSEEEALSILRQLLSALEYLHSNG--IIHRDLKPENILLDSDGTVKLADFGLAKDL-------DSD 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 189011594 376 STVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd00180  146 DSLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYE 186
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
218-518 7.55e-38

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


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 141.53  E-value: 7.55e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594   218 IGEGGFGCVYRAVMRNTTY------AVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFL 291
Cdd:smart00221   7 LGEGAFGEVYKGTLKGKGDgkevevAVKTLKEDASEQ---QIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVMEYM 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594   292 PNGSLEDqlHLQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRfagan 371
Cdd:smart00221  84 PGGDLLD--YLRKNRPKELSLSDLLSFALQIARGMEYLE--SKNFIHRDLAARNCLVGENLVVKISDFGLSRDLY----- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594   372 psqSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLagqravrTQGAKTKYLKDLIEdeaeevgvtlks 451
Cdd:smart00221 155 ---DDDYYKVKGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIF-------TLGEEPYPGMSNAE------------ 212
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594   452 tqptlwmgvatdawtapIAAQIYKKHLDSRPGPCPPqlglALAQLACCCMHRRAKKRPPMTQVYKRL 518
Cdd:smart00221 213 -----------------VLEYLKKGYRLPKPPNCPP----ELYKLMLQCWAEDPEDRPTFSELVEIL 258
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
217-594 2.36e-37

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 145.93  E-value: 2.36e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEWTVVKQsFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNG 294
Cdd:COG0515   14 LLGRGGMGVVYLARDLRLgrPVALKVLRPELAADPEARER-FRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEGE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEDQLHLQtqacSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFSRfaganpsq 374
Cdd:COG0515   93 SLADLLRRR----GPLPPAEALRILAQLAEALAAAHAAG--IVHRDIKPANILLTPDGRVKLIDFGIARALG-------- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 375 SSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRavrtqgaktkylkdliedeaeevgvtlkstqp 454
Cdd:COG0515  159 GATLTQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRP-------------------------------- 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 455 tlwmgvatdAWTAPIAAQIYKKHLDSRPGPCP---PQLGLALAQLACCCMHRRAKKRPP-MTQVYKRLEGLQAVPPWKLE 530
Cdd:COG0515  207 ---------PFDGDSPAELLRAHLREPPPPPSelrPDLPPALDAIVLRALAKDPEERYQsAAELAAALRAVLRSLAAAAA 277
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594 531 VAGHGSPSPQENSYMSTTGSAQSGDEPWQPLVVTTRAPAQAAQQLQRSPNQPVESDESVPGLSA 594
Cdd:COG0515  278 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAAAAA 341
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
218-519 1.58e-36

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


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 138.06  E-value: 1.58e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRN-----TTYAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLP 292
Cdd:cd00192    3 LGEGAFGEVYKGKLKGgdgktVDVAVKTLKEDASES---ERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLEDqlHLQTQAC-------SPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFs 365
Cdd:cd00192   80 GGDLLD--FLRKSRPvfpspepSTLSLKDLLSFAIQIAKGMEYLA--SKKFVHRDLAARNCLVGEDLVVKISDFGLSRD- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 366 rfaganpSQSSTVARTCT-----VRgtlaYLPEEYIKTGRLAVDTDTFSFGVVILE--TLAGQravRTQGAKTKYLKDLI 438
Cdd:cd00192  155 -------IYDDDYYRKKTggklpIR----WMAPESLKDGIFTSKSDVWSFGVLLWEifTLGAT---PYPGLSNEEVLEYL 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 439 EDeaeevGVTLKstqptlwmgvatdawtapiaaqiykkhldsRPGPCPPqlglALAQLACCCMHRRAKKRPPMTQVYKRL 518
Cdd:cd00192  221 RK-----GYRLP------------------------------KPENCPD----ELYELMLSCWQLDPEDRPTFSELVERL 261

                 .
gi 189011594 519 E 519
Cdd:cd00192  262 E 262
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
218-518 1.64e-36

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 137.66  E-value: 1.64e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594   218 IGEGGFGCVYRAVMRNT------TYAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFL 291
Cdd:smart00219   7 LGEGAFGEVYKGKLKGKggkkkvEVAVKTLKEDASEQ---QIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVMEYM 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594   292 PNGSLEDQLHLQTqacSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSrfagan 371
Cdd:smart00219  84 EGGDLLSYLRKNR---PKLSLSDLLSFALQIARGMEYLE--SKNFIHRDLAARNCLVGENLVVKISDFGLSRDL------ 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594   372 PSQSSTVARTCtvRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLagqravrTQGAKTKYLKDLIEdeaeevgvtlks 451
Cdd:smart00219 153 YDDDYYRKRGG--KLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIF-------TLGEQPYPGMSNEE------------ 211
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594   452 tqptlwmgvatdawtapIAAQIYKKHLDSRPGPCPPqlglALAQLACCCMHRRAKKRPPMTQVYKRL 518
Cdd:smart00219 212 -----------------VLEYLKNGYRLPQPPNCPP----ELYDLMLQCWAEDPEDRPTFSELVEIL 257
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
217-422 3.16e-36

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: 136.95  E-value: 3.16e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAV--MRNTTYAVKRLKEEaDLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNG 294
Cdd:cd14014    7 LLGRGGMGEVYRARdtLLGRPVAIKVLRPE-LAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYVEGG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEDQLHLQtqacSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfaganPSQ 374
Cdd:cd14014   86 SLADLLRER----GPLPPREALRILAQIADALAAAHRAG--IVHRDIKPANILLTEDGRVKLTDFGIAR--------ALG 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 189011594 375 SSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQR 422
Cdd:cd14014  152 DSGLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRP 199
Death_IRAK cd08309
Death domain of Interleukin-1 Receptor-Associated Kinases; Death Domains (DDs) found in ...
17-100 4.43e-36

Death domain of Interleukin-1 Receptor-Associated Kinases; Death Domains (DDs) found in Interleukin-1 (IL-1) Receptor-Associated Kinases (IRAK1-4) and similar proteins. IRAKs are essential components of innate immunity and inflammation in mammals and other vertebrates. All four types are involved in signal transduction involving IL-1 and IL-18 receptors, Toll-like receptors, nuclear factor-kappaB, and mitogen-activated protein kinase pathways. IRAK1 and IRAK4 are active kinases while IRAK2 and IRAK-M (also called IRAK3) are inactive. In general, IRAKs are expressed ubiquitously, except for IRAK-M which is detected only in macrophages. The insect homologs, Pelle and Tube, are important components of the Toll pathway, which functions in establishing dorsoventral polarity in embryos and also in the innate immune response. Most members have an N-terminal DD followed by a kinase domain. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260023  Cd Length: 88  Bit Score: 130.54  E-value: 4.43e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594  17 HFLYEVPPWVMCRFYKVMDALEPADWCQFAALIVRDQTELRLCERSEQR----TASVLWPWINRNARVADLVHILTHLQL 92
Cdd:cd08309    1 TYIRNLPPWVLKRLCKVLDALELAGWRQLASLIPYDQTDVRQIESMKQRgqspTRELLWDWGTQNATVQDLVQLLTQLGL 80

                 ....*...
gi 189011594  93 LRARDIIT 100
Cdd:cd08309   81 FRAADLIT 88
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
217-518 3.66e-35

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: 134.16  E-value: 3.66e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594  217 RIGEGGFGCVYRAVMR------NTTYAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGF 290
Cdd:pfam07714   6 KLGEGAFGEVYKGTLKgegentKIKVAVKTLKEGADEE---EREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594  291 LPNGSLEDQLHLQTQacsPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFsrfagA 370
Cdd:pfam07714  83 MPGGDLLDFLRKHKR---KLTLKDLLSMALQIAKGMEYLE--SKNFVHRDLAARNCLVSENLVVKISDFGLSRD-----I 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594  371 NPSQSSTVARTCTVRgtLAYLPEEYIKTGRLAVDTDTFSFGVVILETLagqravrTQGAKTKYLKDLIEdeaeevgvtlk 450
Cdd:pfam07714 153 YDDDYYRKRGGGKLP--IKWMAPESLKDGKFTSKSDVWSFGVLLWEIF-------TLGEQPYPGMSNEE----------- 212
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594  451 stqptlwmgvatdawtapIAAQIYKKHLDSRPGPCPPQlglaLAQLACCCMHRRAKKRPPMTQVYKRL 518
Cdd:pfam07714 213 ------------------VLEFLEDGYRLPQPENCPDE----LYDLMKQCWAYDPEDRPTFSELVEDL 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
218-421 3.97e-34

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 131.11  E-value: 3.97e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594   218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:smart00220   7 LGEGSFGKVYLARDKKTgkLVAIKVIKKKKIKK---DRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCEGGD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594   296 LEDQLHlqtqACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFsrfagANPSQs 375
Cdd:smart00220  84 LFDLLK----KRGRLSEDEARFYLRQILSALEYLH--SKGIVHRDLKPENILLDEDGHVKLADFGLARQ-----LDPGE- 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 189011594   376 stvaRTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:smart00220 152 ----KLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGK 193
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
218-421 5.78e-33

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: 127.95  E-value: 5.78e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRA--VMRNTTYAVKRLKeeADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd13978    1 LGSGGFGTVSKArhVSWFGMVAIKCLH--SSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLHLQTQacsPLSWPQRLDILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAGANPSQS 375
Cdd:cd13978   79 LKSLLEREIQ---DVPWSLRFRIIHEIALGMNFLHNMDPPLLHHDLKPENILLDNHFHVKISDFGLSKLGMKSISANRRR 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 189011594 376 STVartcTVRGTLAYLPEEYIKTGRLAVDT--DTFSFGVVILETLAGQ 421
Cdd:cd13978  156 GTE----NLGGTPIYMAPEAFDDFNKKPTSksDVYSFAIVIWAVLTRK 199
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
218-519 4.88e-32

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: 125.20  E-value: 4.88e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLE 297
Cdd:cd14061    2 IGVGGFGKVYRGIWRGEEVAVKAARQDPDEDISVTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGGALN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 298 DQLhlqTQACSPlswPQRL-DILLGTARAIQFLHQDSP-SLIHGDIKSSNVLLDERLMP--------KLGDFGLARfsrf 367
Cdd:cd14061   82 RVL---AGRKIP---PHVLvDWAIQIARGMNYLHNEAPvPIIHRDLKSSNILILEAIENedlenktlKITDFGLAR---- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 368 aganpsqssTVARTCTVR--GTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVR-TQGAKTKYlkdliedeaee 444
Cdd:cd14061  152 ---------EWHKTTRMSaaGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKgIDGLAVAY----------- 211
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 445 vgvtlkstqptlwmGVATDAWTAPIaaqiykkhldsrPGPCPPqlglALAQLACCCMHRRAKKRPPMTQVYKRLE 519
Cdd:cd14061  212 --------------GVAVNKLTLPI------------PSTCPE----PFAQLMKDCWQPDPHDRPSFADILKQLE 256
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
218-419 4.76e-28

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 114.24  E-value: 4.76e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRN--TTYAVKRLKEEAdLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd14026    5 LSRGAFGTVSRARHADwrVTVAIKCLKLDS-PVGDSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTNGS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLHLQTQAcSPLSWPQRLDILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFsRFAGANPSQS 375
Cdd:cd14026   84 LNELLHEKDIY-PDVAWPLRLRILYEIALGVNYLHNMSPPLLHHDLKTQNILLDGEFHVKIADFGLSKW-RQLSISQSRS 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 189011594 376 STVArtcTVRGTLAYL-PEEY--IKTGRLAVDTDTFSFGVVILETLA 419
Cdd:cd14026  162 SKSA---PEGGTIIYMpPEEYepSQKRRASVKHDIYSYAIIMWEVLS 205
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
218-422 3.41e-27

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


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 111.07  E-value: 3.41e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEWTVvkQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd06606    8 LGKGSFGSVYLALNLDTgeLMAVKEVELSGDSEEEL--EALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGGS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLhlqtQACSPLSWPQ-RL---DILLGtaraIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSrfagan 371
Cdd:cd06606   86 LASLL----KKFGKLPEPVvRKytrQILEG----LEYLH--SNGIVHRDIKGANILVDSDGVVKLADFGCAKRL------ 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 189011594 372 pSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQR 422
Cdd:cd06606  150 -AEIATGEGTKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKP 199
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
218-524 3.38e-26

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: 108.59  E-value: 3.38e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLE 297
Cdd:cd14146    2 IGVGGFGKVYRATWKGQEVAVKAARQDPDEDIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGTLN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 298 DQLHLQTQACSPLSW----PQRL-DILLGTARAIQFLHQDS-PSLIHGDIKSSNVLLDERL--------MPKLGDFGLAR 363
Cdd:cd14146   82 RALAAANAAPGPRRArripPHILvNWAVQIARGMLYLHEEAvVPILHRDLKSSNILLLEKIehddicnkTLKITDFGLAR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 364 fsrfAGANPSQSSTVartctvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVR-TQGAKTKYlkdliedea 442
Cdd:cd14146  162 ----EWHRTTKMSAA-------GTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRgIDGLAVAY--------- 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 443 eevgvtlkstqptlwmGVATDAWTAPIaaqiykkhldsrPGPCPPqlglALAQLACCCMHRRAKKRPPMTQVykrLEGLQ 522
Cdd:cd14146  222 ----------------GVAVNKLTLPI------------PSTCPE----PFAKLMKECWEQDPHIRPSFALI---LEQLT 266

                 ..
gi 189011594 523 AV 524
Cdd:cd14146  267 AI 268
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
217-422 4.99e-26

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 107.97  E-value: 4.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVY--RAVMRNTTYAVK-------------RLKEEAdlewtvvkqsflTEVEQLsRFRHpnIVDFAGYCAES 281
Cdd:cd14025    3 KVGSGGFGQVYkvRHKHWKTWLAIKcppslhvddsermELLEEA------------KKMEMA-KFRH--ILPVYGICSEP 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 282 gfYCLVYGFLPNGSLEDQLhlqtqACSPLSWPQRLDILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLMPKLGDFGL 361
Cdd:cd14025   68 --VGLVMEYMETGSLEKLL-----ASEPLPWELRFRIIHETAVGMNFLHCMKPPLLHLDLKPANILLDAHYHVKISDFGL 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189011594 362 ARFSRFAganpsqSSTVARTCTVRGTLAYLPEEYIKTGRLAVDT--DTFSFGVVILETLAGQR 422
Cdd:cd14025  141 AKWNGLS------HSHDLSRDGLRGTIAYLPPERFKEKNRCPDTkhDVYSFAIVIWGILTQKK 197
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
218-521 1.12e-24

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: 103.67  E-value: 1.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVKRLKEEADlewtvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLE 297
Cdd:cd14058    1 VGRGSFGVVCKARWRNQIVAVKIIESESE------KKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 298 DQLH-----LQTQACSPLSWpqrldiLLGTARAIQFLHQDSP-SLIHGDIKSSNVLLDER-LMPKLGDFGLArfsrfagA 370
Cdd:cd14058   75 NVLHgkepkPIYTAAHAMSW------ALQCAKGVAYLHSMKPkALIHRDLKPPNLLLTNGgTVLKICDFGTA-------C 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 371 NPSQSSTVArtctvRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVrtqgaktkylkDLIEDEAeevgvtlk 450
Cdd:cd14058  142 DISTHMTNN-----KGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPF-----------DHIGGPA-------- 197
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189011594 451 stqPTLWMGVatdawtapiaaqiykkHLDSRPgPCPPQLGLALAQLACCCMHRRAKKRPPMTQVYKRLEGL 521
Cdd:cd14058  198 ---FRIMWAV----------------HNGERP-PLIKNCPKPIESLMTRCWSKDPEKRPSMKEIVKIMSHL 248
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
217-434 1.34e-24

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 104.33  E-value: 1.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTTYAVKRLKEEAdlewtvvKQSFLTEVE--QLSRFRHPNIVDFagYCAESGF------YCLVY 288
Cdd:cd14053    2 IKARGRFGAVWKAQYLNRLVAVKIFPLQE-------KQSWLTEREiySLPGMKHENILQF--IGAEKHGesleaeYWLIT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 289 GFLPNGSLEDQLHLQTqacspLSWPQRLDILLGTARAIQFLHQD--------SPSLIHGDIKSSNVLLDERLMPKLGDFG 360
Cdd:cd14053   73 EFHERGSLCDYLKGNV-----ISWNELCKIAESMARGLAYLHEDipatngghKPSIAHRDFKSKNVLLKSDLTACIADFG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 361 LARfsRF-AGANPSQS-STVartctvrGTLAYL-PE------EYIKTGRLAVdtDTFSFGVVILETLAgqRAVRTQGAKT 431
Cdd:cd14053  148 LAL--KFePGKSCGDThGQV-------GTRRYMaPEvlegaiNFTRDAFLRI--DMYAMGLVLWELLS--RCSVHDGPVD 214

                 ...
gi 189011594 432 KYL 434
Cdd:cd14053  215 EYQ 217
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
214-423 1.36e-24

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: 103.70  E-value: 1.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 214 EELR-IGEGGFGCVYRAVMRNT--TYAVKR--LKEEADLEwtvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVY 288
Cdd:cd08215    3 EKIRvIGKGSFGSAYLVRRKSDgkLYVLKEidLSNMSEKE----REEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 289 GFLPNGSLEDQLHLQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfa 368
Cdd:cd08215   79 EYADGGDLAQKIKKQKKKGQPFPEEQILDWFVQICLALKYLH--SRKILHRDLKTQNIFLTKDGVVKLGDFGISK----- 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189011594 369 ganpSQSSTVARTCTVRGTLAYL-PE-----EYIKTgrlavdTDTFSFGVVILETLAGQRA 423
Cdd:cd08215  152 ----VLESTTDLAKTVVGTPYYLsPElcenkPYNYK------SDIWALGCVLYELCTLKHP 202
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
204-416 1.39e-24

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror 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: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 104.38  E-value: 1.39e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 204 EISQGTCNFSEELriGEGGFGCVYRAVM-------RNTTYAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAG 276
Cdd:cd05048    1 EIPLSAVRFLEEL--GEGAFGKVYKGELlgpsseeSAISVAIKTLKENASPK---TQQDFRREAELMSDLQHPNIVCLLG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 277 YCAESGFYCLVYGFLPNGSLEDQLHLQTQAC------------SPLSWPQRLDILLGTARAIQFLhqDSPSLIHGDIKSS 344
Cdd:cd05048   76 VCTKEQPQCMLFEYMAHGDLHEFLVRHSPHSdvgvssdddgtaSSLDQSDFLHIAIQIAAGMEYL--SSHHYVHRDLAAR 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189011594 345 NVLLDERLMPKLGDFGLARFSRFAGANPSQSSTVartCTVRgtlaYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd05048  154 NCLVGDGLTVKISDFGLSRDIYSSDYYRVQSKSL---LPVR----WMPPEAILYGKFTTESDVWSFGVVLWE 218
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
218-519 2.39e-24

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: 102.76  E-value: 2.39e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLE 297
Cdd:cd14148    2 IGVGGFGKVYKGLWRGEEVAVKAARQDPDEDIAVTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGALN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 298 DQLHLQTQACSPL-SWPQRLdillgtARAIQFLHQDSP-SLIHGDIKSSNVLLDERL--------MPKLGDFGLARfsrf 367
Cdd:cd14148   82 RALAGKKVPPHVLvNWAVQI------ARGMNYLHNEAIvPIIHRDLKSSNILILEPIenddlsgkTLKITDFGLAR---- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 368 aganPSQSSTvarTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRtqgaktkylkdliedEAEEVGV 447
Cdd:cd14148  152 ----EWHKTT---KMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYR---------------EIDALAV 209
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189011594 448 TlkstqptlwMGVATDAWTAPIaaqiykkhldsrPGPCPPqlglALAQLACCCMHRRAKKRPPMTQVYKRLE 519
Cdd:cd14148  210 A---------YGVAMNKLTLPI------------PSTCPE----PFARLLEECWDPDPHGRPDFGSILKRLE 256
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
218-519 2.45e-24

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: 102.19  E-value: 2.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVKRLKEEADlewtvvkqsflTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLE 297
Cdd:cd14059    1 LGSGAQGAVFLGKFRGEEVAVKKVRDEKE-----------TDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLY 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 298 DQLHlqtqACSPLSwPQRL-DILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfagaNPSQSS 376
Cdd:cd14059   70 EVLR----AGREIT-PSLLvDWSKQIASGMNYLH--LHKIIHRDLKSPNVLVTYNDVLKISDFGTSK-------ELSEKS 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 377 TvarTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQravrtqgakTKYlKDLiedeaeevgvtlkSTQPTL 456
Cdd:cd14059  136 T---KMSFAGTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGE---------IPY-KDV-------------DSSAII 189
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189011594 457 WmGVATDAWTAPIaaqiykkhldsrPGPCPPQLGLALAQlaccCMHRRAKKRPPMTQVYKRLE 519
Cdd:cd14059  190 W-GVGSNSLQLPV------------PSTCPDGFKLLMKQ----CWNSKPRNRPSFRQILMHLD 235
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
218-421 7.79e-24

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: 101.45  E-value: 7.79e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVKRL-------KEEADLewtvvkqsFLTEVEQLSRFRHPNIVDFAGYCAES-GFYCLVYG 289
Cdd:cd14064    1 IGSGSFGKVYKGRCRNKIVAIKRYrantycsKSDVDM--------FCREVSILCRLNHPCVIQFVGACLDDpSQFAIVTQ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLEDQLHLQTQACSPLSwpqRLDILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFsrfag 369
Cdd:cd14064   73 YVSGGSLFSLLHEQKRVIDLQS---KLIIAVDVAKGMEYLHNLTQPIIHRDLNSHNILLYEDGHAVVADFGESRF----- 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 189011594 370 anpSQSSTVARTCTVRGTLAYL-PEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd14064  145 ---LQSLDEDNMTKQPGNLRWMaPEVFTQCTRYSIKADVFSYALCLWELLTGE 194
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
214-521 4.38e-23

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: 99.33  E-value: 4.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 214 EELR----IGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYG 289
Cdd:cd14147    3 QELRleevIGIGGFGKVYRGSWRGELVAVKAARQDPDEDISVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLEDQLhlQTQACSP---LSWPQRLdillgtARAIQFLHQDS-PSLIHGDIKSSNVLLD--------ERLMPKLG 357
Cdd:cd14147   83 YAAGGPLSRAL--AGRRVPPhvlVNWAVQI------ARGMHYLHCEAlVPVIHRDLKSNNILLLqpienddmEHKTLKIT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 358 DFGLARfsrfAGANPSQSSTVartctvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVR-TQGAKTKYlkd 436
Cdd:cd14147  155 DFGLAR----EWHKTTQMSAA-------GTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRgIDCLAVAY--- 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 437 liedeaeevgvtlkstqptlwmGVATDAWTAPIaaqiykkhldsrPGPCPPqlglALAQLACCCMHRRAKKRPPMTQVYK 516
Cdd:cd14147  221 ----------------------GVAVNKLTLPI------------PSTCPE----PFAQLMADCWAQDPHRRPDFASILQ 262

                 ....*
gi 189011594 517 RLEGL 521
Cdd:cd14147  263 QLEAL 267
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
217-421 6.93e-23

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


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 99.00  E-value: 6.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTTYAVKRLKEEADleWTVVKQSFLTEVeQLSRFRHPNIVDFAGycAESGFYCLVYG-----FL 291
Cdd:cd13979   10 PLGSGGFGSVYKATYKGETVAVKIVRRRRK--NRASRQSFWAEL-NAARLRHENIVRVLA--AETGTDFASLGliimeYC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 PNGSLEdqlHLQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGlARFSRFAGan 371
Cdd:cd13979   85 GNGTLQ---QLIYEGSEPLPLAHRILISLDIARALRFCH--SHGIVHLDVKPANILISEQGVCKLCDFG-CSVKLGEG-- 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 189011594 372 psqSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd13979  157 ---NEVGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRE 203
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
218-521 2.55e-22

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 97.04  E-value: 2.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVKRLKEEADlewtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLE 297
Cdd:cd05039   14 IGKGEFGDVMLGDYRGQKVAVKCLKDDST-----AAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYMAKGSLV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 298 DqlHLQTQACSPLSWPQRLDILLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSrfaganpSQSST 377
Cdd:cd05039   89 D--YLRSRGRAVITRKDQLGFALDVCEGMEYL--ESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEA-------SSNQD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 378 VARtctvrgtlayLP-----EEYIKTGRLAVDTDTFSFGVVILETLAGQRAvrtqgaktKY----LKDLIedEAEEVGVT 448
Cdd:cd05039  158 GGK----------LPikwtaPEALREKKFSTKSDVWSFGILLWEIYSFGRV--------PYpripLKDVV--PHVEKGYR 217
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189011594 449 LKStqptlwmgvatdawtapiaaqiykkhldsrPGPCPPQlglaLAQLACCCMHRRAKKRPPMTQVYKRLEGL 521
Cdd:cd05039  218 MEA------------------------------PEGCPPE----VYKVMKNCWELDPAKRPTFKQLREKLEHI 256
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
217-416 3.15e-22

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: 96.50  E-value: 3.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEWTVVKQsfltEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNG 294
Cdd:cd05122    7 KIGKGGFGVVYKARHKKTgqIVAIKKINLESKEKKESILN----EIAILKKCKHPNIVKYYGSYLKKDELWIVMEFCSGG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEDQLHlqtQACSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLArfSRFAGANPSQ 374
Cdd:cd05122   83 SLKDLLK---NTNKTLTEQQIAYVCKEVLKGLEYLHSHG--IIHRDIKAANILLTSDGEVKLIDFGLS--AQLSDGKTRN 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 189011594 375 SSTvartctvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd05122  156 TFV--------GTPYWMAPEVIQGKPYGFKADIWSLGITAIE 189
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
217-413 4.18e-22

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: 96.98  E-value: 4.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVY--RAVMRNTTYAVKRLK-------EEAdlewtvvkqsfLTEVEQLSRFRHPNIVDFAGYC--AESGFYC 285
Cdd:cd13986    7 LLGEGGFSFVYlvEDLSTGRLYALKKILchskedvKEA-----------MREIENYRLFNHPNILRLLDSQivKEAGGKK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 286 LVYGFLP---NGSLEDQLHLQTQACSPLSWPQRLDILLGTARAIQFLHQ-DSPSLIHGDIKSSNVLLDERLMPKLGDFGL 361
Cdd:cd13986   76 EVYLLLPyykRGSLQDEIERRLVKGTFFPEDRILHIFLGICRGLKAMHEpELVPYAHRDIKPGNVLLSEDDEPILMDLGS 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 362 ARFSRFAGANPSQSSTVARTCTVRGTLAYLPEEY--IKTGRLAVD-TDTFSFGVV 413
Cdd:cd13986  156 MNPARIEIEGRREALALQDWAAEHCTMPYRAPELfdVKSHCTIDEkTDIWSLGCT 210
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
211-518 2.20e-21

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: 94.72  E-value: 2.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 211 NFSE---ELRIGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLV 287
Cdd:cd14145    4 DFSElvlEEIIGIGGFGKVYRAIWIGDEVAVKAARHDPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 288 YGFLPNGSLEDQlhLQTQACSP---LSWPQRLdillgtARAIQFLHQDS-PSLIHGDIKSSNVLLDERL--------MPK 355
Cdd:cd14145   84 MEFARGGPLNRV--LSGKRIPPdilVNWAVQI------ARGMNYLHCEAiVPVIHRDLKSSNILILEKVengdlsnkILK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 356 LGDFGLARfsrfaganpsqssTVARTC--TVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVR-TQGAKTK 432
Cdd:cd14145  156 ITDFGLAR-------------EWHRTTkmSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRgIDGLAVA 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 433 YlkdliedeaeevgvtlkstqptlwmGVATDAWTAPIaaqiykkhldsrPGPCPPqlglALAQLACCCMHRRAKKRPPMT 512
Cdd:cd14145  223 Y-------------------------GVAMNKLSLPI------------PSTCPE----PFARLMEDCWNPDPHSRPPFT 261

                 ....*.
gi 189011594 513 QVYKRL 518
Cdd:cd14145  262 NILDQL 267
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
217-420 3.00e-21

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: 93.93  E-value: 3.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTTyAVKRLKEEADLEWTVvkQSFLTEVEQLSRFRHPNIVDFAGYCAESGFyCLVYGFLPNGSL 296
Cdd:cd14150    7 RIGTGSFGTVFRGKWHGDV-AVKILKVTEPTPEQL--QAFKNEMQVLRKTRHVNILLFMGFMTRPNF-AIITQWCEGSSL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 297 EDQLHLqtqACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARF-SRFAGANPSQS 375
Cdd:cd14150   83 YRHLHV---TETRFDTMQLIDVARQTAQGMDYLH--AKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVkTRWSGSQQVEQ 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 189011594 376 STvartctvrGTLAYLPEEYIK---TGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd14150  158 PS--------GSILWMAPEVIRmqdTNPYSFQSDVYAYGVVLYELMSG 197
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
218-421 3.59e-21

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: 93.61  E-value: 3.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTyAVKRLK----EEADLewtvvkQSFLTEVEQLSRFRHPNIVDFAGYCAESGFyCLVYGFLPN 293
Cdd:cd14062    1 IGSGSFGTVYKGRWHGDV-AVKKLNvtdpTPSQL------QAFKNEVAVLRKTRHVNILLFMGYMTKPQL-AIVTQWCEG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 294 GSLEDQLHLQTQACSPLswpQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARF-SRFAGANP 372
Cdd:cd14062   73 SSLYKHLHVLETKFEML---QLIDIARQTAQGMDYLH--AKNIIHRDLKSNNIFLHEDLTVKIGDFGLATVkTRWSGSQQ 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 373 SQSSTvartctvrGTLAYLPEEYIktgRLAVDT------DTFSFGVVILETLAGQ 421
Cdd:cd14062  148 FEQPT--------GSILWMAPEVI---RMQDENpysfqsDVYAFGIVLYELLTGQ 191
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
219-521 4.75e-21

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: 92.71  E-value: 4.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 219 GEGGFGCVYRA--VMRNTTYAVKRL-KEEAdlewtvvkqsfltEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd14060    2 GGGSFGSVYRAiwVSQDKEVAVKKLlKIEK-------------EAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGS 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDqlHLQTQACSPLSWPQRLDILLGTARAIQFLHQDSP-SLIHGDIKSSNVLLDERLMPKLGDFGLARFsrfaganpsQ 374
Cdd:cd14060   69 LFD--YLNSNESEEMDMDQIMTWATDIAKGMHYLHMEAPvKVIHRDLKSRNVVIAADGVLKICDFGASRF---------H 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 375 SSTVARTCTvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVR-TQGAKTKYLkdliedeaeevgVTLKSTQ 453
Cdd:cd14060  138 SHTTHMSLV--GTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKgLEGLQVAWL------------VVEKNER 203
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594 454 PTLwmgvatdawtapiaaqiykkhldsrPGPCPPqlglALAQLACCCMHRRAKKRPPMTQVYKRLEGL 521
Cdd:cd14060  204 PTI-------------------------PSSCPR----SFAELMRRCWEADVKERPSFKQIIGILESM 242
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
218-393 1.26e-20

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 93.19  E-value: 1.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVKRLKEEAdlewtvvKQSFLTEVE--QLSRFRHPNIVDFAGYC---AESGF--YCLVYGF 290
Cdd:cd14054    3 IGQGRYGTVWKGSLDERPVAVKVFPARH-------RQNFQNEKDiyELPLMEHSNILRFIGADerpTADGRmeYLLVLEY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDQLHLQTqacspLSWPQRLDILLGTARAIQFLHQD-------SPSLIHGDIKSSNVLLDERLMPKLGDFGLA- 362
Cdd:cd14054   76 APKGSLCSYLRENT-----LDWMSSCRMALSLTRGLAYLHTDlrrgdqyKPAIAHRDLNSRNVLVKADGSCVICDFGLAm 150
                        170       180       190
                 ....*....|....*....|....*....|....
gi 189011594 363 --RFSRFAGANPSQSSTVArtCTVRGTLAYL-PE 393
Cdd:cd14054  151 vlRGSSLVRGRPGAAENAS--ISEVGTLRYMaPE 182
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
218-518 1.55e-20

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


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 91.78  E-value: 1.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRaVMRNTTYAVKRLKEEADlewTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLE 297
Cdd:cd14065    1 LGKGFFGEVYK-VTHRETGKVMVMKELKR---FDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 298 DqlhLQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPK---LGDFGLArfsRFAGANPSQ 374
Cdd:cd14065   77 E---LLKSMDEQLPWSQRVSLAKDIASGMAYLH--SKNIIHRDLNSKNCLVREANRGRnavVADFGLA---REMPDEKTK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 375 SSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAgqravRTQgAKTKYLKdliedEAEEVGVTLkstqp 454
Cdd:cd14065  149 KPDRKKRLTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEIIG-----RVP-ADPDYLP-----RTMDFGLDV----- 212
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594 455 tlwmgvatdawtapiaaqiyKKHLDSRPGPCPPQlglaLAQLACCCMHRRAKKRPPMTQVYKRL 518
Cdd:cd14065  213 --------------------RAFRTLYVPDCPPS----FLPLAIRCCQLDPEKRPSFVELEHHL 252
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
218-421 2.06e-20

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: 91.38  E-value: 2.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEWTVVKQsFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd14007    8 LGKGKFGNVYLAREKKSgfIVALKVISKSQLQKSGLEHQ-LRREIEIQSHLRHPNILRLYGYFEDKKRIYLILEYAPNGE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLhlqtQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLArfsrfAGANPSQS 375
Cdd:cd14007   87 LYKEL----KKQKRFDEKEAAKYIYQLALALDYLH--SKNIIHRDIKPENILLGSNGELKLADFGWS-----VHAPSNRR 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 189011594 376 STVartCtvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd14007  156 KTF---C---GTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGK 195
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
218-421 3.68e-20

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: 90.73  E-value: 3.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd06623    9 LGQGSSGVVYKVRHKPTgkIYALKKIHVDGDEE---FRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDGGS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLhlqtQACSPLSWPQRLDILLGTARAIQFLHQDSpSLIHGDIKSSNVLLDERLMPKLGDFGLARFSrfaganpsqS 375
Cdd:cd06623   86 LADLL----KKVGKIPEPVLAYIARQILKGLDYLHTKR-HIIHRDIKPSNLLINSKGEVKIADFGISKVL---------E 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 189011594 376 STVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd06623  152 NTLDQCNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGK 197
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
218-523 4.84e-20

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


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 90.23  E-value: 4.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRaVMRNTTYAVKRLKEEadlEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLE 297
Cdd:cd14155    1 IGSGFFSEVYK-VRHRTSGQVMALKMN---TLSSNRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 298 DQLhlqtQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLL---DERLMPKLGDFGLARfsrfagANPSQ 374
Cdd:cd14155   77 QLL----DSNEPLSWTVRVKLALDIARGLSYLH--SKGIFHRDLTSKNCLIkrdENGYTAVVGDFGLAE------KIPDY 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 375 SSTVARTCTVrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAgqravRTQgAKTKYLKDliedeaeevgvtlkstqp 454
Cdd:cd14155  145 SDGKEKLAVV-GSPYWMAPEVLRGEPYNEKADVFSYGIILCEIIA-----RIQ-ADPDYLPR------------------ 199
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 455 TLWMGVATDAWtapiaaqiykKHLdsrPGPCPPQLgLALAqLACCCMHrrAKKRPPMTQVYKRLEGLQA 523
Cdd:cd14155  200 TEDFGLDYDAF----------QHM---VGDCPPDF-LQLA-FNCCNMD--PKSRPSFHDIVKTLEEILE 251
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
218-416 4.93e-20

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 90.99  E-value: 4.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRN-------TTYAVKRLKEEADlewTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGF 290
Cdd:cd05049   13 LGEGAFGKVFLGECYNlepeqdkMLVAVKTLKDASS---PDARKDFEREAELLTNLQHENIVKFYGVCTEGDPLLMVFEY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDQLHL----------QTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFG 360
Cdd:cd05049   90 MEHGDLNKFLRShgpdaaflasEDSAPGELTLSQLLHIAVQIASGMVYLA--SQHFVHRDLATRNCLVGTNLVVKIGDFG 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189011594 361 LAR------FSRFAGanpsqsstvARTCTVRgtlaYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd05049  168 MSRdiystdYYRVGG---------HTMLPIR----WMPPESILYRKFTTESDVWSFGVVLWE 216
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
211-418 6.76e-20

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: 90.43  E-value: 6.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 211 NFSEELRIGEGGFGCVY--RAVMRNTTYAVK--RLKEEADLEWTVVKqsfltEVEQLSRFRHPNIVDFAGYCAESGF--- 283
Cdd:cd13996    7 DFEEIELLGSGGFGSVYkvRNKVDGVTYAIKkiRLTEKSSASEKVLR-----EVKALAKLNHPNIVRYYTAWVEEPPlyi 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 284 ---YClvygflPNGSLEDQLHLQTQACSpLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDER-LMPKLGDF 359
Cdd:cd13996   82 qmeLC------EGGTLRDWIDRRNSSSK-NDRKLALELFKQILKGVSYIH--SKGIVHRDLKPSNIFLDNDdLQVKIGDF 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594 360 GLARF----SRFAGANPSQSSTVARTCTVR-GTLAYLPEEYIKTGRLAVDTDTFSFGVVILETL 418
Cdd:cd13996  153 GLATSignqKRELNNLNNNNNGNTSNNSVGiGTPLYASPEQLDGENYNEKADIYSLGIILFEML 216
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
217-416 9.10e-20

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 89.26  E-value: 9.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTT-YAVKRLKEEadlewTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd05034    2 KLGAGQFGEVWMGVWNGTTkVAVKTLKPG-----TMSPEAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKGS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDqlHLQTQACSPLSWPQRLDILLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAGANPSQS 375
Cdd:cd05034   77 LLD--YLRTGEGRALRLPQLIDMAAQIASGMAYL--ESRNYIHRDLAARNILVGENNVCKVADFGLARLIEDDEYTAREG 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 189011594 376 STVArtctVRGTlayLPEEyIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd05034  153 AKFP----IKWT---APEA-ALYGRFTIKSDVWSFGILLYE 185
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
211-437 1.25e-19

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


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 89.47  E-value: 1.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 211 NFSEELRIGEGGFGCVYRAVMR--NTTYAVKRLK---EEADlewtvvkqsflTEVEQLSRFRHPNIVDFagYCAESGF-Y 284
Cdd:cd14047    7 DFKEIELIGSGGFGQVFKAKHRidGKTYAIKRVKlnnEKAE-----------REVKALAKLDHPNIVRY--NGCWDGFdY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 285 CLVYGFL-PNGSLEDQLHLQTQACS--PL-SWPQR-----------LDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLD 349
Cdd:cd14047   74 DPETSSSnSSRSKTKCLFIQMEFCEkgTLeSWIEKrngekldkvlaLEIFEQITKGVEYIH--SKKLIHRDLKPSNIFLV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 350 ERLMPKLGDFGLArfSRFAGANPSQSStvartctvRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAgqrAVRTQGA 429
Cdd:cd14047  152 DTGKVKIGDFGLV--TSLKNDGKRTKS--------KGTLSYMSPEQISSQDYGKEVDIYALGLILFELLH---VCDSAFE 218

                 ....*...
gi 189011594 430 KTKYLKDL 437
Cdd:cd14047  219 KSKFWTDL 226
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
218-435 5.85e-19

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: 87.32  E-value: 5.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTY--AVKRLKEeADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd14116   13 LGKGKFGNVYLAREKQSKFilALKVLFK-AQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGT 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLhlqtQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSrfaganPSqs 375
Cdd:cd14116   92 VYREL----QKLSKFDEQRTATYITELANALSYCH--SKRVIHRDIKPENLLLGSAGELKIADFGWSVHA------PS-- 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189011594 376 stvARTCTVRGTLAYLPEEYIKtGRLAVD-TDTFSFGVVILETLAGQRAVRTQGAKTKYLK 435
Cdd:cd14116  158 ---SRRTTLCGTLDYLPPEMIE-GRMHDEkVDLWSLGVLCYEFLVGKPPFEANTYQETYKR 214
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
217-429 5.88e-19

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


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 87.08  E-value: 5.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMR--NTTYAVK---------RLKEEAdlewtvvkqsfLTEVEQLSRFRHPNIVDFAGYCAESGFYC 285
Cdd:cd08529    7 KLGKGSFGVVYKVVRKvdGRVYALKqidisrmsrKMREEA-----------IDEARVLSKLNSPYVIKYYDSFVDKGKLN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 286 LVYGFLPNGSLEDQLHLQTQacSPLS----WPQRLDILLGtaraIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGL 361
Cdd:cd08529   76 IVMEYAENGDLHSLIKSQRG--RPLPedqiWKFFIQTLLG----LSHLH--SKKILHRDIKSMNIFLDKGDNVKIGDLGV 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 362 ARFSrfaganpSQSSTVARtcTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRA--VRTQGA 429
Cdd:cd08529  148 AKIL-------SDTTNFAQ--TIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPfeAQNQGA 208
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
218-421 6.03e-19

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: 86.90  E-value: 6.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEWTVvkQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd06627    8 IGRGAFGSVYKGLNLNTgeFVAIKQISLEKIPKSDL--KSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVENGS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLHlqtqACSPLswPQRL------DILLGTAraiqFLHQDspSLIHGDIKSSNVLLDERLMPKLGDFGLArfSRFAG 369
Cdd:cd06627   86 LASIIK----KFGKF--PESLvavyiyQVLEGLA----YLHEQ--GVIHRDIKGANILTTKDGLVKLADFGVA--TKLNE 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 189011594 370 ANPSQSSTVartctvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd06627  152 VEKDENSVV-------GTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGN 196
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
217-422 6.09e-19

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: 87.36  E-value: 6.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTTY--AVKRLKEEaDLEWTVVKQsFLTEVEQLSRFRHPNIVDFAG-------------YCAES 281
Cdd:cd06626    7 KIGEGTFGKVYTAVNLDTGElmAMKEIRFQ-DNDPKTIKE-IADEMKVLEGLDHPNLVRYYGvevhreevyifmeYCQEG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 282 GfyclVYGFLPNGSLEDQLHLQTQAcsplswpqrLDILlgtaRAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGL 361
Cdd:cd06626   85 T----LEELLRHGRILDEAVIRVYT---------LQLL----EGLAYLHENG--IVHRDIKPANIFLDSNGLIKLGDFGS 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 362 ARFSrfagANPSQSSTVARTCTVRGTLAYLPEEYIK----TGRLAVDtDTFSFGVVILETLAGQR 422
Cdd:cd06626  146 AVKL----KNNTTTMAPGEVNSLVGTPAYMAPEVITgnkgEGHGRAA-DIWSLGCVVLEMATGKR 205
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
218-416 8.64e-19

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


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 87.18  E-value: 8.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRaVMRNTTYAVKRLKE--EADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd14154    1 LGKGFFGQAIK-VTHRETGEVMVMKEliRFDEE---AQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLHLQTQacsPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARF---SRFAGANP 372
Cdd:cd14154   77 LKDVLKDMAR---PLPWAQRVRFAKDIASGMAYLH--SMNIIHRDLNSHNCLVREDKTVVVADFGLARLiveERLPSGNM 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 189011594 373 SQSSTVART--------CTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd14154  152 SPSETLRHLkspdrkkrYTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCE 203
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
219-418 1.40e-18

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 86.29  E-value: 1.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 219 GEGGFGcVYRAVMRNTTYAVKRLKEEAdlewtVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLED 298
Cdd:cd13992   12 GEPKYV-KKVGVYGGRTVAIKHITFSR-----TEKRTILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 299 QLHLQTQacsPLSWPQRLDILLGTARAIQFLHQdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRfaGANPSQSSTV 378
Cdd:cd13992   86 VLLNREI---KMDWMFKSSFIKDIVKGMNYLHS-SSIGYHGRLKSSNCLVDSRWVVKLTDFGLRNLLE--EQTNHQLDED 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 189011594 379 ARtctvRGTLAYLPEEYIK----TGRLAVDTDTFSFGVVILETL 418
Cdd:cd13992  160 AQ----HKKLLWTAPELLRgsllEVRGTQKGDVYSFAIILYEIL 199
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
217-420 1.52e-18

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: 85.96  E-value: 1.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMR--NTTYAVKRLKEE--ADLewtvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLP 292
Cdd:cd05041    2 KIGRGNFGDVYRGVLKpdNTEVAVKTCRETlpPDL-----KRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLEDqlHLQTQAcSPLSWPQRLDILLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfaganp 372
Cdd:cd05041   77 GGSLLT--FLRKKG-ARLTVKQLLQMCLDAAAGMEYL--ESKNCIHRDLAARNCLVGENNVLKISDFGMSR--------- 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 189011594 373 sqsSTVARTCTVRGTLAYLP-----EEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd05041  143 ---EEEDGEYTVSDGLKQIPikwtaPEALNYGRYTSESDVWSFGILLWEIFSL 192
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
204-421 2.05e-18

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 85.88  E-value: 2.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 204 EISQGTCNFSEelRIGEGGFGCVYRAVMRNTTyAVKRLKEEADLEWTVvkQSFLTEVEQLSRFRHPNIVDFAGYCAESGF 283
Cdd:cd14151    4 EIPDGQITVGQ--RIGSGSFGTVYKGKWHGDV-AVKMLNVTAPTPQQL--QAFKNEVGVLRKTRHVNILLFMGYSTKPQL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 284 yCLVYGFLPNGSLEDQLHLQTqacSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLAR 363
Cdd:cd14151   79 -AIVTQWCEGSSLYHHLHIIE---TKFEMIKLIDIARQTAQGMDYLH--AKSIIHRDLKSNNIFLHEDLTVKIGDFGLAT 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189011594 364 F-SRFAGANPSQSstvartctVRGTLAYLPEEYIK---TGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd14151  153 VkSRWSGSHQFEQ--------LSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQ 206
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
218-416 2.37e-18

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 85.95  E-value: 2.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVKRLKEEAdlewtvvKQSFLTEVE--QLSRFRHPNIVDF-AGYCAESGF---YCLVYGFL 291
Cdd:cd13998    3 IGKGRFGEVWKASLKNEPVAVKIFSSRD-------KQSWFREKEiyRTPMLKHENILQFiAADERDTALrteLWLVTAFH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 PNGSLEDQLHLQTqacspLSWPQRLDILLGTARAIQFLHQD-------SPSLIHGDIKSSNVLLDERLMPKLGDFGLA-R 363
Cdd:cd13998   76 PNGSL*DYLSLHT-----IDWVSLCRLALSVARGLAHLHSEipgctqgKPAIAHRDLKSKNILVKNDGTCCIADFGLAvR 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 364 FSrfaganPSQSSTVARTCTVRGTLAYLPEEYIKtGRLAVD-------TDTFSFGVVILE 416
Cdd:cd13998  151 LS------PSTGEEDNANNGQVGTKRYMAPEVLE-GAINLRdfesfkrVDIYAMGLVLWE 203
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
217-379 5.03e-18

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: 85.06  E-value: 5.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTT--YAVKRLKEEADLEwtVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNg 294
Cdd:cd07833    8 VVGEGAYGVVLKCRNKATGeiVAIKKFKESEDDE--DVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEYVER- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEDQLHLQTQACSP-----LSWpQRLdillgtaRAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFSRfAG 369
Cdd:cd07833   85 TLLELLEASPGGLPPdavrsYIW-QLL-------QAIAYCHSHN--IIHRDIKPENILVSESGVLKLCDFGFARALT-AR 153
                        170
                 ....*....|
gi 189011594 370 ANPSQSSTVA 379
Cdd:cd07833  154 PASPLTDYVA 163
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
211-420 5.92e-18

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: 83.97  E-value: 5.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 211 NFSEELRIGEGGFGCVYRAVMRNTT--YAVKRLKEEadLEWTVVKQSFLTEVEQLSRF-RHPNIVDFagYCA--ESGFYC 285
Cdd:cd13997    1 HFHELEQIGSGSFSEVFKVRSKVDGclYAVKKSKKP--FRGPKERARALREVEAHAALgQHPNIVRY--YSSweEGGHLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 286 LVYGFLPNGSLEDQLHLQTQAcSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLArfS 365
Cdd:cd13997   77 IQMELCENGSLQDALEELSPI-SKLSEAEVWDLLLQVALGLAFIH--SKGIVHLDIKPDNIFISNKGTCKIGDFGLA--T 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 189011594 366 RFAGANPSQsstvartctvRGTLAYLPEEYIKTGRLAVD-TDTFSFGVVILETLAG 420
Cdd:cd13997  152 RLETSGDVE----------EGDSRYLAPELLNENYTHLPkADIFSLGVTVYEAATG 197
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
218-416 6.07e-18

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA 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: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 84.63  E-value: 6.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRN-------TTYAVKRLKEEADlewtVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGF 290
Cdd:cd05092   13 LGEGAFGKVFLAECHNllpeqdkMLVAVKALKEATE----SARQDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDQLHL-----------QTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDF 359
Cdd:cd05092   89 MRHGDLNRFLRShgpdakildggEGQAPGQLTLGQMLQIASQIASGMVYLA--SLHFVHRDLATRNCLVGQGLVVKIGDF 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189011594 360 GLAR------FSRFAGanpsqsstvaRTCTvrgTLAYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd05092  167 GMSRdiystdYYRVGG----------RTML---PIRWMPPESILYRKFTTESDIWSFGVVLWE 216
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
217-421 7.21e-18

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: 84.70  E-value: 7.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTTyAVKRLKEEADLEWTVvkQSFLTEVEQLSRFRHPNIVDFAGYCAESGFyCLVYGFLPNGSL 296
Cdd:cd14149   19 RIGSGSFGTVYKGKWHGDV-AVKILKVVDPTPEQF--QAFRNEVAVLRKTRHVNILLFMGYMTKDNL-AIVTQWCEGSSL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 297 EDQLHLQTqacSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARF-SRFAGANPSQS 375
Cdd:cd14149   95 YKHLHVQE---TKFQMFQLIDIARQTAQGMDYLH--AKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVkSRWSGSQQVEQ 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 189011594 376 STvartctvrGTLAYLPEEYIK---TGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd14149  170 PT--------GSILWMAPEVIRmqdNNPFSFQSDVYSYGIVLYELMTGE 210
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
217-421 8.36e-18

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: 83.80  E-value: 8.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNT--TYAVKRLKEEADlewtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNG 294
Cdd:cd06614    7 KIGEGASGEVYKATDRATgkEVAIKKMRLRKQ-----NKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEDQLhlqTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLArfsrfAGANPSQ 374
Cdd:cd06614   82 SLTDII---TQNPVRMNESQIAYVCREVLQGLEYLH--SQNVIHRDIKSDNILLSKDGSVKLADFGFA-----AQLTKEK 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 189011594 375 SStvaRTcTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd06614  152 SK---RN-SVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGE 194
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
214-422 1.96e-17

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 83.00  E-value: 1.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 214 EELrIGEGGFGCVYRAVM-----RNTTYAVKRLKEEADLEWtvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVY 288
Cdd:cd05065    9 EEV-IGAGEFGEVCRGRLklpgkREIFVAIKTLKSGYTEKQ---RRDFLSEASIMGQFDHPNIIHLEGVVTKSRPVMIIT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 289 GFLPNGSLEDQLHLQTQACSPLswpQRLDILLGTARAIQFLHQdsPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFA 368
Cdd:cd05065   85 EFMENGALDSFLRQNDGQFTVI---QLVGMLRGIAAGMKYLSE--MNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDD 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 369 GANPSQSSTVARTCTVRGTlaylPEEYIKTGRLAVDTDTFSFGVVILETLA-GQR 422
Cdd:cd05065  160 TSDPTYTSSLGGKIPIRWT----APEAIAYRKFTSASDVWSYGIVMWEVMSyGER 210
Pkinase pfam00069
Protein kinase domain;
212-443 1.97e-17

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 81.52  E-value: 1.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594  212 FSEELRIGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEWTvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYG 289
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTgkIVAIKKIKKEKIKKKK--DKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594  290 FLPNGSLEDQLHLQTqacsPLSWPQRLDILLGTARAIqflhqdspslihgdikssnvllderlmpklgdfglarfsrfag 369
Cdd:pfam00069  79 YVEGGSLFDLLSEKG----AFSEREAKFIMKQILEGL------------------------------------------- 111
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594  370 ANPSQsstvarTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAKTKYLKDLIEDEAE 443
Cdd:pfam00069 112 ESGSS------LTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAF 179
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
218-421 2.08e-17

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: 82.45  E-value: 2.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVK--RLKEEADLEWTVVKQsFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPN 293
Cdd:cd06632    8 LGSGSFGSVYEGFNGDTgdFFAVKevSLVDDDKKSRESVKQ-LEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVPG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 294 GSLEDQLhlqtQACSPLSWPQ-RL---DILLGtaraIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfag 369
Cdd:cd06632   87 GSIHKLL----QRYGAFEEPViRLytrQILSG----LAYLH--SRNTVHRDIKGANILVDTNGVVKLADFGMAK------ 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 189011594 370 anpsQSSTVARTCTVRGTLAYLPEEYIKTGRLAVD--TDTFSFGVVILETLAGQ 421
Cdd:cd06632  151 ----HVEAFSFAKSFKGSPYWMAPEVIMQKNSGYGlaVDIWSLGCTVLEMATGK 200
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
211-414 2.34e-17

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: 82.77  E-value: 2.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 211 NFSEELRIGEGGFGCVYRAVMRNTT--YAVKRL--KEEADLewtvvkQSFLTEVEQLSRF-RHPNIVDFAGycaeSGFY- 284
Cdd:cd13985    1 RYQVTKQLGEGGFSYVYLAHDVNTGrrYALKRMyfNDEEQL------RVAIKEIEIMKRLcGHPNIVQYYD----SAILs 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 285 -------CLVYGFLPnGSLEDQLhlQTQACSPLSWPQRLDILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLMPKLG 357
Cdd:cd13985   71 segrkevLLLMEYCP-GSLVDIL--EKSPPSPLSEEEVLRIFYQICQAVGHLHSQSPPIIHRDIKIENILFSNTGRFKLC 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 358 DFGLARFSRFAGANPSQSSTVARTCTVRGTLAYLPEEYIKT-GRLAVDT--DTFSFGVVI 414
Cdd:cd13985  148 DFGSATTEHYPLERAEEVNIIEEEIQKNTTPMYRAPEMIDLySKKPIGEkaDIWALGCLL 207
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
218-421 2.58e-17

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: 82.65  E-value: 2.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMR--NTTYAVKRL------KEEadlewtvvKQSFLT-EVEQLSRFRHPNIVDFagYCA---ESGFYc 285
Cdd:cd05581    9 LGEGSYSTVVLAKEKetGKEYAIKVLdkrhiiKEK--------KVKYVTiEKEVLSRLAHPGIVKL--YYTfqdESKLY- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 286 LVYGFLPNGSLEDQLHLQT---QACSPLSWPQRLDillgtarAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLA 362
Cdd:cd05581   78 FVLEYAPNGDLLEYIRKYGsldEKCTRFYTAEIVL-------ALEYLH--SKGIIHRDLKPENILLDEDMHIKITDFGTA 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 363 RF--------SRFAGANPSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd05581  149 KVlgpdsspeSTKGDADSQIAYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGK 215
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
212-416 3.51e-17

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


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 82.47  E-value: 3.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELRIGEGGFGCVYRAVMRNTT---YAVKRLKEEADLEWTVVKQsfLTEVE---QLSRFRHPNIVDFAGYCAESGFYC 285
Cdd:cd14052    2 FANVELIGSGEFSQVYKVSERVPTgkvYAVKKLKPNYAGAKDRLRR--LEEVSilrELTLDGHDNIVQLIDSWEYHGHLY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 286 LVYGFLPNGSLEDQLHLQTQAcsplswpQRLD------ILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDF 359
Cdd:cd14052   80 IQTELCENGSLDVFLSELGLL-------GRLDefrvwkILVELSLGLRFIH--DHHFVHLDLKPANVLITFEGTLKIGDF 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 360 GLArfsrfaganpsQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd14052  151 GMA-----------TVWPLIRGIEREGDREYIAPEILSEHMYDKPADIFSLGLILLE 196
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
212-419 3.65e-17

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


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 81.92  E-value: 3.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEElrIGEGGFGCVYRAVMRN-TTYAVKRLKEEADLEwtvvkQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGF 290
Cdd:cd05112    8 FVQE--IGSGQFGLVHLGYWLNkDKVAIKTIREGAMSE-----EDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDqlHLQTQACSpLSWPQRLDILLGTARAIQFLHQDspSLIHGDIKSSNVLLDERLMPKLGDFGLARFSrfagA 370
Cdd:cd05112   81 MEHGCLSD--YLRTQRGL-FSAETLLGMCLDVCEGMAYLEEA--SVIHRDLAARNCLVGENQVVKVSDFGMTRFV----L 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 189011594 371 NPSQSSTVARTCTVRgtlaYLPEEYIKTGRLAVDTDTFSFGVVILETLA 419
Cdd:cd05112  152 DDQYTSSTGTKFPVK----WSSPEVFSFSRYSSKSDVWSFGVLMWEVFS 196
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
221-421 4.82e-17

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: 81.78  E-value: 4.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 221 GGFGCVYRAVMRNTTYAVkrLKeeadlewTVVK--------QSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLP 292
Cdd:cd14027    4 GGFGKVSLCFHRTQGLVV--LK-------TVYTgpnciehnEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYME 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLedqLHLQTQACSPLSWPQR--LDILLGTAraiqFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAGA 370
Cdd:cd14027   75 KGNL---MHVLKKVSVPLSVKGRiiLEIIEGMA----YLHGKG--VIHKDLKPENILVDNDFHIKIADLGLASFKMWSKL 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 371 NPSQS---STVARTC-TVRGTLAYLPEEYIKT--GRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd14027  146 TKEEHneqREVDGTAkKNAGTLYYMAPEHLNDvnAKPTEKSDVYSFAIVLWAIFANK 202
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
218-419 9.40e-17

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 80.86  E-value: 9.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRN----TTYAVKRLKEEADLEwtvVKQSFLTEVEQLSRF-RHPNIVDFAGYCAESGFYCLVYGFLP 292
Cdd:cd05047    3 IGEGNFGQVLKARIKKdglrMDAAIKRMKEYASKD---DHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLEDQLH----LQTQ--------ACSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFG 360
Cdd:cd05047   80 HGNLLDFLRksrvLETDpafaiansTASTLSSQQLLHFAADVARGMDYLSQKQ--FIHRDLAARNILVGENYVAKIADFG 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594 361 LARfsrfaganpsqsstvARTCTVRGTLAYLPEEYIKTGRL-----AVDTDTFSFGVVILETLA 419
Cdd:cd05047  158 LSR---------------GQEVYVKKTMGRLPVRWMAIESLnysvyTTNSDVWSYGVLLWEIVS 206
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
211-421 1.26e-16

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: 81.26  E-value: 1.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 211 NFSEELRIGEGGFGCVYRAvmRNTT----YAVKRLKEEADLEWTVVkqSFLTEVEQLSRFRHPNIVDF----AGYCAESG 282
Cdd:cd07845    8 EFEKLNRIGEGTYGIVYRA--RDTTsgeiVALKKVRMDNERDGIPI--SSLREITLLLNLRHPNIVELkevvVGKHLDSI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 283 FycLVYGFLPN--GSLEDQLHlqtqacSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFG 360
Cdd:cd07845   84 F--LVMEYCEQdlASLLDNMP------TPFSESQVKCLMLQLLRGLQYLHENF--IIHRDLKVSNLLLTDKGCLKIADFG 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594 361 LARfsRFagANPSQSSTvarTCTVrgTLAYLPEEYI---KTGRLAVdtDTFSFGVVILETLAGQ 421
Cdd:cd07845  154 LAR--TY--GLPAKPMT---PKVV--TLWYRAPELLlgcTTYTTAI--DMWAVGCILAELLAHK 206
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
218-416 1.44e-16

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


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 80.00  E-value: 1.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMR--NTTYAVKRLKEEADLewtvvkQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd06612   11 LGEGSYGSVYKAIHKetGQVVAIKVVPVEEDL------QEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYCGAGS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLHLqtqACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfaganpSQS 375
Cdd:cd06612   85 VSDIMKI---TNKTLTEEEIAAILYQTLKGLEYLH--SNKKIHRDIKAGNILLNEEGQAKLADFGVSG---------QLT 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 189011594 376 STVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd06612  151 DTMAKRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIE 191
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
218-362 1.53e-16

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


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 80.63  E-value: 1.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRA--VMRNTTYAVKRL---KEEAdlewtvvKQSFLTEVEQLSRFR-HPNIVDF--AGYCA--ESGFYCLV 287
Cdd:cd14036    8 IAEGGFAFVYEAqdVGTGKEYALKRLlsnEEEK-------NKAIIQEINFMKKLSgHPNIVQFcsAASIGkeESDQGQAE 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594 288 YGFLP---NGSLEDQLHlQTQACSPLSWPQRLDILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLMPKLGDFGLA 362
Cdd:cd14036   81 YLLLTelcKGQLVDFVK-KVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSPPIIHRDLKIENLLIGNQGQIKLCDFGSA 157
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
235-416 1.81e-16

Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 79.90  E-value: 1.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 235 TYAVKRLKEEAdleWTVVKqSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLEDQLhLQTQAcsPLSWPQ 314
Cdd:cd14045   32 TVAIKKIAKKS---FTLSK-RIRKEVKQVRELDHPNLCKFIGGCIEVPNVAIITEYCPKGSLNDVL-LNEDI--PLNWGF 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 315 RLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAGANPSqSSTVARTCTVrgtlaYLPEE 394
Cdd:cd14045  105 RFSFATDIARGMAYLHQHK--IYHGRLKSSNCVIDDRWVCKIADYGLTTYRKEDGSENA-SGYQQRLMQV-----YLPPE 176
                        170       180
                 ....*....|....*....|....
gi 189011594 395 YIKTGRLAVD--TDTFSFGVVILE 416
Cdd:cd14045  177 NHSNTDTEPTqaTDVYSYAIILLE 200
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
218-419 1.86e-16

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 79.66  E-value: 1.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRN-TTYAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGsl 296
Cdd:cd05085    4 LGKGNFGEVYKGTLKDkTPVAVKTCKEDLPQE---LKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGG-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 297 eDQLHLQTQACSPLSWPQRLDILLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfAGANPSQSS 376
Cdd:cd05085   79 -DFLSFLRKKKDELKTKQLVKFSLDAAAGMAYL--ESKNCIHRDLAARNCLVGENNALKISDFGMSR----QEDDGVYSS 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 189011594 377 TVARTCTVRGTlaylPEEYIKTGRLAVDTDTFSFGVVILETLA 419
Cdd:cd05085  152 SGLKQIPIKWT----APEALNYGRYSSESDVWSFGILLWETFS 190
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
212-416 2.04e-16

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: 79.66  E-value: 2.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELRIGEGGFGCVYRAVMRNTT--YAVKRLKEEADLEwtVVKQSFLTEVEQLSRF-RHPNIVDFAGYCAESGfyclvy 288
Cdd:cd14050    3 FTILSKLGEGSFGEVFKVRSREDGklYAVKRSRSRFRGE--KDRKRKLEEVERHEKLgEHPNCVRFIKAWEEKG------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 289 gflpngsledQLHLQTQACSP-----------LSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLG 357
Cdd:cd14050   75 ----------ILYIQTELCDTslqqyceethsLPESEVWNILLDLLKGLKHLH--DHGLIHLDIKPANIFLSKDGVCKLG 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 358 DFGLArfsrfaganpSQSSTVARTCTVRGTLAYLPEEYIKtGRLAVDTDTFSFGVVILE 416
Cdd:cd14050  143 DFGLV----------VELDKEDIHDAQEGDPRYMAPELLQ-GSFTKAADIFSLGITILE 190
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
217-363 2.52e-16

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: 79.83  E-value: 2.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEWtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNg 294
Cdd:cd07829    6 KLGEGTYGVVYKAKDKKTgeIVALKKIRLDNEEEG--IPSTALREISLLKELKHPNIVKLLDVIHTENKLYLVFEYCDQ- 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 295 SLEDQLHLQTqacSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLAR 363
Cdd:cd07829   83 DLKKYLDKRP---GPLPPNLIKSIMYQLLRGLAYCH--SHRILHRDLKPQNLLINRDGVLKLADFGLAR 146
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
217-422 3.63e-16

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 78.80  E-value: 3.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTT-YAVKRLKEEadlewTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYcLVYGFLPNGS 295
Cdd:cd14203    2 KLGQGCFGEVWMGTWNGTTkVAIKTLKPG-----TMSPEAFLEEAQIMKKLRHDKLVQLYAVVSEEPIY-IVTEFMSKGS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDqlHLQTQACSPLSWPQRLDILLGTARAIQFLHQdsPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAGANPSQS 375
Cdd:cd14203   76 LLD--FLKDGEGKYLKLPQLVDMAAQIASGMAYIER--MNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQG 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 189011594 376 STVARTCTVrgtlaylPEEYIkTGRLAVDTDTFSFGVVILETLAGQR 422
Cdd:cd14203  152 AKFPIKWTA-------PEAAL-YGRFTIKSDVWSFGILLTELVTKGR 190
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
217-423 3.78e-16

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: 78.76  E-value: 3.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTTYAVKRLKEEadlewtVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYcLVYGFLPNGSL 296
Cdd:cd05083   13 IIGEGEFGAVLQGEYMGQKVAVKNIKCD------VTAQAFLEETAVMTKLQHKNLVRLLGVILHNGLY-IVMELMSKGNL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 297 EDQLHLQTQACSPLswPQRLDILLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfagANPSQSS 376
Cdd:cd05083   86 VNFLRSRGRALVPV--IQLLQFSLDVAEGMEYL--ESKKLVHRDLAARNILVSEDGVAKISDFGLAK------VGSMGVD 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 189011594 377 tvartcTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRA 423
Cdd:cd05083  156 ------NSRLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGRA 196
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
218-518 6.38e-16

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 78.07  E-value: 6.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVKRLKEEADLEwtVVKQsfltEVEQLSRFRHPNIVDF--AGYCAESgfycLVYGFLPNGS 295
Cdd:cd14068    2 LGDGGFGSVYRAVYRGEDVAVKIFNKHTSFR--LLRQ----ELVVLSHLHHPSLVALlaAGTAPRM----LVMELAPKGS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEdqlHLQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLL-----DERLMPKLGDFGLARFSRFAGA 370
Cdd:cd14068   72 LD---ALLQQDNASLTRTLQHRIALHVADGLRYLH--SAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQYCCRMGI 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 371 NPSQSSTVARTCTV-RGTLAYLPEeyiktgrlavdTDTFSFGVVILETLA-GQRAVrtQGAKtkylkdlIEDEAEEVGVT 448
Cdd:cd14068  147 KTSEGTPGFRAPEVaRGNVIYNQQ-----------ADVYSFGLLLYDILTcGERIV--EGLK-------FPNEFDELAIQ 206
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 449 LKSTQPTlwmgvatdawtapiaaqiykKHLDSRPGPcppqlglALAQLACCCMHRRAKKRPPMTQVYKRL 518
Cdd:cd14068  207 GKLPDPV--------------------KEYGCAPWP-------GVEALIKDCLKENPQCRPTSAQVFDIL 249
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
217-416 7.06e-16

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 78.22  E-value: 7.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTT-YAVKRLKEEadlewTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd05068   15 KLGSGQFGEVWEGLWNNTTpVAVKTLKPG-----TMDPEDFLREAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKHGS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLHLQTQAcspLSWPQRLDILLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFsrFAGANPSQS 375
Cdd:cd05068   90 LLEYLQGKGRS---LQLPQLIDMAAQVASGMAYL--ESQNYIHRDLAARNVLVGENNICKVADFGLARV--IKVEDEYEA 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 189011594 376 STVARTctvrgTLAYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd05068  163 REGAKF-----PIKWTAPEAANYNRFSIKSDVWSFGILLTE 198
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
218-422 7.75e-16

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: 78.42  E-value: 7.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVKRL---------KEEADLEWTVVKQS--------FLTEVEQLSRFRHPNIVDFAGYCAE 280
Cdd:cd14000    2 LGDGGFGSVYRASYKGEPVAVKIFnkhtssnfaNVPADTMLRHLRATdamknfrlLRQELTVLSHLHHPSIVYLLGIGIH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 281 SgfYCLVYGFLPNGSLEDQLHLQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLL-----DERLMPK 355
Cdd:cd14000   82 P--LMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQRIALQVADGLRYLH--SAMIIYRDLKSHNVLVwtlypNSAIIIK 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 356 LGDFGLARFSRFAGANpsqsstvartcTVRGTLAYLPEEyIKTGRLAVD--TDTFSFGVVILETLAGQR 422
Cdd:cd14000  158 IADYGISRQCCRMGAK-----------GSEGTPGFRAPE-IARGNVIYNekVDVFSFGMLLYEILSGGA 214
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
218-393 7.81e-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: 7.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT--YAVK-----RLKEEADlewtvvkQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGF 290
Cdd:cd05117    8 LGRGSFGVVRLAVHKKTGeeYAVKiidkkKLKSEDE-------EMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDQLHlqtqACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMP---KLGDFGLARFSRf 367
Cdd:cd05117   81 CTGGELFDRIV----KKGSFSEREAAKIMKQILSAVAYLH--SQGIVHRDLKPENILLASKDPDspiKIIDFGLAKIFE- 153
                        170       180
                 ....*....|....*....|....*..
gi 189011594 368 agaNPSQSSTVArtctvrGTLAYL-PE 393
Cdd:cd05117  154 ---EGEKLKTVC------GTPYYVaPE 171
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
218-416 8.22e-16

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 78.34  E-value: 8.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVM-------RNTTYAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGF 290
Cdd:cd05050   13 IGQGAFGRVFQARApgllpyePFTMVAVKMLKEEASAD---MQADFQREAALMAEFDHPNIVKLLGVCAVGKPMCLLFEY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDQL-----HLQTQACS-------------PLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERL 352
Cdd:cd05050   90 MAYGDLNEFLrhrspRAQCSLSHstssarkcglnplPLSCTEQLCIAKQVAAGMAYLSERK--FVHRDLATRNCLVGENM 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 353 MPKLGDFGLAR---FSRFAGANPSQSSTVArtctvrgtlaYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd05050  168 VVKIADFGLSRniySADYYKASENDAIPIR----------WMPPESIFYNRYTTESDVWAYGVVLWE 224
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
217-362 1.14e-15

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: 77.35  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTT--YAVKRLKEEADLEWTVVKQsfltEVEQLSRFRHPNIVDFAG---------YCAEsgfYC 285
Cdd:cd06613    7 RIGSGTYGDVYKARNIATGelAAVKVIKLEPGDDFEIIQQ----EISMLKECRHPNIVAYFGsylrrdklwIVME---YC 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 286 lvygflPNGSLEDQLHLQtqacSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLA 362
Cdd:cd06613   80 ------GGGSLQDIYQVT----GPLSELQIAYVCRETLKGLAYLHSTG--KIHRDIKGANILLTEDGDVKLADFGVS 144
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
218-362 1.14e-15

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: 77.59  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEeADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGyCAESGFYclVYGFL---P 292
Cdd:cd14099    9 LGKGGFAKCYEVTDMSTgkVYAGKVVPK-SSLTKPKQREKLKSEIKIHRSLKHPNIVKFHD-CFEDEEN--VYILLelcS 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLEDqLHlqtQACSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLA 362
Cdd:cd14099   85 NGSLME-LL---KRRKALTEPEVRYFMRQILSGVKYLHSNR--IIHRDLKLGNLFLDENMNVKIGDFGLA 148
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
217-418 1.29e-15

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 77.77  E-value: 1.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTT-YAVKRLKEEadlewTVVKQSFLTEVEQLSRFRHPNIVD-FAGYCAESGFYcLVYGFLPNG 294
Cdd:cd05072   14 KLGAGQFGEVWMGYYNNSTkVAVKTLKPG-----TMSVQAFLEEANLMKTLQHDKLVRlYAVVTKEEPIY-IITEYMAKG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEDqlHLQTQACSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFSRfaganpsQ 374
Cdd:cd05072   88 SLLD--FLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKN--YIHRDLRAANVLVSESLMCKIADFGLARVIE-------D 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 189011594 375 SSTVARTcTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETL 418
Cdd:cd05072  157 NEYTARE-GAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIV 199
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
218-419 1.42e-15

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


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 77.17  E-value: 1.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRaVMRNTT---YAVKRLKEEADlewtvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNG 294
Cdd:cd14156    1 IGSGFFSKVYK-VTHGATgkvMVVKIYKNDVD------QHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEDQLhlqTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLdeRLMPK-----LGDFGLAR-FSRFA 368
Cdd:cd14156   74 CLEELL---AREELPLSWREKVELACDISRGMVYLH--SKNIYHRDLNSKNCLI--RVTPRgreavVTDFGLAReVGEMP 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 189011594 369 GANPSqsstvaRTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLA 419
Cdd:cd14156  147 ANDPE------RKLSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEILA 191
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
212-416 1.53e-15

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: 77.41  E-value: 1.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELRIGEGGFGCVYRAvmRNTT----YAVKRLKEEADlewTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLV 287
Cdd:cd14046    8 FEELQVLGKGAFGQVVKV--RNKLdgryYAIKKIKLRSE---SKNNSRILREVMLLSRLNHQHVVRYYQAWIERANLYIQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 288 YGFLPNGSLEDQ----LHLQTQAcsplSWpqRL--DILLGTAraiqflHQDSPSLIHGDIKSSNVLLDERLMPKLGDFGL 361
Cdd:cd14046   83 MEYCEKSTLRDLidsgLFQDTDR----LW--RLfrQILEGLA------YIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGL 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594 362 ARFSRFAGANPSQ---SSTVAR-------TCTVrGTLAYLPEEyIKTGRLAV---DTDTFSFGVVILE 416
Cdd:cd14046  151 ATSNKLNVELATQdinKSTSAAlgssgdlTGNV-GTALYVAPE-VQSGTKSTyneKVDMYSLGIIFFE 216
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
218-418 2.03e-15

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: 77.22  E-value: 2.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRA--VMRNTTYAVKRLKEeADLEwtVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGfyclvygflPNGS 295
Cdd:cd14048   14 LGRGGFGVVFEAknKVDDCNYAVKRIRL-PNNE--LAREKVLREVRALAKLDHPGIVRYFNAWLERP---------PEGW 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQ----LHLQTQACSPLS---WPQR------------LDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKL 356
Cdd:cd14048   82 QEKMdevyLYIQMQLCRKENlkdWMNRrctmesrelfvcLNIFKQIASAVEYLH--SKGLIHRDLKPSNVFFSLDDVVKV 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 357 GDFGLARFS-----RFAGANPSQSStvARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETL 418
Cdd:cd14048  160 GDFGLVTAMdqgepEQTVLTPMPAY--AKHTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI 224
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
204-419 2.07e-15

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 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: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 77.37  E-value: 2.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 204 EISQGTCNFSEELriGEGGFGCVYRAVMRNTT-------YAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAG 276
Cdd:cd05091    2 EINLSAVRFMEEL--GEDRFGKVYKGHLFGTApgeqtqaVAIKTLKDKAEGP---LREEFRHEAMLRSRLQHPNIVCLLG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 277 YCAESGFYCLVYGFLPNGSLEDQLHLQTQAC------------SPLSWPQRLDILLGTARAIQFLhqDSPSLIHGDIKSS 344
Cdd:cd05091   77 VVTKEQPMSMIFSYCSHGDLHEFLVMRSPHSdvgstdddktvkSTLEPADFLHIVTQIAAGMEYL--SSHHVVHKDLATR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 345 NVLLDERLMPKLGDFGLAR------FSRFAGANPSqsstvartctvrgTLAYLPEEYIKTGRLAVDTDTFSFGVVILETL 418
Cdd:cd05091  155 NVLVFDKLNVKISDLGLFRevyaadYYKLMGNSLL-------------PIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVF 221

                 .
gi 189011594 419 A 419
Cdd:cd05091  222 S 222
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
218-519 2.31e-15

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 76.56  E-value: 2.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVKRLKEEAdlewtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAE--SGFYcLVYGFLPNGS 295
Cdd:cd05082   14 IGKGEFGDVMLGDYRGNKVAVKCIKNDA------TAQAFLAEASVMTQLRHSNLVQLLGVIVEekGGLY-IVTEYMAKGS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDqlHLQTQACSPLSWPQRLDILLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfaganpsQS 375
Cdd:cd05082   87 LVD--YLRSRGRSVLGGDCLLKFSLDVCEAMEYL--EGNNFVHRDLAARNVLVSEDNVAKVSDFGLTK----------EA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 376 STVARTCTVrgTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQgaktkylkdliedeaeevgVTLKSTQPT 455
Cdd:cd05082  153 SSTQDTGKL--PVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPR-------------------IPLKDVVPR 211
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594 456 LWMGVATDAwtapiaaqiykkhldsrPGPCPPQLGLALAQlaccCMHRRAKKRPPMTQVYKRLE 519
Cdd:cd05082  212 VEKGYKMDA-----------------PDGCPPAVYDVMKN----CWHLDAAMRPSFLQLREQLE 254
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
215-519 3.01e-15

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 76.65  E-value: 3.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 215 ELRIGEGGFGCVYRAVMRNTT-YAVKRLKEEadlewTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYcLVYGFLPN 293
Cdd:cd05071   14 EVKLGQGCFGEVWMGTWNGTTrVAIKTLKPG-----TMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIY-IVTEYMSK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 294 GSLEDqlHLQTQACSPLSWPQRLDILLGTARAIQFLHQdsPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAGANPS 373
Cdd:cd05071   88 GSLLD--FLKGEMGKYLRLPQLVDMAAQIASGMAYVER--MNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTAR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 374 QSSTVARTCTVRGTLAYlpeeyiktGRLAVDTDTFSFGVVILEtLAGQRAVRTQGAKTKYLKDLIEdeaeevgvtlkstq 453
Cdd:cd05071  164 QGAKFPIKWTAPEAALY--------GRFTIKSDVWSFGILLTE-LTTKGRVPYPGMVNREVLDQVE-------------- 220
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189011594 454 ptlwmgvatdawtapiaaQIYKKhldsrpgPCPPQLGLALAQLACCCMHRRAKKRPPMTQVYKRLE 519
Cdd:cd05071  221 ------------------RGYRM-------PCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLE 261
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
218-422 3.28e-15

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 76.26  E-value: 3.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT-----TYAVKRLKEEA-DLEWTvvkqSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFL 291
Cdd:cd05033   12 IGGGEFGEVCSGSLKLPgkkeiDVAIKTLKSGYsDKQRL----DFLTEASIMGQFDHPNVIRLEGVVTKSRPVMIVTEYM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 PNGSLEDQLHLQTQAcspLSWPQRLDILLGTARAIQFLHQdsPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAGAn 371
Cdd:cd05033   88 ENGSLDKFLRENDGK---FTVTQLVGMLRGIASGMKYLSE--MNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDSEA- 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 372 psqsstvarTCTVRG---TLAYLPEEYIKTGRLAVDTDTFSFGVVILETLA-GQR 422
Cdd:cd05033  162 ---------TYTTKGgkiPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSyGER 207
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
218-421 3.41e-15

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: 76.02  E-value: 3.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEWTVVKQSFlTEVEQLSRFRHPNIVDFagYCA--ESGFYCLVYGFLPN 293
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTgkLYAMKVLRKKEIIKRKEVEHTL-NERNILERVNHPFIVKL--HYAfqTEEKLYLVLDYVPG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 294 GSLEDqlHLQTQACSPLSWPQRL--DILLgtarAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSrfagan 371
Cdd:cd05123   78 GELFS--HLSKEGRFPEERARFYaaEIVL----ALEYLH--SLGIIYRDLKPENILLDSDGHIKLTDFGLAKEL------ 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 189011594 372 psqSSTVARTCTVRGTLAYL-PE-----EYIKtgrlAVdtDTFSFGVVILETLAGQ 421
Cdd:cd05123  144 ---SSDGDRTYTFCGTPEYLaPEvllgkGYGK----AV--DWWSLGVLLYEMLTGK 190
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
218-362 4.17e-15

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


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 76.32  E-value: 4.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTY--AVKR--LKEEADLEwtvvkqSFLTEVEQLSRFRHPNIVDF-AGYCAESGFYCLVYgFLP 292
Cdd:cd06611   13 LGDGAFGKVYKAQHKETGLfaAAKIiqIESEEELE------DFMVEIDILSECKHPNIVGLyEAYFYENKLWILIE-FCD 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLeDQLHLQTQAcsPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLA 362
Cdd:cd06611   86 GGAL-DSIMLELER--GLTEPQIRYVCRQMLEALNFLH--SHKVIHRDLKAGNILLTLDGDVKLADFGVS 150
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
218-416 4.22e-15

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


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 76.27  E-value: 4.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRA---VMRNTTY---AVKRLKEEADlewTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFY--CLVYG 289
Cdd:cd05038   12 LGEGHFGSVELCrydPLGDNTGeqvAVKSLQPSGE---EQHMSDFKREIEILRTLDHEYIVKYKGVCESPGRRslRLIME 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLEDqlHLQTQAcSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARF----- 364
Cdd:cd05038   89 YLPSGSLRD--YLQRHR-DQIDLKRLLLFASQICKGMEYLG--SQRYIHRDLAARNILVESEDLVKISDFGLAKVlpedk 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 189011594 365 SRFAGANPSQSStvartctvrgTLAYLPEEyIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd05038  164 EYYYVKEPGESP----------IFWYAPEC-LRESRFSSASDVWSFGVTLYE 204
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
218-419 5.56e-15

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 76.19  E-value: 5.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRN----TTYAVKRLKEEADLEwtvVKQSFLTEVEQLSRF-RHPNIVDFAGYCAESGFYCLVYGFLP 292
Cdd:cd05089   10 IGEGNFGQVIKAMIKKdglkMNAAIKMLKEFASEN---DHRDFAGELEVLCKLgHHPNIINLLGACENRGYLYIAIEYAP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLEDQLH----LQTQ--------ACSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFG 360
Cdd:cd05089   87 YGNLLDFLRksrvLETDpafakehgTASTLTSQQLLQFASDVAKGMQYLSEKQ--FIHRDLAARNVLVGENLVSKIADFG 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594 361 LARfsrfaganpsqsstvARTCTVRGTLAYLPEEYIKTGRL-----AVDTDTFSFGVVILETLA 419
Cdd:cd05089  165 LSR---------------GEEVYVKKTMGRLPVRWMAIESLnysvyTTKSDVWSFGVLLWEIVS 213
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
217-421 5.92e-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: 75.35  E-value: 5.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRA--VMRNTTYAVKRLKEEadlewTVVKQSFLTEVEQLSRFR----HPNIV----DFagYCAESGFYCL 286
Cdd:cd05118    6 KIGEGAFGTVWLArdKVTGEKVAIKKIKND-----FRHPKAALREIKLLKHLNdvegHPNIVklldVF--EHRGGNHLCL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 287 VYGFLPngslEDQLHLQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERL-MPKLGDFGLARFS 365
Cdd:cd05118   79 VFELMG----MNLYELIKDYPRGLPLDLIKSYLYQLLQALDFLH--SNGIIHRDLKPENILINLELgQLKLADFGLARSF 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 366 RfagaNPSQSSTVArtctvrgTLAYL-PEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd05118  153 T----SPPYTPYVA-------TRWYRaPEVLLGAKPYGSSIDIWSLGCILAELLTGR 198
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
218-413 6.50e-15

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: 75.25  E-value: 6.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRL-KEEADLEWTV-VKQsfltEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPN 293
Cdd:cd14003    8 LGEGSFGKVKLARHKLTgeKVAIKIIdKSKLKEEIEEkIKR----EIEIMKLLNHPNIIKLYEVIETENKIYLVMEYASG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 294 GSLEDQLHlqtqacsplswpQRLDILLGTAR--------AIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFS 365
Cdd:cd14003   84 GELFDYIV------------NNGRLSEDEARrffqqlisAVDYCH--SNGIVHRDLKLENILLDKNGNLKIIDFGLSNEF 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 189011594 366 RfaganpsQSSTVARTCtvrGTLAYLPEEYIK-TGRLAVDTDTFSFGVV 413
Cdd:cd14003  150 R-------GGSLLKTFC---GTPAYAAPEVLLgRKYDGPKADVWSLGVI 188
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
212-416 7.08e-15

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: 75.15  E-value: 7.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELRIGEGGFGcvyravmrnTTYAVKRLKEEADLEWTVVKQSF------------LTEVEQLSRFRHPNIVDFAGYCA 279
Cdd:cd08222    2 YRVVRKLGSGNFG---------TVYLVSDLKATADEELKVLKEISvgelqpdetvdaNREAKLLSKLDHPAIVKFHDSFV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 280 ESGFYCLVYGFLPNGSLEDQLHLQTQACSPLSWPQRLDILLGTARAIQFLHQDspSLIHGDIKSSNVLLDERLMpKLGDF 359
Cdd:cd08222   73 EKESFCIVTEYCEGGDLDDKISEYKKSGTTIDENQILDWFIQLLLAVQYMHER--RILHRDLKAKNIFLKNNVI-KVGDF 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 360 GLARFSrfaganpSQSSTVARTCTvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd08222  150 GISRIL-------MGTSDLATTFT--GTPYYMSPEVLKHEGYNSKSDIWSLGCILYE 197
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
217-418 7.27e-15

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 75.77  E-value: 7.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTTYAVKRL--KEEadlewtvvkQSFLTEVE--QLSRFRHPNIVDF-------AGYCAEsgfYC 285
Cdd:cd14056    2 TIGKGRYGEVWLGKYRGEKVAVKIFssRDE---------DSWFRETEiyQTVMLRHENILGFiaadiksTGSWTQ---LW 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 286 LVYGFLPNGSLEDQLHLQTqacspLSWPQRLDILLGTARAIQFLH------QDSPSLIHGDIKSSNVLLDERLMPKLGDF 359
Cdd:cd14056   70 LITEYHEHGSLYDYLQRNT-----LDTEEALRLAYSAASGLAHLHteivgtQGKPAIAHRDLKSKNILVKRDGTCCIADL 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594 360 GLA-RFSrfaganpSQSSTVARTCTVR-GTLAYLPEEYIkTGRLAVD-------TDTFSFGVVILETL 418
Cdd:cd14056  145 GLAvRYD-------SDTNTIDIPPNPRvGTKRYMAPEVL-DDSINPKsfesfkmADIYSFGLVLWEIA 204
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
217-362 8.18e-15

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 75.49  E-value: 8.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMR------NTTYAVKRLKEEADLEWTVVKQSFlteveQLSRFRHPNIVDFagYCAE---SGF---Y 284
Cdd:cd14055    2 LVGKGRFAEVWKAKLKqnasgqYETVAVKIFPYEEYASWKNEKDIF-----TDASLKHENILQF--LTAEergVGLdrqY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 285 CLVYGFLPNGSLEDQLhlqtqACSPLSWPQRLDILLGTARAIQFLHQDSPS-------LIHGDIKSSNVLLDERLMPKLG 357
Cdd:cd14055   75 WLITAYHENGSLQDYL-----TRHILSWEDLCKMAGSLARGLAHLHSDRTPcgrpkipIAHRDLKSSNILVKNDGTCVLA 149

                 ....*
gi 189011594 358 DFGLA 362
Cdd:cd14055  150 DFGLA 154
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
218-364 8.27e-15

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: 75.68  E-value: 8.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEADlewtvvKQSF----LTEVEQLSRFRHPNIVDF------AGYCAESGFYC 285
Cdd:cd07840    7 IGEGTYGQVYKARNKKTgeLVALKKIRMENE------KEGFpitaIREIKLLQKLDHPNVVRLkeivtsKGSAKYKGSIY 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 286 LVYGFLPNgsleDQLHLQTQACSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARF 364
Cdd:cd07840   81 MVFEYMDH----DLTGLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNG--ILHRDIKGSNILINNDGVLKLADFGLARP 153
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
218-421 9.52e-15

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: 74.57  E-value: 9.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMR--NTTYAVKRLKEEadlewTVVK---QSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLP 292
Cdd:cd14009    1 IGRGSFATVWKGRHKqtGEVVAIKEISRK-----KLNKklqENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLEDQLHLQtqacSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLL---DERLMPKLGDFGLARFsrfag 369
Cdd:cd14009   76 GGDLSQYIRKR----GRLPEAVARHFMQQLASGLKFLR--SKNIIHRDLKPQNLLLstsGDDPVLKIADFGFARS----- 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 189011594 370 anpSQSSTVARtcTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd14009  145 ---LQPASMAE--TLCGSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGK 191
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
218-421 1.01e-14

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: 74.60  E-value: 1.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAV------KRLKEEADLewtvvkQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFL 291
Cdd:cd14002    9 IGEGSFGKVYKGRRKYTGQVValkfipKRGKSEKEL------RNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEYA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 P---------NGSL-EDQlhLQTQACSPLSwpqrldillgtarAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGL 361
Cdd:cd14002   83 QgelfqiledDGTLpEEE--VRSIAKQLVS-------------ALHYLH--SNRIIHRDMKPQNILIGKGGVVKLCDFGF 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 362 ARfsrfagaNPSQSSTVARtcTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd14002  146 AR-------AMSCNTLVLT--SIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQ 196
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
217-420 1.29e-14

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: 74.43  E-value: 1.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNG 294
Cdd:cd14098    7 RLGSGTFAEVKKAVEVETgkMRAIKQIVKRKVAGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVMEYVEGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEDQL----HLQTQACSPLSwpqrLDILlgtaRAIQFLHqdSPSLIHGDIKSSNVLL--DERLMPKLGDFGLARFsrfa 368
Cdd:cd14098   87 DLMDFImawgAIPEQHARELT----KQIL----EAMAYTH--SMGITHRDLKPENILItqDDPVIVKISDFGLAKV---- 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 369 ganpSQSSTVART-CtvrGTLAYLPEEYIKTGRLAVD------TDTFSFGVVILETLAG 420
Cdd:cd14098  153 ----IHTGTFLVTfC---GTMAYLAPEILMSKEQNLQggysnlVDMWSVGCLVYVMLTG 204
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
218-412 1.36e-14

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


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 74.63  E-value: 1.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT--YAVKRLKEEADLEWTVVKQsfltEVEQLSRFR-HPNIVDFAGYCA----ESGFYCLVY-G 289
Cdd:cd14037   11 LAEGGFAHVYLVKTSNGGnrAALKRVYVNDEHDLNVCKR----EIEIMKRLSgHKNIVGYIDSSAnrsgNGVYEVLLLmE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLEDQL--HLQTQacspLSWPQRLDILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRF 367
Cdd:cd14037   87 YCKGGGVIDLMnqRLQTG----LTESEILKIFCDVCEAVAAMHYLKPPLIHRDLKVENVLISDSGNYKLCDFGSATTKIL 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 189011594 368 AGANPSQSSTVARTCTVRGTLAYLPEEYIKT-GRLAVDT--DTFSFGV 412
Cdd:cd14037  163 PPQTKQGVTYVEEDIKKYTTLQYRAPEMIDLyRGKPITEksDIWALGC 210
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
159-421 1.59e-14

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 75.63  E-value: 1.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 159 LQVPLSD-SLGPPLQSSAPSSIKPSPESPVSGLQRARPSPfcwPFCEISQGTcnfseelRIGEGGFGCVYRAVMRNTT-- 235
Cdd:PLN00034  32 LPLPQRDpSLAVPLPLPPPSSSSSSSSSSSASGSAPSAAK---SLSELERVN-------RIGSGAGGTVYKVIHRPTGrl 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 236 YAVKRLKEEADlewTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLEDQLHLQTQACSPLSwpqr 315
Cdd:PLN00034 102 YALKVIYGNHE---DTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLEGTHIADEQFLADVA---- 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 316 LDILLGtaraIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFSRfAGANPSQSSTvartctvrGTLAYLPEEY 395
Cdd:PLN00034 175 RQILSG----IAYLHRRH--IVHRDIKPSNLLINSAKNVKIADFGVSRILA-QTMDPCNSSV--------GTIAYMSPER 239
                        250       260       270
                 ....*....|....*....|....*....|.
gi 189011594 396 IKT----GRL-AVDTDTFSFGVVILETLAGQ 421
Cdd:PLN00034 240 INTdlnhGAYdGYAGDIWSLGVSILEFYLGR 270
Death_IRAK2 cd08795
Death domain of Interleukin 1 Receptor Associated Kinase-2; Death Domain (DD) of Interleukin-1 ...
18-99 2.03e-14

Death domain of Interleukin 1 Receptor Associated Kinase-2; Death Domain (DD) of Interleukin-1 Receptor-Associated Kinase 1 (IRAK1). IRAKs are essential components of innate immunity and inflammation in mammals and other vertebrates. They are involved in signal transduction pathways involving IL-1 and IL-18 receptors, Toll-like receptors (TLRs), nuclear factor-kappaB (NF-kB), and mitogen-activated protein kinases (MAPKs). IRAKs contain an N-terminal DD domain and a C-terminal kinase domain. IRAK2 is an essential component of several signaling pathways, including NF-kappaB and the IL-1 signaling pathways. It is an inactive kinase that participates in septic shock mediated by TLR4 and TLR9. It plays a redundant role with IRAK1 in early NF-kB and MAPK responses, and remains present at later stages whereas IRAK1 disappears. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 176773  Cd Length: 88  Bit Score: 69.18  E-value: 2.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594  18 FLYEVPPWVMCRFYKVMDALEPADWCQFAALIVRDQTELRLCERSEQRTASV----LWPWINRNARVADLVHILTHLQLL 93
Cdd:cd08795    2 YVYQLPAWVLDDFCRNMDALSDWDWMRFASYVITDQTQLRKIKSMEWTGVSItrelMWWWGMRLATVQQLVDLLQRLELY 81

                 ....*.
gi 189011594  94 RARDII 99
Cdd:cd08795   82 RAAQII 87
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
218-419 2.07e-14

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 74.65  E-value: 2.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRN----TTYAVKRLKEEADLEwtvVKQSFLTEVEQLSRF-RHPNIVDFAGYCAESGFYCLVYGFLP 292
Cdd:cd05088   15 IGEGNFGQVLKARIKKdglrMDAAIKRMKEYASKD---DHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLEDQLH----LQT--------QACSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFG 360
Cdd:cd05088   92 HGNLLDFLRksrvLETdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQ--FIHRDLAARNILVGENYVAKIADFG 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594 361 LARfsrfaganpsqsstvARTCTVRGTLAYLPEEYIKTGRL-----AVDTDTFSFGVVILETLA 419
Cdd:cd05088  170 LSR---------------GQEVYVKKTMGRLPVRWMAIESLnysvyTTNSDVWSYGVLLWEIVS 218
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
204-419 2.15e-14

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 74.28  E-value: 2.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 204 EISQGTCNFSEELriGEGGFGCVYRAVM------RNTTYAVKRLKEEADLE-WTvvkqSFLTEVEQLSRFRHPNIVDFAG 276
Cdd:cd05090    1 ELPLSAVRFMEEL--GECAFGKIYKGHLylpgmdHAQLVAIKTLKDYNNPQqWN----EFQQEASLMTELHHPNIVCLLG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 277 YCAESGFYCLVYGFLPNGSLEDQLHLQTQ----ACSP---------LSWPQRLDILLGTARAIQFLhqDSPSLIHGDIKS 343
Cdd:cd05090   75 VVTQEQPVCMLFEFMNQGDLHEFLIMRSPhsdvGCSSdedgtvkssLDHGDFLHIAIQIAAGMEYL--SSHFFVHKDLAA 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189011594 344 SNVLLDERLMPKLGDFGLARFSRFAGANPSQSSTVArtctvrgTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLA 419
Cdd:cd05090  153 RNILVGEQLHVKISDLGLSREIYSSDYYRVQNKSLL-------PIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFS 221
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
217-432 2.22e-14

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: 73.92  E-value: 2.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTTyAVK-----RLKEEADlewtvvkQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFL 291
Cdd:cd14063    7 VIGKGRFGRVHRGRWHGDV-AIKllnidYLNEEQL-------EAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSLC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 PNGSLEDQLHLQTqacSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDE-RLMpkLGDFGLARFSRFAGA 370
Cdd:cd14063   79 KGRTLYSLIHERK---EKFDFNKTVQIAQQICQGMGYLH--AKGIIHKDLKSKNIFLENgRVV--ITDFGLFSLSGLLQP 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 371 NpsqsstvARTCT---VRGTLAYLPEEYIKTGRLAVD----------TDTFSFGVVILETLAGQRAVRTQGAKTK 432
Cdd:cd14063  152 G-------RREDTlviPNGWLCYLAPEIIRALSPDLDfeeslpftkaSDVYAFGTVWYELLAGRWPFKEQPAESI 219
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
218-416 2.45e-14

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: 73.64  E-value: 2.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTY-AVKRLKEEADLEwtvvkQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSL 296
Cdd:cd05059   12 LGSGQFGVVHLGKWRGKIDvAIKMIKEGSMSE-----DDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMANGCL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 297 EDQLHLQTQAcspLSWPQRLDILLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSrfagANPSQSS 376
Cdd:cd05059   87 LNYLRERRGK---FQTEQLLEMCKDVCEAMEYL--ESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYV----LDDEYTS 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 189011594 377 TVARTCTVRgtlaYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd05059  158 SVGTKFPVK----WSPPEVFMYSKFSSKSDVWSFGVLMWE 193
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
218-481 2.48e-14

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: 74.57  E-value: 2.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT--YAVKRLKEEA-----DLEWTVVKQSFLTEVeqlsrFRHPNIVDFagYCA----ESGFYCL 286
Cdd:cd05619   13 LGKGSFGKVFLAELKGTNqfFAIKALKKDVvlmddDVECTMVEKRVLSLA-----WEHPFLTHL--FCTfqtkENLFFVM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 287 VYgfLPNGSLedQLHLQTqaCSPLSWPQRL----DILLGtaraIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLA 362
Cdd:cd05619   86 EY--LNGGDL--MFHIQS--CHKFDLPRATfyaaEIICG----LQFLH--SKGIVYRDLKLDNILLDKDGHIKIADFGMC 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 363 RFSRFAGAnpsqsstvaRTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAK---------TKY 433
Cdd:cd05619  154 KENMLGDA---------KTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEelfqsirmdNPF 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 189011594 434 LKDLIEDEAEEVGVTLKSTQPTLWMGVATDAWTAPIAAQIYKKHLDSR 481
Cdd:cd05619  225 YPRWLEKEAKDILVKLFVREPERRLGVRGDIRQHPFFREINWEALEER 272
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
217-416 2.68e-14

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 73.38  E-value: 2.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTT-YAVKRLKEEadlewTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYcLVYGFLPNGS 295
Cdd:cd05067   14 RLGAGQFGEVWMGYYNGHTkVAIKSLKQG-----SMSPDAFLAEANLMKQLQHQRLVRLYAVVTQEPIY-IITEYMENGS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDqlHLQTQACSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFSRfaganpsQS 375
Cdd:cd05067   88 LVD--FLKTPSGIKLTINKLLDMAAQIAEGMAFIEERN--YIHRDLRAANILVSDTLSCKIADFGLARLIE-------DN 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 189011594 376 STVARTcTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd05067  157 EYTARE-GAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTE 196
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
217-416 2.73e-14

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 73.61  E-value: 2.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMR--NTTYAVKRLKEEadlewTVVKQSFLTEVEQLSRFRHPNIVDFAGYCA-ESGFYcLVYGFLPN 293
Cdd:cd05052   13 KLGGGQYGEVYEGVWKkyNLTVAVKTLKED-----TMEVEEFLKEAAVMKEIKHPNLVQLLGVCTrEPPFY-IITEFMPY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 294 GSLEDQLhlqtQACSPLSWPQRLDILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAGANPS 373
Cdd:cd05052   87 GNLLDYL----RECNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAH 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 189011594 374 QSSTVARTCTVRGTLAYlpeeyiktGRLAVDTDTFSFGVVILE 416
Cdd:cd05052  163 AGAKFPIKWTAPESLAY--------NKFSIKSDVWAFGVLLWE 197
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
211-420 2.83e-14

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: 73.19  E-value: 2.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 211 NFSEELRIGEGGFGCVYRaVMR---NTTYAVKR--LKEEADLEwtvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYC 285
Cdd:cd08530    1 DFKVLKKLGKGSYGSVYK-VKRlsdNQVYALKEvnLGSLSQKE----REDSVNEIRLLASVNHPNIIRYKEAFLDGNRLC 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 286 LVYGFLPNGSLEDQLHLQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFS 365
Cdd:cd08530   76 IVMEYAPFGDLSKLISKRKKKRRLFPEDDIWRIFIQMLRGLKALH--DQKILHRDLKSANILLSAGDLVKIGDLGISKVL 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 366 RFAGANpsqsstvartcTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd08530  154 KKNLAK-----------TQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATF 197
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
221-477 2.87e-14

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2a (or ActRIIA) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 73.92  E-value: 2.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 221 GGFGCVYRAVMRNTTYAVKRLKEEADLEWtvvKQSFltEVEQLSRFRHPNIVDFAGyCAESGFYC-----LVYGFLPNGS 295
Cdd:cd14141    6 GRFGCVWKAQLLNEYVAVKIFPIQDKLSW---QNEY--EIYSLPGMKHENILQFIG-AEKRGTNLdvdlwLITAFHEKGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLHLQTqacspLSWPQRLDILLGTARAIQFLHQD--------SPSLIHGDIKSSNVLLDERLMPKLGDFGLA-RFSr 366
Cdd:cd14141   80 LTDYLKANV-----VSWNELCHIAQTMARGLAYLHEDipglkdghKPAIAHRDIKSKNVLLKNNLTACIADFGLAlKFE- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 367 fagANPSQSSTVARTCTVRGTLAYLPEEYIKTGRLA-VDTDTFSFGVVILETLAgqRAVRTQGAKTKYLKDLiedeAEEV 445
Cdd:cd14141  154 ---AGKSAGDTHGQVGTRRYMAPEVLEGAINFQRDAfLRIDMYAMGLVLWELAS--RCTASDGPVDEYMLPF----EEEV 224
                        250       260       270
                 ....*....|....*....|....*....|....
gi 189011594 446 GvtlksTQPTL--WMGVATDAWTAPIAAQIYKKH 477
Cdd:cd14141  225 G-----QHPSLedMQEVVVHKKKRPVLRECWQKH 253
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
218-421 3.12e-14

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


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 73.44  E-value: 3.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRaVMRNTTYAVKRLKE--EADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd14222    1 LGKGFFGQAIK-VTHKATGKVMVMKEliRCDEE---TQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLhlqtQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARF--SRFAGANPS 373
Cdd:cd14222   77 LKDFL----RADDPFPWQQKVSFAKGIASGMAYLH--SMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLivEEKKKPPPD 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 374 QSSTVARTC---------TVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLaGQ 421
Cdd:cd14222  151 KPTTKKRTLrkndrkkryTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEII-GQ 206
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
218-416 3.44e-14

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: 73.11  E-value: 3.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFgCVYRAVMR-----NTTYAVKRLKEEADLEWTV-VKQSFLTEVEQLSRFRHPNIVDFAGYC-AESGFYCLVYGF 290
Cdd:cd13994    1 IGKGAT-SVVRIVTKknprsGVLYAVKEYRRRDDESKRKdYVKRLTSEYIISSKLHHPNIVKVLDLCqDLHGKWCLVMEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDQLHlQTQACSPLswpQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAga 370
Cdd:cd13994   80 CPGGDLFTLIE-KADSLSLE---EKDCFFKQILRGVAYLH--SHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFGMP-- 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 189011594 371 npsQSSTVARTCTVRGTLAYL-PEEYIK---TGRLAvdtDTFSFGVVILE 416
Cdd:cd13994  152 ---AEKESPMSAGLCGSEPYMaPEVFTSgsyDGRAV---DVWSCGIVLFA 195
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
204-518 3.47e-14

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 73.82  E-value: 3.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 204 EISQGTCNFSEELriGEGGFGCVYRAVMRNTT------------------YAVKRLKEEADLEwtvVKQSFLTEVEQLSR 265
Cdd:cd05096    1 KFPRGHLLFKEKL--GEGQFGEVHLCEVVNPQdlptlqfpfnvrkgrpllVAVKILRPDANKN---ARNDFLKEVKILSR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 266 FRHPNIVDFAGYCAESGFYCLVYGFLPNGSLEDQL---HLQTQA-----------CSP-LSWPQRLDILLGTARAIQFLh 330
Cdd:cd05096   76 LKDPNIIRLLGVCVDEDPLCMITEYMENGDLNQFLsshHLDDKEengndavppahCLPaISYSSLLHVALQIASGMKYL- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 331 qDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfSRFAGANPS-QSSTVArtctvrgTLAYLPEEYIKTGRLAVDTDTFS 409
Cdd:cd05096  155 -SSLNFVHRDLATRNCLVGENLTIKIADFGMSR-NLYAGDYYRiQGRAVL-------PIRWMAWECILMGKFTTASDVWA 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 410 FGVVILETLAgqrAVRTQGAKTKYLKDLIEDEAEevgvtlkstqptlwmgVATDAwtapiAAQIYKkhldSRPGPCPPql 489
Cdd:cd05096  226 FGVTLWEILM---LCKEQPYGELTDEQVIENAGE----------------FFRDQ-----GRQVYL----FRPPPCPQ-- 275
                        330       340
                 ....*....|....*....|....*....
gi 189011594 490 glALAQLACCCMHRRAKKRPPMTQVYKRL 518
Cdd:cd05096  276 --GLYELMLQCWSRDCRERPSFSDIHAFL 302
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
218-416 3.62e-14

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: 73.07  E-value: 3.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAvmRNTTYAVKRLKEEADLEWTVV--KQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd08225    8 IGEGSFGKIYLA--KAKSDSEHCVIKEIDLTKMPVkeKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYCDGGD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLHLQTQACspLSWPQRLDILLGTARAIQFLHQDspSLIHGDIKSSNVLLDERLM-PKLGDFGLARfsrfagaNPSQ 374
Cdd:cd08225   86 LMKRINRQRGVL--FSEDQILSWFVQISLGLKHIHDR--KILHRDIKSQNIFLSKNGMvAKLGDFGIAR-------QLND 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 189011594 375 SSTVARTCTvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd08225  155 SMELAYTCV--GTPYYLSPEICQNRPYNNKTDIWSLGCVLYE 194
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
217-413 4.12e-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: 72.99  E-value: 4.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTTY----AVK---RLKEEADLewtvvKQSFLT-EVEQLSRFRHPNIVDFAGYCAESGFYCLVY 288
Cdd:cd14080    7 TIGEGSYSKVKLAEYTKSGLkekvACKiidKKKAPKDF-----LEKFLPrELEILRKLRHPNIIQVYSIFERGSKVFIFM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 289 GFLPNGSLedqlhLQ-TQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRf 367
Cdd:cd14080   82 EYAEHGDL-----LEyIQKRGALSESQARIWFRQLALAVQYLH--SLDIAHRDLKCENILLDSNNNVKLSDFGFARLCP- 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 189011594 368 aganPSQSSTVART-CtvrGTLAYLPEEYIKT----GRLAvdtDTFSFGVV 413
Cdd:cd14080  154 ----DDDGDVLSKTfC---GSAAYAAPEILQGipydPKKY---DIWSLGVI 194
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
221-424 4.61e-14

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2b (or ActRIIB) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 73.53  E-value: 4.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 221 GGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQSFLTeveqlSRFRHPNIVDFA-----GYCAESGFYcLVYGFLPNGS 295
Cdd:cd14140    6 GRFGCVWKAQLMNEYVAVKIFPIQDKQSWQSEREIFST-----PGMKHENLLQFIaaekrGSNLEMELW-LITAFHDKGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLHlqtqaCSPLSWPQRLDILLGTARAIQFLHQD---------SPSLIHGDIKSSNVLLDERLMPKLGDFGLArfSR 366
Cdd:cd14140   80 LTDYLK-----GNIVSWNELCHIAETMARGLSYLHEDvprckgeghKPAIAHRDFKSKNVLLKNDLTAVLADFGLA--VR 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594 367 FAGANPSqsstvARTCTVRGTLAYLPEEYIKtGRLAVDTDTF------SFGVVILETLAGQRAV 424
Cdd:cd14140  153 FEPGKPP-----GDTHGQVGTRRYMAPEVLE-GAINFQRDSFlridmyAMGLVLWELVSRCKAA 210
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
218-422 4.72e-14

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: 72.67  E-value: 4.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVyRAVMRNTT---YAVKRLKEEADLEWTVVkQSFLTEVEQLSRFRHPNIVDF-AGYCAESGFYcLVYGFLPN 293
Cdd:cd05578    8 IGKGSFGKV-CIVQKKDTkkmFAMKYMNKQKCIEKDSV-RNVLNELEILQELEHPFLVNLwYSFQDEEDMY-MVVDLLLG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 294 GSLedQLHLQTQAcsPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRfaganPS 373
Cdd:cd05578   85 GDL--RYHLQQKV--KFSEETVKFYICEIVLALDYLH--SKNIIHRDIKPDNILLDEQGHVHITDFNIATKLT-----DG 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 189011594 374 QSSTvartcTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQR 422
Cdd:cd05578  154 TLAT-----STSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKR 197
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
218-421 5.48e-14

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: 72.75  E-value: 5.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRL-KEEADLEWtvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNG 294
Cdd:cd14069    9 LGEGAFGEVFLAVNRNTeeAVAVKFVdMKRAPGDC---PENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYASGG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEDQLHLQTQACSPLSwpQR-LDILLGtarAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLArfSRFAGANPS 373
Cdd:cd14069   86 ELFDKIEPDVGMPEDVA--QFyFQQLMA---GLKYLH--SCGITHRDIKPENLLLDENDNLKISDFGLA--TVFRYKGKE 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 189011594 374 QSSTVArtctvRGTLAYL-PEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd14069  157 RLLNKM-----CGTLPYVaPELLAKKKYRAEPVDVWSCGIVLFAMLAGE 200
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
215-422 6.08e-14

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 72.80  E-value: 6.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 215 ELRIGEGGFGCVYRAVMRNTT-YAVKRLKEEadlewTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYcLVYGFLPN 293
Cdd:cd05069   17 DVKLGQGCFGEVWMGTWNGTTkVAIKTLKPG-----TMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIY-IVTEFMGK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 294 GSLEDqlHLQTQACSPLSWPQRLDILLGTARAIQFLHQdsPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAGANPS 373
Cdd:cd05069   91 GSLLD--FLKEGDGKYLKLPQLVDMAAQIADGMAYIER--MNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTAR 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 189011594 374 QSSTVARTCTVRGTLAYlpeeyiktGRLAVDTDTFSFGVVILETLAGQR 422
Cdd:cd05069  167 QGAKFPIKWTAPEAALY--------GRFTIKSDVWSFGILLTELVTKGR 207
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
218-422 7.50e-14

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 72.45  E-value: 7.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRN--------TTYAVKRLKEEA-DLEwtvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVY 288
Cdd:cd05044    3 LGSGAFGEVFEGTAKDilgdgsgeTKVAVKTLRKGAtDQE----KAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 289 GFLPNGSLEDQLHL---QTQACSPLSWPQRLDILLGTARAIQFLHQdsPSLIHGDIKSSNVLL-----DERLMpKLGDFG 360
Cdd:cd05044   79 ELMEGGDLLSYLRAarpTAFTPPLLTLKDLLSICVDVAKGCVYLED--MHFVHRDLAARNCLVsskdyRERVV-KIGDFG 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 361 LAR------FSRFAGanpsqsstvARTCTVRgtlaYLPEEYIKTGRLAVDTDTFSFGVVILETLA-GQR 422
Cdd:cd05044  156 LARdiykndYYRKEG---------EGLLPVR----WMAPESLVDGVFTTQSDVWAFGVLMWEILTlGQQ 211
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
217-435 1.02e-13

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: 71.77  E-value: 1.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGcvyRAVM-RNTTYAVKRLKEEADLEWTVVK--QSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPN 293
Cdd:cd08218    7 KIGEGSFG---KALLvKSKEDGKQYVIKEINISKMSPKerEESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCDG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 294 GSLEDQLHLQTQAcsPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFsrfaganps 373
Cdd:cd08218   84 GDLYKRINAQRGV--LFPEDQILDWFVQLCLALKHVHDRK--ILHRDIKSQNIFLTKDGIIKLGDFGIARV--------- 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594 374 QSSTV--ARTCTvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAKTKYLK 435
Cdd:cd08218  151 LNSTVelARTCI--GTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLK 212
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
212-416 1.05e-13

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 71.70  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELRIGEGGFGCVYRAVMRNTT-YAVKRLKEEADLewtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGF 290
Cdd:cd05148    8 FTLERKLGSGYFGEVWEGLWKNRVrVAIKILKSDDLL----KQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLedQLHLQTQACSPLSWPQRLDILLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRfaga 370
Cdd:cd05148   84 MEKGSL--LAFLRSPEGQVLPVASLIDMACQVAEGMAYL--EEQNSIHRDLAARNILVGEDLVCKVADFGLARLIK---- 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 189011594 371 nPSQSSTVARTCTVRGTlaylPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd05148  156 -EDVYLSSDKKIPYKWT----APEAASHGTFSTKSDVWSFGILLYE 196
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
212-416 1.26e-13

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


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 72.36  E-value: 1.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELRIGEGGFGCVY--RAVMRNTTYAVKRLK---EEADLEWtvvkQSFLTEVEQLSRFRHPNIVDFAG-YCAESGF-- 283
Cdd:cd06634   17 FSDLREIGHGSFGAVYfaRDVRNNEVVAIKKMSysgKQSNEKW----QDIIKEVKFLQKLRHPNTIEYRGcYLREHTAwl 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 284 ---YCLvygflpnGSLEDQLHLQTQacsPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFG 360
Cdd:cd06634   93 vmeYCL-------GSASDLLEVHKK---PLQEVEIAAITHGALQGLAYLH--SHNMIHRDVKAGNILLTEPGLVKLGDFG 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 361 LArfsrfaganpsqsSTVARTCTVRGTLAYLPEEYI---KTGRLAVDTDTFSFGVVILE 416
Cdd:cd06634  161 SA-------------SIMAPANSFVGTPYWMAPEVIlamDEGQYDGKVDVWSLGITCIE 206
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
218-387 1.49e-13

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: 71.56  E-value: 1.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEwtvvkQSFLTEVEQLSRF-RHPNIVDFAGycaesgfyclvyGFLPNG 294
Cdd:cd06608   14 IGEGTYGKVYKARHKKTgqLAAIKIMDIIEDEE-----EEIKLEINILRKFsNHPNIATFYG------------AFIKKD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SL--EDQLHLQTQAC----------SPLSWPQRLD------ILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKL 356
Cdd:cd06608   77 PPggDDQLWLVMEYCgggsvtdlvkGLRKKGKRLKeewiayILRETLRGLAYLHENK--VIHRDIKGQNILLTEEAEVKL 154
                        170       180       190
                 ....*....|....*....|....*....|.
gi 189011594 357 GDFGLARFSrfaganpsqSSTVARTCTVRGT 387
Cdd:cd06608  155 VDFGVSAQL---------DSTLGRRNTFIGT 176
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
218-416 1.49e-13

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB 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: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 71.61  E-value: 1.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT-------YAVKRLKEEADlewtVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGF 290
Cdd:cd05093   13 LGEGAFGKVFLAECYNLCpeqdkilVAVKTLKDASD----NARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSL---------EDQLHLQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGL 361
Cdd:cd05093   89 MKHGDLnkflrahgpDAVLMAEGNRPAELTQSQMLHIAQQIAAGMVYLA--SQHFVHRDLATRNCLVGENLLVKIGDFGM 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189011594 362 AR------FSRFAGANpsqsstvarTCTVRgtlaYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd05093  167 SRdvystdYYRVGGHT---------MLPIR----WMPPESIMYRKFTTESDVWSLGVVLWE 214
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
218-519 1.74e-13

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


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 71.30  E-value: 1.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRN-----TTYAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYcLVYGFLP 292
Cdd:cd05056   14 IGEGQFGDVYQGVYMSpenekIAVAVKTCKNCTSPS---VREKFLQEAYIMRQFDHPHIVKLIGVITENPVW-IVMELAP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLEDqlHLQTQAcsplswpQRLDIL------LGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFsr 366
Cdd:cd05056   90 LGELRS--YLQVNK-------YSLDLAslilyaYQLSTALAYLE--SKRFVHRDIAARNVLVSSPDCVKLGDFGLSRY-- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 367 faganpSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAgqRAVRT-QGAKTKYLKDLIEDeaeev 445
Cdd:cd05056  157 ------MEDESYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILM--LGVKPfQGVKNNDVIGRIEN----- 223
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594 446 gvtlkstqptlwmgvatdawtapiaaqiykkhlDSRPgPCPPQLGLALAQLACCCMHRRAKKRPPMTQVYKRLE 519
Cdd:cd05056  224 ---------------------------------GERL-PMPPNCPPTLYSLMTKCWAYDPSKRPRFTELKAQLS 263
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
217-416 1.89e-13

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


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 70.83  E-value: 1.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTT-----YAVKRLKEEAdLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYcLVYGFL 291
Cdd:cd05040    2 KLGDGSFGVVRRGEWTTPSgkviqVAVKCLKSDV-LSQPNAMDDFLKEVNAMHSLDHPNLIRLYGVVLSSPLM-MVTELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 PNGSLEDQLHlqtQACSPLSWPQRLDILLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfagAN 371
Cdd:cd05040   80 PLGSLLDRLR---KDQGHFLISTLCDYAVQIANGMAYL--ESKRFIHRDLAARNILLASKDKVKIGDFGLMR------AL 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 189011594 372 PSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd05040  149 PQNEDHYVMQEHRKVPFAWCAPESLKTRKFSHASDVWMFGVTLWE 193
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
218-416 1.93e-13

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: 71.99  E-value: 1.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAV--MRNTTYAVKRLK---EEADLEWtvvkQSFLTEVEQLSRFRHPNIVDFAG-YCAESGF-----YCL 286
Cdd:cd06633   29 IGHGSFGAVYFATnsHTNEVVAIKKMSysgKQTNEKW----QDIIKEVKFLQQLKHPNTIEYKGcYLKDHTAwlvmeYCL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 287 vygflpnGSLEDQLHLQTQacsPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFsr 366
Cdd:cd06633  105 -------GSASDLLEVHKK---PLQEVEIAAITHGALQGLAYLH--SHNMIHRDIKAGNILLTEPGQVKLADFGSASI-- 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 367 fagANPSQSSTvartctvrGTLAYLPEEYIktgrLAVD-------TDTFSFGVVILE 416
Cdd:cd06633  171 ---ASPANSFV--------GTPYWMAPEVI----LAMDegqydgkVDIWSLGITCIE 212
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
218-416 1.93e-13

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 71.27  E-value: 1.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT-------YAVKRL----KEEADLEwtvvkqsFLTEVEQLSRFRHPNIVDFAGYCAESGFYCL 286
Cdd:cd05036   14 LGQGAFGEVYEGTVSGMPgdpsplqVAVKTLpelcSEQDEMD-------FLMEALIMSKFNHPNIVRCIGVCFQRLPRFI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 287 VYGFLPNGSLEDQLHL---QTQACSPLSWPQRLDILLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERL---MPKLGDFG 360
Cdd:cd05036   87 LLELMAGGDLKSFLREnrpRPEQPSSLTMLDLLQLAQDVAKGCRYL--EENHFIHRDIAARNCLLTCKGpgrVAKIGDFG 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594 361 LAR------FSRFAGanpsqsstvartctvRGTL--AYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd05036  165 MARdiyradYYRKGG---------------KAMLpvKWMPPEAFLDGIFTSKTDVWSFGVLLWE 213
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
217-421 2.03e-13

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: 71.21  E-value: 2.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEWtvVKQSFLTEVEQLSRFR-HPNIVDF-AGYCAESGFYcLVYGFLP 292
Cdd:cd07832    7 RIGEGAHGIVFKAKDRETgeTVALKKVALRKLEGG--IPNQALREIKALQACQgHPYVVKLrDVFPHGTGFV-LVFEYML 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 nGSLEDQLHLQTQacsPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFsrFAGANP 372
Cdd:cd07832   84 -SSLSEVLRDEER---PLTEAQVKRYMRMLLKGVAYMHANR--IMHRDLKPANLLISSTGVLKIADFGLARL--FSEEDP 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 189011594 373 SQ-SSTVArtctvrgTLAYLPEEYIKTGR---LAVdtDTFSFGVVILETLAGQ 421
Cdd:cd07832  156 RLySHQVA-------TRWYRAPELLYGSRkydEGV--DLWAVGCIFAELLNGS 199
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
217-420 2.04e-13

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


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 71.29  E-value: 2.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNT--------TYAVKRLKEEA---DLewtvvkQSFLTEVEQLSRF-RHPNIVDFAGYCAESGFY 284
Cdd:cd05053   19 PLGEGAFGQVVKAEAVGLdnkpnevvTVAVKMLKDDAtekDL------SDLVSEMEMMKMIgKHKNIINLLGACTQDGPL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 285 CLVYGFLPNGSLEDQLHL---QTQACSP---------LSWPQRLDILLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERL 352
Cdd:cd05053   93 YVVVEYASKGNLREFLRArrpPGEEASPddprvpeeqLTQKDLVSFAYQVARGMEYL--ASKKCIHRDLAARNVLVTEDN 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189011594 353 MPKLGDFGLARFSRfaganpsqSSTVARTCTvRGTLAY--LPEEYIKTGRLAVDTDTFSFGVVILE--TLAG 420
Cdd:cd05053  171 VMKIADFGLARDIH--------HIDYYRKTT-NGRLPVkwMAPEALFDRVYTHQSDVWSFGVLLWEifTLGG 233
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
214-362 2.06e-13

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


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 70.94  E-value: 2.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 214 EELR-IGEGGFGCVY--RAVMRNTTYAVKRLK---EEADLEWtvvkQSFLTEVEQLSRFRHPNIVDFAG-YCAESGF--- 283
Cdd:cd06607    4 EDLReIGHGSFGAVYyaRNKRTSEVVAIKKMSysgKQSTEKW----QDIIKEVKFLRQLRHPNTIEYKGcYLREHTAwlv 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 284 --YCLvygflpnGSLEDQLHLQTQacsPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGL 361
Cdd:cd06607   80 meYCL-------GSASDIVEVHKK---PLQEVEIAAICHGALQGLAYLH--SHNRIHRDVKAGNILLTEPGTVKLADFGS 147

                 .
gi 189011594 362 A 362
Cdd:cd06607  148 A 148
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
217-419 2.25e-13

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: 70.73  E-value: 2.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMR--NTTYAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNG 294
Cdd:cd05084    3 RIGRGNFGEVFSGRLRadNTPVAVKSCRETLPPD---LKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLedQLHLQTQAcSPLSWPQRLDILLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfaganPSQ 374
Cdd:cd05084   80 DF--LTFLRTEG-PRLKVKELIRMVENAAAGMEYL--ESKHCIHRDLAARNCLVTEKNVLKISDFGMSR--------EEE 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 189011594 375 SSTVARTCTVRGT-LAYLPEEYIKTGRLAVDTDTFSFGVVILETLA 419
Cdd:cd05084  147 DGVYAATGGMKQIpVKWTAPEALNYGRYSSESDVWSFGILLWETFS 192
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
215-416 2.27e-13

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


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 70.80  E-value: 2.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 215 ELRIGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAES--GFYC--LVYGF 290
Cdd:cd14033    6 NIEIGRGSFKTVYRGLDTETTVEVAWCELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSWKSTvrGHKCiiLVTEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDQLHLQTQACSPLSWPQRLDILlgtaRAIQFLHQDSPSLIHGDIKSSNVLLDERLMP-KLGDFGLARFSRFAG 369
Cdd:cd14033   86 MTSGTLKTYLKRFREMKLKLLQRWSRQIL----KGLHFLHSRCPPILHRDLKCDNIFITGPTGSvKIGDLGLATLKRASF 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 189011594 370 ANpsqsstvartcTVRGTLAYL-PEEYIKTGRLAVdtDTFSFGVVILE 416
Cdd:cd14033  162 AK-----------SVIGTPEFMaPEMYEEKYDEAV--DVYAFGMCILE 196
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
218-421 2.37e-13

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


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 70.90  E-value: 2.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVY--RAVMRNTTYAVKRLKEEADLEwtvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd06624   16 LGKGTFGVVYaaRDLSTQVRIAIKEIPERDSRE----VQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEdqlHLQTQACSPLSWPQRL------DILLGtaraIQFLHQDspSLIHGDIKSSNVLLDERL-MPKLGDFGLARfsRFA 368
Cdd:cd06624   92 LS---ALLRSKWGPLKDNENTigyytkQILEG----LKYLHDN--KIVHRDIKGDNVLVNTYSgVVKISDFGTSK--RLA 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 369 GANPSqsstvarTCTVRGTLAYLPEEYIKTGR--LAVDTDTFSFGVVILETLAGQ 421
Cdd:cd06624  161 GINPC-------TETFTGTLQYMAPEVIDKGQrgYGPPADIWSLGCTIIEMATGK 208
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
218-412 2.64e-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: 70.66  E-value: 2.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAvmRNTT----YAVK-----RLK-----EEADLEWTVVKQSFLTEVEQLSRFRHPNIV-------Dfag 276
Cdd:cd14008    1 LGRGSFGKVKLA--LDTEtgqlYAIKifnksRLRkrregKNDRGKIKNALDDVRREIAIMKKLDHPNIVrlyevidD--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 277 ycAESGFYCLVYGFLPNGSLEDQLHLQTqaCSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKL 356
Cdd:cd14008   76 --PESDKLYLVLEYCEGGPVMELDSGDR--VPPLPEETARKYFRDLVLGLEYLH--ENGIVHRDIKPENLLLTADGTVKI 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 357 GDFGLARFsrFAGANPSQSSTVartctvrGTLAYLPEEYIKTGRLAVD---TDTFSFGV 412
Cdd:cd14008  150 SDFGVSEM--FEDGNDTLQKTA-------GTPAFLAPELCDGDSKTYSgkaADIWALGV 199
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
218-422 2.77e-13

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily 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).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 70.77  E-value: 2.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMR-----NTTYAVKRLKEEADLEWtvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLP 292
Cdd:cd05063   13 IGAGEFGEVFRGILKmpgrkEVAVAIKTLKPGYTEKQ---RQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYME 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLEDQLHLQTQACSPLswpQRLDILLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLarfSRFAGANP 372
Cdd:cd05063   90 NGALDKYLRDHDGEFSSY---QLVGMLRGIAAGMKYL--SDMNYVHRDLAARNILVNSNLECKVSDFGL---SRVLEDDP 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 189011594 373 SQSSTvarTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLA-GQR 422
Cdd:cd05063  162 EGTYT---TSGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSfGER 209
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
206-354 2.90e-13

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 70.82  E-value: 2.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 206 SQGTCNFSEELRIGEGGFGCVYRAVMR--NTTYAVKRLKEEadLEWTVVKQSFLTEVEQLSRF-RHPNIVDFAGYCAESG 282
Cdd:cd14138    1 SRYATEFHELEKIGSGEFGSVFKCVKRldGCIYAIKRSKKP--LAGSVDEQNALREVYAHAVLgQHSHVVRYYSAWAEDD 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189011594 283 FYCLVYGFLPNGSLEDQLHLQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMP 354
Cdd:cd14138   79 HMLIQNEYCNGGSLADAISENYRIMSYFTEPELKDLLLQVARGLKYIH--SMSLVHMDIKPSNIFISRTSIP 148
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
217-422 3.78e-13

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: 70.76  E-value: 3.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTT--YAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIV------DFAGYCAESGFYCLVY 288
Cdd:cd14038    1 RLGTGGFGNVLRWINQETGeqVAIKQCRQELSPK---NRERWCLEIQIMKRLNHPNVVaardvpEGLQKLAPNDLPLLAM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 289 GFLPNGSLEDQLHlQTQACSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLL---DERLMPKLGDFGLARfs 365
Cdd:cd14038   78 EYCQGGDLRKYLN-QFENCCGLREGAILTLLSDISSALRYLHENR--IIHRDLKPENIVLqqgEQRLIHKIIDLGYAK-- 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594 366 rfagaNPSQSSTvartCT-VRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQR 422
Cdd:cd14038  153 -----ELDQGSL----CTsFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFR 201
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
218-416 4.03e-13

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: 70.00  E-value: 4.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGcvyRAVM-----RNTTYAVK--RLKEEADLEWTVVKQSFLteveqLSRFRHPNIVDFAGYCAESGFYCLVYGF 290
Cdd:cd08219    8 VGEGSFG---RALLvqhvnSDQKYAMKeiRLPKSSSAVEDSRKEAVL-----LAKMKHPNIVAFKESFEADGHLYIVMEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDQLHLQTQACSP----LSWpqRLDILLGtaraIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFsr 366
Cdd:cd08219   80 CDGGDLMQKIKLQRGKLFPedtiLQW--FVQMCLG----VQHIHEKR--VLHRDIKSKNIFLTQNGKVKLGDFGSARL-- 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 189011594 367 faganpsQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd08219  150 -------LTSPGAYACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYE 192
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
214-363 5.35e-13

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: 70.00  E-value: 5.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 214 EEL-RIGEGGFGCVYRA--VMRNTTYAVKRLKEEADLEWtvVKQSFLTEV---EQLSRFRHPNIVD----FAGYCAESGF 283
Cdd:cd07838    2 EEVaEIGEGAYGTVYKArdLQDGRFVALKKVRVPLSEEG--IPLSTIREIallKQLESFEHPNVVRlldvCHGPRTDREL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 284 YC-LVYGFLpngsleDQ-LHLQTQACSP--LSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDF 359
Cdd:cd07838   80 KLtLVFEHV------DQdLATYLDKCPKpgLPPETIKDLMRQLLRGLDFLH--SHRIVHRDLKPQNILVTSDGQVKLADF 151

                 ....
gi 189011594 360 GLAR 363
Cdd:cd07838  152 GLAR 155
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
211-397 5.71e-13

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


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 69.61  E-value: 5.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 211 NFSEELRIGEGGFGCVYRAVMR--NTTYAVKRLK--EEADLewtVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCL 286
Cdd:cd08224    1 NYEIEKKIGKGQFSVVYRARCLldGRLVALKKVQifEMMDA---KARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 287 VYGFLPNGSLEDQLHLQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFsr 366
Cdd:cd08224   78 VLELADAGDLSRLIKHFKKQKRLIPERTIWKYFVQLCSALEHMH--SKRIMHRDIKPANVFITANGVVKLGDLGLGRF-- 153
                        170       180       190
                 ....*....|....*....|....*....|.
gi 189011594 367 FaganpSQSSTVARTcTVrGTLAYLPEEYIK 397
Cdd:cd08224  154 F-----SSKTTAAHS-LV-GTPYYMSPERIR 177
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
222-419 5.77e-13

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 70.12  E-value: 5.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 222 GFGC---VY------RAVMRNTTYAVKRLKEEADLEWTVVKQSFLT-EVEQLSRFRHPNIVDFAGYC-AESGFYCLVYGF 290
Cdd:cd14001    8 GYGTgvnVYlmkrspRGGSSRSPWAVKKINSKCDKGQRSLYQERLKeEAKILKSLNHPNIVGFRAFTkSEDGSLCLAMEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LP---NGSLEDQLHLQTQacsPLSWPQRLDILLGTARAIQFLHQDSpSLIHGDIKSSNVLLDerlmpklGDFGLARFSRF 367
Cdd:cd14001   88 GGkslNDLIEERYEAGLG---PFPAATILKVALSIARALEYLHNEK-KILHGDIKSGNVLIK-------GDFESVKLCDF 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 189011594 368 AGANP-SQSSTVARTCTVR--GTLAYLPEEYIKTGRLAVD-TDTFSFGVVILETLA 419
Cdd:cd14001  157 GVSLPlTENLEVDSDPKAQyvGTEPWKAKEALEEGGVITDkADIFAYGLVLWEMMT 212
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
218-420 6.41e-13

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: 69.28  E-value: 6.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAV--MRNTTYAVKRLKEEadlewTVVKQSFLTEVeQLSRF--RHPNIVD-FAGYCAESGFYCLVYGFLP 292
Cdd:cd13987    1 LGEGTYGKVLLAVhkGSGTKMALKFVPKP-----STKLKDFLREY-NISLElsVHPHIIKtYDVAFETEDYYVFAQEYAP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLEDQLhlQTQACSPLSWPQRldILLGTARAIQFLHqdSPSLIHGDIKSSNVLL---DERLMpKLGDFGLARfsrfag 369
Cdd:cd13987   75 YGDLFSII--PPQVGLPEERVKR--CAAQLASALDFMH--SKNLVHRDIKPENVLLfdkDCRRV-KLCDFGLTR------ 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 189011594 370 anpSQSSTVARtctVRGTLAYLPEEY---IKTGRLAVD--TDTFSFGVVILETLAG 420
Cdd:cd13987  142 ---RVGSTVKR---VSGTIPYTAPEVceaKKNEGFVVDpsIDVWAFGVLLFCCLTG 191
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
218-422 7.34e-13

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: 69.30  E-value: 7.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd06605    9 LGEGNGGVVSKVRHRPSgqIMAVKVIRLEIDEA---LQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMDGGS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LeDQLHLQTQACsplswPQRL--DILLGTARAIQFLHQDSpSLIHGDIKSSNVLLDERLMPKLGDFGLArfsrfaganPS 373
Cdd:cd06605   86 L-DKILKEVGRI-----PERIlgKIAVAVVKGLIYLHEKH-KIIHRDVKPSNILVNSRGQVKLCDFGVS---------GQ 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 189011594 374 QSSTVARTCTvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILEtLAGQR 422
Cdd:cd06605  150 LVDSLAKTFV--GTRSYMAPERISGGKYTVKSDIWSLGLSLVE-LATGR 195
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
218-418 8.04e-13

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: 68.92  E-value: 8.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLK---EEADLEWTVvkQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLP 292
Cdd:cd06625    8 LGQGAFGQVYLCYDADTgrELAVKQVEidpINTEASKEV--KALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLEDQLHLQTQACSPLSWPQRLDILLGTAraiqFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLA-RFSRFAGAN 371
Cdd:cd06625   86 GGSVKDEIKAYGALTENVTRKYTRQILEGLA----YLH--SNMIVHRDIKGANILRDSNGNVKLGDFGASkRLQTICSST 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 189011594 372 PSQSstvartctVRGTLAYLPEEYIKT---GRLAvdtDTFSFGVVILETL 418
Cdd:cd06625  160 GMKS--------VTGTPYWMSPEVINGegyGRKA---DIWSVGCTVVEML 198
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
214-423 1.16e-12

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: 68.61  E-value: 1.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 214 EELRI-GEGGFGCVY--RAVMRNTTYAVKRL------KEEadlewtvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFY 284
Cdd:cd08220    3 EKIRVvGRGAYGTVYlcRRKDDNKLVIIKQIpveqmtKEE--------RQAALNEVKVLSMLHHPNIIEYYESFLEDKAL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 285 CLVYGFLPNGSLEDqlHLQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDE-RLMPKLGDFGLAR 363
Cdd:cd08220   75 MIVMEYAPGGTLFE--YIQQRKGSLLSEEEILHFFVQILLALHHVH--SKQILHRDLKTQNILLNKkRTVVKIGDFGISK 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 364 FsrfaganpsqSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRA 423
Cdd:cd08220  151 I----------LSSKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRA 200
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
218-364 1.36e-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: 69.14  E-value: 1.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEadlEWTVVK----QSFLTEVEQLSRFRHPNIVDF-AGYCAESgFYCLVYGF 290
Cdd:cd07841    8 LGEGTYAVVYKARDKETgrIVAIKKIKLG---ERKEAKdginFTALREIKLLQELKHPNIIGLlDVFGHKS-NINLVFEF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPnGSLE----DQLHLQTQAcsplswpqrlDI---LLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLAR 363
Cdd:cd07841   84 ME-TDLEkvikDKSIVLTPA----------DIksyMLMTLRGLEYLH--SNWILHRDLKPNNLLIASDGVLKLADFGLAR 150

                 .
gi 189011594 364 F 364
Cdd:cd07841  151 S 151
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
218-421 1.42e-12

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: 68.60  E-value: 1.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEwtVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd07846    9 VGEGSYGMVMKCRHKETgqIVAIKKFLESEDDK--MVKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFEFVDHTV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDqlhLQtQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFsrFAGANPSQS 375
Cdd:cd07846   87 LDD---LE-KYPNGLDESRVRKYLFQILRGIDFCH--SHNIIHRDIKPENILVSQSGVVKLCDFGFART--LAAPGEVYT 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 189011594 376 STVArtctvrgTLAY-LPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd07846  159 DYVA-------TRWYrAPELLVGDTKYGKAVDVWAVGCLVTEMLTGE 198
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
217-422 1.44e-12

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


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 68.14  E-value: 1.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMR-----NTTYAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFyCLVYGFL 291
Cdd:cd05060    2 ELGHGNFGSVRKGVYLmksgkEVEVAVKTLKQEHEKA---GKKEFLREASVMAQLDHPCIVRLIGVCKGEPL-MLVMELA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 PNGSLEDQL--HLQTQACSPLSWpqrldiLLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRfAG 369
Cdd:cd05060   78 PLGPLLKYLkkRREIPVSDLKEL------AHQVAMGMAYL--ESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALG-AG 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 189011594 370 ANPSQSSTVARtCTVRGtlaYLPEEyIKTGRLAVDTDTFSFGVVILETLA-GQR 422
Cdd:cd05060  149 SDYYRATTAGR-WPLKW---YAPEC-INYGKFSSKSDVWSYGVTLWEAFSyGAK 197
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
212-416 1.54e-12

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


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 69.31  E-value: 1.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELRIGEGGFGCVY--RAVMRNTTYAVKRLK---EEADLEWtvvkQSFLTEVEQLSRFRHPNIVDFAG-YCAESGF-- 283
Cdd:cd06635   27 FSDLREIGHGSFGAVYfaRDVRTSEVVAIKKMSysgKQSNEKW----QDIIKEVKFLQRIKHPNSIEYKGcYLREHTAwl 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 284 ---YCLvygflpnGSLEDQLHLQTQacsPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFG 360
Cdd:cd06635  103 vmeYCL-------GSASDLLEVHKK---PLQEIEIAAITHGALQGLAYLH--SHNMIHRDIKAGNILLTEPGQVKLADFG 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 361 LARFsrfagANPSQSSTvartctvrGTLAYLPEEYI---KTGRLAVDTDTFSFGVVILE 416
Cdd:cd06635  171 SASI-----ASPANSFV--------GTPYWMAPEVIlamDEGQYDGKVDVWSLGITCIE 216
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
218-416 1.91e-12

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


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 68.15  E-value: 1.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRA--VMRNTTYAVKRLkeeaDLE-WTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNG 294
Cdd:cd06610    9 IGSGATAVVYAAycLPKKEKVAIKRI----DLEkCQTSMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPLLSGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLedqLHLQTQACSPLSWPQRL--DILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSrfagANP 372
Cdd:cd06610   85 SL---LDIMKSSYPRGGLDEAIiaTVLKEVLKGLEYLH--SNGQIHRDVKAGNILLGEDGSVKIADFGVSASL----ATG 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 189011594 373 SQSSTVARTcTVRGTLAYLPEEYIKTGR-LAVDTDTFSFGVVILE 416
Cdd:cd06610  156 GDRTRKVRK-TFVGTPCWMAPEVMEQVRgYDFKADIWSFGITAIE 199
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
217-421 2.10e-12

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: 67.95  E-value: 2.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRaVMRNTTYAVKRLKE-------EADlewtvvKQSFLTEVEQLSRFRHPNIVdfaGYC------AESGF 283
Cdd:cd08217    7 TIGKGSFGTVRK-VRRKSDGKILVWKEidygkmsEKE------KQQLVSEVNILRELKHPNIV---RYYdrivdrANTTL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 284 YcLVYGFLPNGSLED--QLHLQTQacSPLSWPQRLDILLGTARAIQFLH---QDSPSLIHGDIKSSNVLLDERLMPKLGD 358
Cdd:cd08217   77 Y-IVMEYCEGGDLAQliKKCKKEN--QYIPEEFIWKIFTQLLLALYECHnrsVGGGKILHRDLKPANIFLDSDNNVKLGD 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189011594 359 FGLARfsrfagaNPSQSSTVARTCTvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd08217  154 FGLAR-------VLSHDSSFAKTYV--GTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALH 207
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
215-422 2.47e-12

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 67.79  E-value: 2.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 215 ELRIGEGGFGCVYRAVMR-NTTYAVKRLKEEadlewTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYcLVYGFLPN 293
Cdd:cd05070   14 IKRLGNGQFGEVWMGTWNgNTKVAIKTLKPG-----TMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIY-IVTEYMSK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 294 GSLEDqlHLQTQACSPLSWPQRLDILLGTARAIQFLHQdsPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAGANPS 373
Cdd:cd05070   88 GSLLD--FLKDGEGRALKLPNLVDMAAQVAAGMAYIER--MNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTAR 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 189011594 374 QSSTVARTCTVRGTLAYlpeeyiktGRLAVDTDTFSFGVVILETLAGQR 422
Cdd:cd05070  164 QGAKFPIKWTAPEAALY--------GRFTIKSDVWSFGILLTELVTKGR 204
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
218-429 2.70e-12

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 67.50  E-value: 2.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVM-----RNTTYAVKRLKEEADLEwtVVKQsFLTEVEQLSRFRHPNIVDFAGYCAES-GFYCLVYGFL 291
Cdd:cd05058    3 IGKGHFGCVYHGTLidsdgQKIHCAVKSLNRITDIE--EVEQ-FLKEGIIMKDFSHPNVLSLLGICLPSeGSPLVVLPYM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 PNGSLEDQLHlqtqacSPLSWPQRLDIL---LGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLAR--FSR 366
Cdd:cd05058   80 KHGDLRNFIR------SETHNPTVKDLIgfgLQVAKGMEYLA--SKKFVHRDLAARNCMLDESFTVKVADFGLARdiYDK 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189011594 367 faganpsQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLagqravrTQGA 429
Cdd:cd05058  152 -------EYYSVHNHTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELM-------TRGA 200
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
217-421 3.12e-12

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: 67.26  E-value: 3.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTTY--AVKRLkeeaDLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNG 294
Cdd:cd06647   14 KIGQGASGTVYTAIDVATGQevAIKQM----NLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEDQLhlqTQACspLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLArfsrfAGANPSQ 374
Cdd:cd06647   90 SLTDVV---TETC--MDEGQIAAVCRECLQALEFLH--SNQVIHRDIKSDNILLGMDGSVKLTDFGFC-----AQITPEQ 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 189011594 375 SstvaRTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd06647  158 S----KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGE 200
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
218-420 3.29e-12

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: 67.63  E-value: 3.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEeADLEWTVVKQSFLTEVEQLSRFRHPNIVD-FAGYCAESGFYcLVYGFLPNG 294
Cdd:cd05579    1 ISRGAYGRVYLAKKKSTgdLYAIKVIKK-RDMIRKNQVDSVLAERNILSQAQNPFVVKlYYSFQGKKNLY-LVMEYLPGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEdqlhlqtqacSPLSWPQRLD----------ILLgtarAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARF 364
Cdd:cd05579   79 DLY----------SLLENVGALDedvariyiaeIVL----ALEYLHSHG--IIHRDLKPDNILIDANGHLKLTDFGLSKV 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189011594 365 ------SRFAGANPSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd05579  143 glvrrqIKLSIQKKSNGAPEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVG 204
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
218-363 3.49e-12

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: 67.08  E-value: 3.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVY--RAVMRNTTYAVKR--LKEEADLEWTVVKQsfltEVEQLSRFRHPNIVDFA-GYCAESGFYCLVYGFLP 292
Cdd:cd08223    8 IGKGSYGEVWlvRHKRDRKQYVIKKlnLKNASKRERKAAEQ----EAKLLSKLKHPNIVSYKeSFEGEDGFLYIVMGFCE 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189011594 293 NGSLEDQLhlQTQACSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLAR 363
Cdd:cd08223   84 GGDLYTRL--KEQKGVLLEERQVVEWFVQIAMALQYMHERN--ILHRDLKTQNIFLTKSNIIKVGDLGIAR 150
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
218-369 3.56e-12

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: 67.03  E-value: 3.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAV--KRLKEEADLEWTVVKQSFLTEV-------EQLSRFRHPNIVDFAGYCAESGFYCLVy 288
Cdd:cd14004    8 MGEGAYGQVNLAIYKSKGKEVviKFIFKERILVDTWVRDRKLGTVpleihilDTLNKRSHPNIVKLLDFFEDDEFYYLV- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 289 gFLPNGS---LEDQLHLQTQACSPLSwpqRLdILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLA--- 362
Cdd:cd14004   87 -MEKHGSgmdLFDFIERKPNMDEKEA---KY-IFRQVADAVKHLH--DQGIVHRDIKDENVILDGNGTIKLIDFGSAayi 159
                        170
                 ....*....|
gi 189011594 363 ---RFSRFAG 369
Cdd:cd14004  160 ksgPFDTFVG 169
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
217-416 3.74e-12

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: 67.35  E-value: 3.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFG----CVYRAVMRNT--TYAVKRLKEEADLEWtvvkQSFLTEVEQLSRFRHPNIVDFAGYCAESGF--YCLVY 288
Cdd:cd14205   11 QLGKGNFGsvemCRYDPLQDNTgeVVAVKKLQHSTEEHL----RDFEREIEILKSLQHDNIVKYKGVCYSAGRrnLRLIM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 289 GFLPNGSLEDQLHLQTQacsplswpqRLD---ILLGTA---RAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLA 362
Cdd:cd14205   87 EYLPYGSLRDYLQKHKE---------RIDhikLLQYTSqicKGMEYLGTKR--YIHRDLATRNILVENENRVKIGDFGLT 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 363 RF-----SRFAGANPSQSStvartctvrgTLAYLPEEYIKTgRLAVDTDTFSFGVVILE 416
Cdd:cd14205  156 KVlpqdkEYYKVKEPGESP----------IFWYAPESLTES-KFSVASDVWSFGVVLYE 203
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
217-363 3.97e-12

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: 67.63  E-value: 3.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNT--TYAVKRLKEEAdlewtvVKQSF----LTEVEQLSRFRHPNIVDFA----GYCAESGFycL 286
Cdd:cd07843   12 RIEEGTYGVVYRARDKKTgeIVALKKLKMEK------EKEGFpitsLREINILLKLQHPNIVTVKevvvGSNLDKIY--M 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 287 VYGFLPNgSLEDQLHLQTQacsPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLAR 363
Cdd:cd07843   84 VMEYVEH-DLKSLMETMKQ---PFLQSEVKCLMLQLLSGVAHLHDNW--ILHRDLKTSNLLLNNRGILKICDFGLAR 154
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
218-422 4.20e-12

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: 67.25  E-value: 4.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFG--CVYRAVMRNTTYAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYC-----LVYGF 290
Cdd:cd14039    1 LGTGGFGnvCLYQNQETGEKIAIKSCRLELSVK---NKDRWCHEIQIMKKLNHPNVVKACDVPEEMNFLVndvplLAMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDQLHlQTQACSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDE---RLMPKLGDFGLARfsrf 367
Cdd:cd14039   78 CSGGDLRKLLN-KPENCCGLKESQVLSLLSDIGSGIQYLHENK--IIHRDLKPENIVLQEingKIVHKIIDLGYAK---- 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 189011594 368 agaNPSQSSTvartCT-VRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQR 422
Cdd:cd14039  151 ---DLDQGSL----CTsFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFR 199
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
215-422 4.26e-12

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 66.97  E-value: 4.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 215 ELRIGEGGFGCVYRAVM-RNTTYAVKRLKEEadlewTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYcLVYGFLPN 293
Cdd:cd05073   16 EKKLGAGQFGEVWMATYnKHTKVAVKTMKPG-----SMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEPIY-IITEFMAK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 294 GSLEDQLHLQTQACSPLswPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFSRfaganps 373
Cdd:cd05073   90 GSLLDFLKSDEGSKQPL--PKLIDFSAQIAEGMAFIEQRN--YIHRDLRAANILVSASLVCKIADFGLARVIE------- 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 189011594 374 QSSTVARTcTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQR 422
Cdd:cd05073  159 DNEYTARE-GAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGR 206
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
218-420 5.65e-12

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


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 67.08  E-value: 5.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRA--VMRNTTYAVKRLKEEADlewTVVKQSFLTEVEQLSRFRHPNIVDFAG-YCAESGFYCLVYGFLPNG 294
Cdd:cd06620   13 LGAGNGGSVSKVlhIPTGTIMAKKVIHIDAK---SSVRKQILRELQILHECHSPYIVSFYGaFLNENNNIIICMEYMDCG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEdqlhlqtqACSPLSWPQRLDIL----LGTARAIQFLHqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfaga 370
Cdd:cd06620   90 SLD--------KILKKKGPFPEEVLgkiaVAVLEGLTYLY-NVHRIIHRDIKPSNILVNSKGQIKLCDFGVSG------- 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 189011594 371 npSQSSTVARTCTvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd06620  154 --ELINSIADTFV--GTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALG 199
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
212-420 5.66e-12

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: 66.88  E-value: 5.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELRIGEGGFGCVYRAVMRNT--TYAVKRLK-EEADLEWTVVKQsfltEVEQLSRFRHPNIVDFAGYCAESGFYCLVY 288
Cdd:cd06609    3 FTLLERIGKGSFGEVYKGIDKRTnqVVAIKVIDlEEAEDEIEDIQQ----EIQFLSQCDSPYITKYYGSFLKGSKLWIIM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 289 GFLPNGSLEDQLHlqtqacsplswPQRLD------ILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLA 362
Cdd:cd06609   79 EYCGGGSVLDLLK-----------PGPLDetyiafILREVLLGLEYLHSEG--KIHRDIKAANILLSEEGDVKLADFGVS 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 363 rfsrfaganpSQ-SSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd06609  146 ----------GQlTSTMSKRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKG 194
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
217-421 5.68e-12

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 68.67  E-value: 5.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAV-MR-NTTYAVKRLKeeADLewtVVKQSFLTeveqlsRFR----------HPNIV---DfAGycAES 281
Cdd:NF033483  14 RIGRGGMAEVYLAKdTRlDRDVAVKVLR--PDL---ARDPEFVA------RFRreaqsaaslsHPNIVsvyD-VG--EDG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 282 GFYCLVYGFLPNGSLEDQLHLQtqacSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGL 361
Cdd:NF033483  80 GIPYIVMEYVDGRTLKDYIREH----GPLSPEEAVEIMIQILSALEHAHRNG--IVHRDIKPQNILITKDGRVKVTDFGI 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189011594 362 AR-FSrfaganpsqSSTVARTCTVRGTLAYLPEEYIKTGrlAVD--TDTFSFGVVILETLAGQ 421
Cdd:NF033483 154 ARaLS---------STTMTQTNSVLGTVHYLSPEQARGG--TVDarSDIYSLGIVLYEMLTGR 205
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
218-421 5.81e-12

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: 66.69  E-value: 5.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVM-RNTTYAVKRL------KEEADLEWTVVKQsfltEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGF 290
Cdd:cd06631    9 LGKGAYGTVYCGLTsTGQLIAVKQVeldtsdKEKAEKEYEKLQE----EVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDQLHLQTQACSPLSWPQRLDILLGtaraIQFLHQDspSLIHGDIKSSNVLlderLMP----KLGDFGLARFSR 366
Cdd:cd06631   85 VPGGSIASILARFGALEEPVFCRYTKQILEG----VAYLHNN--NVIHRDIKGNNIM----LMPngviKLIDFGCAKRLC 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 367 FAGANPSQSSTVArtcTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd06631  155 INLSSGSQSQLLK---SMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGK 206
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
218-420 5.88e-12

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: 66.83  E-value: 5.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEeadleWTVVKQS----FLTEVEQLSRFRHPNIVD-FAGYCAESGFYcLVYGF 290
Cdd:cd05580    9 LGTGSFGRVRLVKHKDSgkYYALKILKK-----AKIIKLKqvehVLNEKRILSEVRHPFIVNlLGSFQDDRNLY-MVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDqlHLQTQACSPLSWPQ--RLDILLgtarAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFa 368
Cdd:cd05580   83 VPGGELFS--LLRRSGRFPNDVAKfyAAEVVL----ALEYLH--SLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVKD- 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 369 ganpsqsstvaRTCTVRGTLAYLPEEYIKT---GRLAvdtDTFSFGVVILETLAG 420
Cdd:cd05580  154 -----------RTYTLCGTPEYLAPEIILSkghGKAV---DWWALGILIYEMLAG 194
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
218-440 6.09e-12

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: 66.42  E-value: 6.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEAdLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd14186    9 LGKGSFACVYRARSLHTglEVAIKMIDKKA-MQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEMCHNGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLHLQTQacsPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFaganPSQs 375
Cdd:cd14186   88 MSRYLKNRKK---PFTEDEARHFMHQIVTGMLYLH--SHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKM----PHE- 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 376 stvaRTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAKTKYLKDLIED 440
Cdd:cd14186  158 ----KHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLAD 218
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
218-522 6.23e-12

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


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 66.52  E-value: 6.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTyAVKRLKE--EADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd14221    1 LGKGCFGQAIKVTHRETG-EVMVMKEliRFDEE---TQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLHLQTQACSplsWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARF-----SRFAGA 370
Cdd:cd14221   77 LRGIIKSMDSHYP---WSQRVSFAKDIASGMAYLH--SMNIIHRDLNSHNCLVRENKSVVVADFGLARLmvdekTQPEGL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 371 NPSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAgqravrTQGAKTKYLKDliedeaeevgvtlk 450
Cdd:cd14221  152 RSLKKPDRKKRYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEIIG------RVNADPDYLPR-------------- 211
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189011594 451 stqpTLWMGVATDAWtapiaaqiykkhLDSRpgpCPPQLGLALAQLACCCMHRRAKKRPPMTQVYKRLEGLQ 522
Cdd:cd14221  212 ----TMDFGLNVRGF------------LDRY---CPPNCPPSFFPIAVLCCDLDPEKRPSFSKLEHWLETLR 264
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
212-421 6.34e-12

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: 66.57  E-value: 6.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELRIGEGGFGCVYRAvmrnttyavkRLKEEADLEWTVV---------KQSFL-TEVEQLSRFRHPNIVDFAGYCAES 281
Cdd:cd14202    4 FSRKDLIGHGAFAVVFKG----------RHKEKHDLEVAVKcinkknlakSQTLLgKEIKILKELKHENIVALYDFQEIA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 282 GFYCLVYGFLPNGSLEDQLHlqTQACspLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLD----ERLMP--- 354
Cdd:cd14202   74 NSVYLVMEYCNGGDLADYLH--TMRT--LSEDTIRLFLQQIAGAMKMLH--SKGIIHRDLKPQNILLSysggRKSNPnni 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 355 --KLGDFGLARFsrfaganpSQSSTVArtCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd14202  148 riKIADFGFARY--------LQNNMMA--ATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGK 206
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
218-422 6.53e-12

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: 66.64  E-value: 6.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRL---KEEADLEW----TVVKqSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVY 288
Cdd:cd06629    9 IGKGTYGRVYLAMNATTgeMLAVKQVelpKTSSDRADsrqkTVVD-ALKSEIDTLKDLDHPNIVQYLGFEETEDYFSIFL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 289 GFLPNGSL----------EDQL--HLQTQacsplswpqrldILLGTAraiqFLHqdSPSLIHGDIKSSNVLLDERLMPKL 356
Cdd:cd06629   88 EYVPGGSIgsclrkygkfEEDLvrFFTRQ------------ILDGLA----YLH--SKGILHRDLKADNILVDLEGICKI 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594 357 GDFGLARFSRFAGANpsQSSTvartcTVRGTLAYLPEEYIKTGR--LAVDTDTFSFGVVILETLAGQR 422
Cdd:cd06629  150 SDFGISKKSDDIYGN--NGAT-----SMQGSVFWMAPEVIHSQGqgYSAKVDIWSLGCVVLEMLAGRR 210
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
218-509 6.65e-12

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: 66.85  E-value: 6.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCV--YRAVMRN----TTYAVKRLKEEADLEWTvvkQSFLTEVEQLSRFRHPNIVDFAGYCAESG--FYCLVYG 289
Cdd:cd05080   12 LGEGHFGKVslYCYDPTNdgtgEMVAVKALKADCGPQHR---SGWKQEIDILKTLYHENIVKYKGCCSEQGgkSLQLIME 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLEDQLHLQTqacspLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARF----- 364
Cdd:cd05080   89 YVPLGSLRDYLPKHS-----IGLAQLLLFAQQICEGMAYLH--SQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAvpegh 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 365 ----SRFAGANPsqsstvartctvrgtLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAgqRAVRTQGAKTKYLkdlied 440
Cdd:cd05080  162 eyyrVREDGDSP---------------VFWYAPECLKEYKFYYASDVWSFGVTLYELLT--HCDSSQSPPTKFL------ 218
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 441 eaEEVGVtlKSTQPTLwmgvatdawtAPIAAQIYKKHLDSRPGPCPPQLGLALAQlaccCMHRRAKKRP 509
Cdd:cd05080  219 --EMIGI--AQGQMTV----------VRLIELLERGERLPCPDKCPQEVYHLMKN----CWETEASFRP 269
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
218-422 7.72e-12

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: 66.70  E-value: 7.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFG--CVYRAVMRNTTYAVKRLKEEADLEWTVvKQSFLTEVEQLSRFRHPNIVDFAGY------CAESGFYCLVYG 289
Cdd:cd13989    1 LGSGGFGyvTLWKHQDTGEYVAIKKCRQELSPSDKN-RERWCLEVQIMKKLNHPNVVSARDVppelekLSPNDLPLLAME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLEDQLHlQTQACSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDE---RLMPKLGDFGLARfsr 366
Cdd:cd13989   80 YCSGGDLRKVLN-QPENCCGLKESEVRTLLSDISSAISYLHENR--IIHRDLKPENIVLQQgggRVIYKLIDLGYAK--- 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 189011594 367 fagaNPSQSSTVArtcTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQR 422
Cdd:cd13989  154 ----ELDQGSLCT---SFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYR 202
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
218-420 7.89e-12

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: 66.40  E-value: 7.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEA-DLEWTVVKQSFLT----EVEQLSRFRHPNIVDFAGYCAESGFYCLVYGF 290
Cdd:cd06628    8 IGSGSFGSVYLGMNASSgeLMAVKQVELPSvSAENKDRKKSMLDalqrEIALLRELQHENIVQYLGSSSDANHLNIFLEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDQLHLQTQACSPLSWPQRLDILLGtaraIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLarfSRFAGA 370
Cdd:cd06628   88 VPGGSVATLLNNYGAFEESLVRNFVRQILKG----LNYLH--NRGIIHRDIKGANILVDNKGGIKISDFGI---SKKLEA 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 189011594 371 NPSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd06628  159 NSLSTKNNGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTG 208
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
232-364 8.43e-12

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-A/B subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 66.46  E-value: 8.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 232 RNTTYAVKRL-KEEADLEwtvvkQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLEDQL---HLQtqac 307
Cdd:cd14042   29 KGNLVAIKKVnKKRIDLT-----REVLKELKHMRDLQHDNLTRFIGACVDPPNICILTEYCPKGSLQDILeneDIK---- 99
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189011594 308 spLSWPQRL----DILLGTAraiqFLHqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARF 364
Cdd:cd14042  100 --LDWMFRYslihDIVKGMH----YLH-DSEIKSHGNLKSSNCVVDSRFVLKITDFGLHSF 153
Death pfam00531
Death domain;
27-102 8.59e-12

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 61.61  E-value: 8.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594   27 MCRFYKVMDALEP--ADWCQFAALIVRDQTELRLCERSEQRTAS----VLWPWINR---NARVADLVHILTHLQLLRARD 97
Cdd:pfam00531   1 RKQLDRLLDPPPPlgKDWRELARKLGLSENEIDEIESENPRLRSqtyeLLRLWEQRegkNATVGTLLEALRKLGRRDAAE 80

                  ....*
gi 189011594   98 IITAW 102
Cdd:pfam00531  81 KIQSI 85
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
217-420 8.69e-12

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


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 66.69  E-value: 8.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTTY---AVKRLKEE---ADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGF 290
Cdd:cd14096    8 KIGEGAFSNVYKAVPLRNTGkpvAIKVVRKAdlsSDNLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYYIVLEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDQLHLQTQACSPLSwpqrLDILLGTARAIQFLHqdSPSLIHGDIKSSNVL----------------------L 348
Cdd:cd14096   88 ADGGEIFHQIVRLTYFSEDLS----RHVITQVASAVKYLH--EIGVVHRDIKPENLLfepipfipsivklrkadddetkV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 349 DE-RLMP----------KLGDFGLARFSRfaganPSQSSTvarTCtvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILET 417
Cdd:cd14096  162 DEgEFIPgvggggigivKLADFGLSKQVW-----DSNTKT---PC---GTVGYTAPEVVKDERYSKKVDMWALGCVLYTL 230

                 ...
gi 189011594 418 LAG 420
Cdd:cd14096  231 LCG 233
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
218-420 1.33e-11

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: 65.88  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKeeadlewtvvKQSF--------------LTEVEQLSRFRHPNIVDFAGYCAES 281
Cdd:cd14084   14 LGSGACGEVKLAYDKSTckKVAIKIIN----------KRKFtigsrreinkprniETEIEILKKLSHPCIIKIEDFFDAE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 282 GFYCLVYGFLPNGSLEDQ----LHLqTQACSPLSWPQRLDillgtarAIQFLHqdSPSLIHGDIKSSNVLL---DERLMP 354
Cdd:cd14084   84 DDYYIVLELMEGGELFDRvvsnKRL-KEAICKLYFYQMLL-------AVKYLH--SNGIIHRDLKPENVLLssqEEECLI 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 355 KLGDFGLARFsrfaganpSQSSTVART-CtvrGTLAYL-PEEYIKTGRLAVD--TDTFSFGVVILETLAG 420
Cdd:cd14084  154 KITDFGLSKI--------LGETSLMKTlC---GTPTYLaPEVLRSFGTEGYTraVDCWSLGVILFICLSG 212
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
211-515 1.59e-11

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 65.82  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 211 NFSEELriGEGGFGCVYRAVMRNTT------------------YAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIV 272
Cdd:cd05051    8 EFVEKL--GEGQFGEVHLCEANGLSdltsddfigndnkdepvlVAVKMLRPDASKN---AREDFLKEVKIMSQLKDPNIV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 273 DFAGYCAESGFYCLVYGFLPNGSL---------EDQLHLQTQAcSPLSWPQRLDILLGTARAIQFLhqDSPSLIHGDIKS 343
Cdd:cd05051   83 RLLGVCTRDEPLCMIVEYMENGDLnqflqkheaETQGASATNS-KTLSYGTLLYMATQIASGMKYL--ESLNFVHRDLAT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 344 SNVLLDERLMPKLGDFGLARfsrfaganpsqSSTVARTCTVRGTlAYLP-----EEYIKTGRLAVDTDTFSFGVVILETL 418
Cdd:cd05051  160 RNCLVGPNYTIKIADFGMSR-----------NLYSGDYYRIEGR-AVLPirwmaWESILLGKFTTKSDVWAFGVTLWEIL 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 419 agqravrtqgaktkylkdliedeaeevgvTLKSTQPtlwMGVATDAWTAPIAAQIYKK-----HLDsRPGPCPPQlglaL 493
Cdd:cd05051  228 -----------------------------TLCKEQP---YEHLTDEQVIENAGEFFRDdgmevYLS-RPPNCPKE----I 270
                        330       340
                 ....*....|....*....|..
gi 189011594 494 AQLACCCMHRRAKKRPPMTQVY 515
Cdd:cd05051  271 YELMLECWRRDEEDRPTFREIH 292
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
218-363 1.63e-11

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: 65.45  E-value: 1.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRL----KEEADLEWTVVKQSFLTEVEQLSRF-RHPNIVDFAGYCAESGFYCLVYGF 290
Cdd:cd14093   11 LGRGVSSTVRRCIEKETgqEFAVKIIditgEKSSENEAEELREATRREIEILRQVsGHPNIIELHDVFESPTFIFLVFEL 90
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189011594 291 LPNGSLEDQLhlqTQACSpLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLAR 363
Cdd:cd14093   91 CRKGELFDYL---TEVVT-LSEKKTRRIMRQLFEAVEFLH--SLNIVHRDLKPENILLDDNLNVKISDFGFAT 157
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
218-364 2.13e-11

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: 65.22  E-value: 2.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRlkeeadlewtvVKQ-----SFltEVEQLSRFRHPNIVDFAGYCAESG------FY 284
Cdd:cd14137   12 IGSGSFGVVYQAKLLETgeVVAIKK-----------VLQdkrykNR--ELQIMRRLKHPNIVKLKYFFYSSGekkdevYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 285 CLVYGFLPNgSLEDQLHLQTQACSPLSwpqRLDILLGT---ARAIQFLHqdSPSLIHGDIKSSNVLLDERLMP-KLGDFG 360
Cdd:cd14137   79 NLVMEYMPE-TLYRVIRHYSKNKQTIP---IIYVKLYSyqlFRGLAYLH--SLGICHRDIKPQNLLVDPETGVlKLCDFG 152

                 ....
gi 189011594 361 LARF 364
Cdd:cd14137  153 SAKR 156
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
218-420 2.19e-11

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: 64.89  E-value: 2.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVK-RLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSL 296
Cdd:cd14117   14 LGKGKFGNVYLAREKQSKFIVAlKVLFKSQIEKEGVEHQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLILEYAPRGEL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 297 EDQLhlqtQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSrfaganPSqss 376
Cdd:cd14117   94 YKEL----QKHGRFDEQRTATFMEELADALHYCH--EKKVIHRDIKPENLLMGYKGELKIADFGWSVHA------PS--- 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 189011594 377 tvARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd14117  159 --LRRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVG 200
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
218-421 2.37e-11

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: 65.48  E-value: 2.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT--YAVKRLK-----EEADLEWTVVKQSFLTeveqlSRFRHPNIVD-FAGYCAESGFYcLVYG 289
Cdd:cd05592    3 LGKGSFGKVMLAELKGTNqyFAIKALKkdvvlEDDDVECTMIERRVLA-----LASQHPFLTHlFCTFQTESHLF-FVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLedQLHLQTQAcsplswpqRLD----------ILLGtaraIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDF 359
Cdd:cd05592   77 YLNGGDL--MFHIQQSG--------RFDedrarfygaeIICG----LQFLH--SRGIIYRDLKLDNVLLDREGHIKIADF 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189011594 360 GLARFSRFAGANPSqsstvartcTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd05592  141 GMCKENIYGENKAS---------TFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQ 193
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
218-421 2.50e-11

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: 64.62  E-value: 2.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT--YAVKrlkeeadlewtVVKQSFLTEVEQLSRF----RHPNIVDFAGYCAESGFYCLVYGFL 291
Cdd:cd14010    8 IGRGKHSVVYKGRRKGTIefVAIK-----------CVDKSKRPEVLNEVRLthelKHPNVLKFYEWYETSNHLWLVVEYC 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 PNGSLEDQL----HLQTQACSPLSwpqrLDIllgtARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLAR---- 363
Cdd:cd14010   77 TGGDLETLLrqdgNLPESSVRKFG----RDL----VRGLHYIH--SKGIIYCDLKPSNILLDGNGTLKLSDFGLARrege 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189011594 364 -----FSRFAGANPSQSSTVARtcTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd14010  147 ilkelFGQFSDEGNVNKVSKKQ--AKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGK 207
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
218-510 2.94e-11

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: 64.37  E-value: 2.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRA--VMRNTTYAVKRLK--EEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPN 293
Cdd:cd06630    8 LGTGAFSSCYQArdVKTGTLMAVKQVSfcRNSSSEQEEVVEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 294 GSLEDQLHLQTQACSPLSWPQRLDILLGTAraiqFLHQDspSLIHGDIKSSNVLLD---ERLmpKLGDFGLA-RF-SRFA 368
Cdd:cd06630   88 GSVASLLSKYGAFSENVIINYTLQILRGLA----YLHDN--QIIHRDLKGANLLVDstgQRL--RIADFGAAaRLaSKGT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 369 GANPSQSSTVartctvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILEtlagqravrtqgaktkylkdliedeaeevgvt 448
Cdd:cd06630  160 GAGEFQGQLL-------GTIAFMAPEVLRGEQYGRSCDVWSVGCVIIE-------------------------------- 200
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189011594 449 lkstqptlwMGVATDAWTA-PIA---AQIYKKHLDSRPGPCPPQLGLALAQLACCCMHRRAKKRPP 510
Cdd:cd06630  201 ---------MATAKPPWNAeKISnhlALIFKIASATTPPPIPEHLSPGLRDVTLRCLELQPEDRPP 257
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
211-363 3.09e-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: 3.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 211 NFSEELRIGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGF 290
Cdd:cd07860    1 NFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEF 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189011594 291 LpNGSLEDqlHLQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLAR 363
Cdd:cd07860   81 L-HQDLKK--FMDASALTGIPLPLIKSYLFQLLQGLAFCH--SHRVLHRDLKPQNLLINTEGAIKLADFGLAR 148
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
218-420 3.09e-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: 64.61  E-value: 3.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVK-------RLKEEADLEwtvVKQSFLTEVEQLSRFR-HPNIVDFAGYCAESGFYCLV 287
Cdd:cd14181   18 IGRGVSSVVRRCVHRHTgqEFAVKiievtaeRLSPEQLEE---VRSSTLKEIHILRQVSgHPSIITLIDSYESSTFIFLV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 288 YGFLPNGSLEDQLhlqTQACSpLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGlarFSRF 367
Cdd:cd14181   95 FDLMRRGELFDYL---TEKVT-LSEKETRSIMRSLLEAVSYLHANN--IVHRDLKPENILLDDQLHIKLSDFG---FSCH 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 368 AGANpsqsSTVARTCtvrGTLAYLPEEYIKTGR------LAVDTDTFSFGVVILETLAG 420
Cdd:cd14181  166 LEPG----EKLRELC---GTPGYLAPEILKCSMdethpgYGKEVDLWACGVILFTLLAG 217
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
218-479 4.02e-11

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: 64.93  E-value: 4.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLK-----EEADLEWTVVKQSFLTeveqLSRfRHPNIVDFagycaesgFYCL---- 286
Cdd:cd05590    3 LGKGSFGKVMLARLKESgrLYAVKVLKkdvilQDDDVECTMTEKRILS----LAR-NHPFLTQL--------YCCFqtpd 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 287 ----VYGFLPNGSLedQLHLQTqaCSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLA 362
Cdd:cd05590   70 rlffVMEFVNGGDL--MFHIQK--SRRFDEARARFYAAEITSALMFLH--DKGIIYRDLKLDNVLLDHEGHCKLADFGMC 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 363 RFSRFAGANpsqsstvarTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAKTKY---LKDLI- 438
Cdd:cd05590  144 KEGIFNGKT---------TSTFCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFeaiLNDEVv 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 189011594 439 -----EDEAEEVGVTLKSTQPTLWMGVATDAWTAPIAAQIYKKHLD 479
Cdd:cd05590  215 yptwlSQDAVDILKAFMTKNPTMRLGSLTLGGEEAILRHPFFKELD 260
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
211-421 4.31e-11

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


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 64.28  E-value: 4.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 211 NFSEELRIGEGGFGCVYRAV--MRNTTYAVKRLK--EEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCL 286
Cdd:cd08228    3 NFQIEKKIGRGQFSEVYRATclLDRKPVALKKVQifEMMDAK---ARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 287 VYGFLPNGSLEDQL-HLQTQAcspLSWPQRL--DILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLAR 363
Cdd:cd08228   80 VLELADAGDLSQMIkYFKKQK---RLIPERTvwKYFVQLCSAVEHMH--SRRVMHRDIKPANVFITATGVVKLGDLGLGR 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594 364 FsrFAGANPSQSSTVartctvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd08228  155 F--FSSKTTAAHSLV-------GTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQ 203
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
217-363 4.37e-11

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: 64.09  E-value: 4.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNT--TYAVKRLKeeadlewtvvkQSF--------LTEVEQLSRF-RHPNIVDFAGYCAESGFYC 285
Cdd:cd07830    6 QLGDGTFGSVYLARNKETgeLVAIKKMK-----------KKFysweecmnLREVKSLRKLnEHPNIVKLKEVFRENDELY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 286 LVYGFLpNGSLEdQLhLQTQACSPLSWPQRLDILLGTARAIQFLHQdspsliHG----DIKSSNVLLDERLMPKLGDFGL 361
Cdd:cd07830   75 FVFEYM-EGNLY-QL-MKDRKGKPFSESVIRSIIYQILQGLAHIHK------HGffhrDLKPENLLVSGPEVVKIADFGL 145

                 ..
gi 189011594 362 AR 363
Cdd:cd07830  146 AR 147
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
212-421 4.46e-11

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


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 63.78  E-value: 4.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELriGEGGFGCVYRAVMRNTTYAVKrlkeeadleWTVVK---------QSFLTEVEQLSRFRHPNIVDFAGYCAESG 282
Cdd:cd13983    5 FNEVL--GRGSFKTVYRAFDTEEGIEVA---------WNEIKlrklpkaerQRFKQEIEILKSLKHPNIIKFYDSWESKS 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 283 FYCLVY--GFLPNGSLEDQL----HLQTQACSplSWPQRldILLGtaraIQFLHQDSPSLIHGDIKSSNVLLDERL-MPK 355
Cdd:cd13983   74 KKEVIFitELMTSGTLKQYLkrfkRLKLKVIK--SWCRQ--ILEG----LNYLHTRDPPIIHRDLKCDNIFINGNTgEVK 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 356 LGDFGLARFSRfaganpsQSSTVartcTVRGTLAYL-PEEYIKTGRLAVdtDTFSFGVVILETLAGQ 421
Cdd:cd13983  146 IGDLGLATLLR-------QSFAK----SVIGTPEFMaPEMYEEHYDEKV--DIYAFGMCLLEMATGE 199
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
215-439 4.84e-11

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 63.97  E-value: 4.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 215 ELR----IGEGGFGCVYRAVM----RNTTY--AVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFy 284
Cdd:cd05057    8 ELEkgkvLGSGAFGTVYKGVWipegEKVKIpvAIKVLREETGPK---ANEEILDEAYVMASVDHPHLVRLLGICLSSQV- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 285 CLVYGFLPNGSLEDQLHLQTQACSP---LSWPQRLdillgtARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGL 361
Cdd:cd05057   84 QLITQLMPLGCLLDYVRNHRDNIGSqllLNWCVQI------AKGMSYLEEKR--LVHRDLAARNVLVKTPNHVKITDFGL 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 362 ARFsrfagANPSQSSTVARTCTVrgTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLA-GQRAVrtQGAKTKYLKDLIE 439
Cdd:cd05057  156 AKL-----LDVDEKEYHAEGGKV--PIKWMALESIQYRIYTHKSDVWSYGVTVWELMTfGAKPY--EGIPAVEIPDLLE 225
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
212-418 5.99e-11

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: 63.79  E-value: 5.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELR-IGEGGFG----CVYRAVMRNT--TYAVKRLKEE------ADLEwtvvkqsflTEVEQLSRFRHPNIVDFAGYC 278
Cdd:cd05079    5 FLKRIRdLGEGHFGkvelCRYDPEGDNTgeQVAVKSLKPEsggnhiADLK---------KEIEILRNLYHENIVKYKGIC 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 279 AESGFYC--LVYGFLPNGSLEDQLhlqTQACSPLSWPQRLDILLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKL 356
Cdd:cd05079   76 TEDGGNGikLIMEFLPSGSLKEYL---PRNKNKINLKQQLKYAVQICKGMDYL--GSRQYVHRDLAARNVLVESEHQVKI 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 357 GDFGLARfsrfaganpsQSSTVARTCTVRGTLA-----YLPEEYIKTgRLAVDTDTFSFGVVILETL 418
Cdd:cd05079  151 GDFGLTK----------AIETDKEYYTVKDDLDspvfwYAPECLIQS-KFYIASDVWSFGVTLYELL 206
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
212-519 6.13e-11

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 63.86  E-value: 6.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELriGEGGFGCVYRAVM------------------RNTTYAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVD 273
Cdd:cd05095    9 FKEKL--GEGQFGEVHLCEAegmekfmdkdfalevsenQPVLVAVKMLRADANKN---ARNDFLKEIKIMSRLKDPNIIR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 274 FAGYCAESGFYCLVYGFLPNGSLeDQLHLQTQACSPLSWPQrlDILLGTARAIQFL---------HQDSPSLIHGDIKSS 344
Cdd:cd05095   84 LLAVCITDDPLCMITEYMENGDL-NQFLSRQQPEGQLALPS--NALTVSYSDLRFMaaqiasgmkYLSSLNFVHRDLATR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 345 NVLLDERLMPKLGDFGLAR------FSRFAGanpsqsstvartctvRGTLA--YLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd05095  161 NCLVGKNYTIKIADFGMSRnlysgdYYRIQG---------------RAVLPirWMSWESILLGKFTTASDVWAFGVTLWE 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 417 TLAgqrAVRTQGAKTKYLKDLIEDEAEevgvtlkstqptlwmgvatdaWTAPIAAQIYKkhldSRPGPCPPqlglALAQL 496
Cdd:cd05095  226 TLT---FCREQPYSQLSDEQVIENTGE---------------------FFRDQGRQTYL----PQPALCPD----SVYKL 273
                        330       340
                 ....*....|....*....|...
gi 189011594 497 ACCCMHRRAKKRPPMTQVYKRLE 519
Cdd:cd05095  274 MLSCWRRDTKDRPSFQEIHTLLQ 296
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
211-421 6.70e-11

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: 63.23  E-value: 6.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 211 NFSEELRIGEGGFGCVYRAVMRNT--TYAVKRLkeeaDLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVY 288
Cdd:cd06648    8 DLDNFVKIGEGSTGIVCIATDKSTgrQVAVKKM----DLRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 289 GFLPNGSLEDqlhLQTQacSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGlarfsrFA 368
Cdd:cd06648   84 EFLEGGALTD---IVTH--TRMNEEQIATVCRAVLKALSFLH--SQGVIHRDIKSDSILLTSDGRVKLSDFG------FC 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 189011594 369 GanpSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd06648  151 A---QVSKEVPRRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGE 200
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
258-421 6.80e-11

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: 63.15  E-value: 6.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 258 TEVEQLSRFRHPNIVDFAGYCAE------SGFYCLVYGFLPNGSLEDQLHlqtqacSPLSWPqrldilLGTAR------- 324
Cdd:cd14012   47 KELESLKKLRHPNLVSYLAFSIErrgrsdGWKVYLLTEYAPGGSLSELLD------SVGSVP------LDTARrwtlqll 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 325 -AIQFLHqdSPSLIHGDIKSSNVLLDERLM---PKLGDFGLARfsRFAGANPSQSSTVARTCTVRgtlayLPEEYIKTGR 400
Cdd:cd14012  115 eALEYLH--RNGVVHKSLHAGNVLLDRDAGtgiVKLTDYSLGK--TLLDMCSRGSLDEFKQTYWL-----PPELAQGSKS 185
                        170       180
                 ....*....|....*....|.
gi 189011594 401 LAVDTDTFSFGVVILETLAGQ 421
Cdd:cd14012  186 PTRKTDVWDLGLLFLQMLFGL 206
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
218-415 6.87e-11

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: 63.52  E-value: 6.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAV--MRNTTYAVKRLKEEADLE---WTVVKQSFLTEVEQLSRF-RHPNIVDFAGYCAESGFYCLVYGFL 291
Cdd:cd13993    8 IGEGAYGVVYLAVdlRTGRKYAIKCLYKSGPNSkdgNDFQKLPQLREIDLHRRVsRHPNIITLHDVFETEVAIYIVLEYC 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 PNGSLEDQLHL--QTQACSPLSWpqrlDILLGTARAIQFLHqdSPSLIHGDIKSSNVLL---DERLmpKLGDFGLA---R 363
Cdd:cd13993   88 PNGDLFEAITEnrIYVGKTELIK----NVFLQLIDAVKHCH--SLGIYHRDIKPENILLsqdEGTV--KLCDFGLAtteK 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594 364 FSRFAGanpsqsstvartctvRGTLAYL-PEEYIKTGRLA--VDT---DTFSFGVVIL 415
Cdd:cd13993  160 ISMDFG---------------VGSEFYMaPECFDEVGRSLkgYPCaagDIWSLGIILL 202
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
218-420 8.26e-11

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 63.83  E-value: 8.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVM---------RNTTYAVKRLKEEA---DLewtvvkQSFLTEVEQLSRF-RHPNIVDFAGYCAESGFY 284
Cdd:cd05099   20 LGEGCFGQVVRAEAygidksrpdQTVTVAVKMLKDNAtdkDL------ADLISEMELMKLIgKHKNIINLLGVCTQEGPL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 285 CLVYGFLPNGSLEDQLHLQTQAC------------SPLSWPQRLDILLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERL 352
Cdd:cd05099   94 YVIVEYAAKGNLREFLRARRPPGpdytfditkvpeEQLSFKDLVSCAYQVARGMEYL--ESRRCIHRDLAARNVLVTEDN 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 353 MPKLGDFGLARfsrfagaNPSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILE--TLAG 420
Cdd:cd05099  172 VMKIADFGLAR-------GVHDIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEifTLGG 234
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
217-416 8.68e-11

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 63.46  E-value: 8.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVY----------------RAVMRNTTYAVKRLKEEADlewTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAE 280
Cdd:cd05097   12 KLGEGQFGEVHlceaeglaeflgegapEFDGQPVLVAVKMLRADVT---KTARNDFLKEIKIMSRLKNPNIIRLLGVCVS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 281 SGFYCLVYGFLPNGSLeDQLHLQTQACSPL---------SWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDER 351
Cdd:cd05097   89 DDPLCMITEYMENGDL-NQFLSQREIESTFthannipsvSIANLLYMAVQIASGMKYLA--SLNFVHRDLATRNCLVGNH 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189011594 352 LMPKLGDFGLAR------FSRFAGanpsqsstvartctvRGTLA--YLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd05097  166 YTIKIADFGMSRnlysgdYYRIQG---------------RAVLPirWMAWESILLGKFTTASDVWAFGVTLWE 223
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
217-421 8.76e-11

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: 63.59  E-value: 8.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRA--VMRNTTYAVKRLkeeaDLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNG 294
Cdd:cd06655   26 KIGQGASGTVFTAidVATGQEVAIKQI----NLQKQPKKELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAGG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEDQLhlqTQACspLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLArfsrfAGANPSQ 374
Cdd:cd06655  102 SLTDVV---TETC--MDEAQIAAVCRECLQALEFLHANQ--VIHRDIKSDNVLLGMDGSVKLTDFGFC-----AQITPEQ 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 189011594 375 SstvaRTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd06655  170 S----KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGE 212
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
218-416 9.31e-11

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


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 63.51  E-value: 9.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT----TYAVKRLKEEADLEwtvvkqSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPN 293
Cdd:cd06644   20 LGDGAFGKVYKAKNKETgalaAAKVIETKSEEELE------DYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCPG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 294 GSLeDQLHLQTQacSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLArfsrfaganPS 373
Cdd:cd06644   94 GAV-DAIMLELD--RGLTEPQIQVICRQMLEALQYLH--SMKIIHRDLKAGNVLLTLDGDIKLADFGVS---------AK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 189011594 374 QSSTVARTCTVRGTLAYL-PE----EYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd06644  160 NVKTLQRRDSFIGTPYWMaPEvvmcETMKDTPYDYKADIWSLGITLIE 207
Death_IRAK-M cd08796
Death domain of Interleukin 1 Receptor Associated Kinase-M; Death Domain (DD) of Interleukin-1 ...
18-100 1.01e-10

Death domain of Interleukin 1 Receptor Associated Kinase-M; Death Domain (DD) of Interleukin-1 Receptor-Associated Kinase M (IRAK-M). IRAKs are essential components of innate immunity and inflammation in mammals and other vertebrates. They are involved in signal transduction pathways involving IL-1 and IL-18 receptors, Toll-like receptors(TLRs), nuclear factor-kappaB (NF-kB), and mitogen-activated protein kinases (MAPKs). IRAKs contain an N-terminal DD domain and a C-terminal kinase domain. IRAK-M, also called IRAK-3, is an inactive kinase present only in macrophages in an inducible manner. It is a negative regulator of TLR signaling and it contributes to the attenuation of NF-kB activation. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260062  Cd Length: 89  Bit Score: 58.72  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594  18 FLYEVPPWVMCRFYKVMD-ALEPADWCQFAALIVRDQTELRLCERSEQR----TASVLWPWINRNARVADLVHILTHLQL 92
Cdd:cd08796    2 LLFDVPPVLMEKFCALLDsGDDSLGWRGLAERISSSWLEVRHIEKYVAQgkspTRELLWSWAQKNKTVGDLLKVLEDMGH 81

                 ....*...
gi 189011594  93 LRARDIIT 100
Cdd:cd08796   82 YRAIQLFT 89
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
212-421 1.02e-10

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


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 63.15  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELRIGEGGFGCVYRAVmRNTTYAVKRLK----EEADLEWTVVKQsfltEVEQLSRFRHPNIVDFAGYCAESGFYCLV 287
Cdd:cd06642    6 FTKLERIGKGSFGEVYKGI-DNRTKEVVAIKiidlEEAEDEIEDIQQ----EITVLSQCDSPYITRYYGSYLKGTKLWII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 288 YGFLPNGSLEDQLHlqtqaCSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLArfsrf 367
Cdd:cd06642   81 MEYLGGGSALDLLK-----PGPLEETYIATILREILKGLDYLH--SERKIHRDIKAANVLLSEQGDVKLADFGVA----- 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 189011594 368 aganPSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd06642  149 ----GQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGE 198
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
218-367 1.11e-10

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk 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: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 62.99  E-value: 1.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRA-VMRNTTYA---VKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPN 293
Cdd:cd05042    3 IGNGWFGKVLLGeIYSGTSVAqvvVKELKASANPK---EQDTFLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFCDL 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 294 GSLEDQLHLQTQACSPLSWPQRLD-ILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLArFSRF 367
Cdd:cd05042   80 GDLKAYLRSEREHERGDSDTRTLQrMACEVAAGLAHLH--KLNFVHSDLALRNCLLTSDLTVKIGDYGLA-HSRY 151
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
218-416 1.34e-10

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC 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: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 62.72  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT-------YAVKRLKEEAdlewTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGF 290
Cdd:cd05094   13 LGEGAFGKVFLAECYNLSptkdkmlVAVKTLKDPT----LAARKDFQREAELLTNLQHDHIVKFYGVCGDGDPLIMVFEY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDQLHLQ------------TQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGD 358
Cdd:cd05094   89 MKHGDLNKFLRAHgpdamilvdgqpRQAKGELGLSQMLHIATQIASGMVYLA--SQHFVHRDLATRNCLVGANLLVKIGD 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594 359 FGLAR------FSRFAGANpsqsstvarTCTVRgtlaYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd05094  167 FGMSRdvystdYYRVGGHT---------MLPIR----WMPPESIMYRKFTTESDVWSFGVILWE 217
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
218-422 1.52e-10

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: 62.50  E-value: 1.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT--YAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAgYCAESGFY-CLVYGFLPNG 294
Cdd:cd05611    4 ISKGAFGSVYLAKKRSTGdyFAIKVLKKSDMIAKNQVTNVKAERAIMMIQGESPYVAKLY-YSFQSKDYlYLVMEYLNGG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEDQLhlQTQACSPLSWPQRL--DILLGtaraIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAGANP 372
Cdd:cd05611   83 DCASLI--KTLGGLPEDWAKQYiaEVVLG----VEDLHQRG--IIHRDIKPENLLIDQTGHLKLTDFGLSRNGLEKRHNK 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 189011594 373 SQSstvartctvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQR 422
Cdd:cd05611  155 KFV----------GTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYP 194
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
217-363 1.57e-10

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: 62.44  E-value: 1.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEWtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLpng 294
Cdd:cd07861    7 KIGEGTYGVVYKGRNKKTgqIVAMKKIRLESEEEG--VPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEFL--- 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 295 SLEDQLHLQTqacspLSWPQRLDILLGTA------RAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLAR 363
Cdd:cd07861   82 SMDLKKYLDS-----LPKGKYMDAELVKSylyqilQGILFCH--SRRVLHRDLKPQNLLIDNKGVIKLADFGLAR 149
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
218-420 1.73e-10

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: 62.24  E-value: 1.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVY--RAVMRNTTYAVKRLKEEADLEWTVVKQSFLtEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd05572    1 LGVGGFGRVElvQLKSKGRTFALKCVKKRHIVQTRQQEHIFS-EKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLH-------LQTQ---ACsplswpqrldILLgtarAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfs 365
Cdd:cd05572   80 LWTILRdrglfdeYTARfytAC----------VVL----AFEYLH--SRGIIYRDLKPENLLLDSNGYVKLVDFGFAK-- 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 366 rfaganpsQSSTVARTCTVRGTLAYLPEEYI--KTGRLAVdtDTFSFGVVILETLAG 420
Cdd:cd05572  142 --------KLGSGRKTWTFCGTPEYVAPEIIlnKGYDFSV--DYWSLGILLYELLTG 188
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
218-416 1.87e-10

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


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 62.50  E-value: 1.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGcvyrAVMRNTTY-----------AVKRLKEEADLEwtvVKQSFLTEVEQLSRF-RHPNIVDFAGYCAESGFYC 285
Cdd:cd05055   43 LGAGAFG----KVVEATAYglsksdavmkvAVKMLKPTAHSS---EREALMSELKIMSHLgNHENIVNLLGACTIGGPIL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 286 LVYGFLPNGSLEDQLHLQTQacSPLSWPQRLDILLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFS 365
Cdd:cd05055  116 VITEYCCYGDLLNFLRRKRE--SFLTLEDLLSFSYQVAKGMAFL--ASKNCIHRDLAARNVLLTHGKIVKICDFGLARDI 191
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 189011594 366 RfaganpSQSSTVARTCTvRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd05055  192 M------NDSNYVVKGNA-RLPVKWMAPESIFNCVYTFESDVWSYGILLWE 235
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
217-421 2.28e-10

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: 62.43  E-value: 2.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRA--VMRNTTYAVKRLkeeaDLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNG 294
Cdd:cd06654   27 KIGQGASGTVYTAmdVATGQEVAIRQM----NLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEDQLhlqTQACspLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLArfsrfAGANPSQ 374
Cdd:cd06654  103 SLTDVV---TETC--MDEGQIAAVCRECLQALEFLH--SNQVIHRDIKSDNILLGMDGSVKLTDFGFC-----AQITPEQ 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 189011594 375 SstvaRTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd06654  171 S----KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGE 213
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
218-449 2.52e-10

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: 61.77  E-value: 2.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLkEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAgYCAES-GFYCLVYGFLPNG 294
Cdd:cd05577    1 LGRGGFGEVCACQVKATgkMYACKKL-DKKRIKKKKGETMALNEKIILEKVSSPFIVSLA-YAFETkDKLCLVLTLMNGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLedQLHLQTQACSPLSWPQRL----DILLGtaraIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLArfSRFAGA 370
Cdd:cd05577   79 DL--KYHIYNVGTRGFSEARAIfyaaEIICG----LEHLHNRF--IVYRDLKPENILLDDHGHVRISDLGLA--VEFKGG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 371 NPSQSSTvartctvrGTLAYLPEEYIKTGRL-AVDTDTFSFGVVILETLAGQRAVRTQGAKTKylKDLIEDEAEEVGVTL 449
Cdd:cd05577  149 KKIKGRV--------GTHGYMAPEVLQKEVAyDFSVDWFALGCMLYEMIAGRSPFRQRKEKVD--KEELKRRTLEMAVEY 218
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
212-420 2.60e-10

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: 61.79  E-value: 2.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELriGEGGFGCVYRAVMRNT--TYAVKRLKEEADlEWTVvkQSFLTEVEQLSRFRHPNIVDFAG--YCAESGFYCLV 287
Cdd:cd06622    5 VLDEL--GKGNYGSVYKVLHRPTgvTMAMKEIRLELD-ESKF--NQIIMELDILHKAVSPYIVDFYGafFIEGAVYMCME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 288 YgfLPNGSLeDQLHLQTQACSPLSWPQRLDILLGTARAIQFLHQDSpSLIHGDIKSSNVLLDERLMPKLGDFGLArfsrf 367
Cdd:cd06622   80 Y--MDAGSL-DKLYAGGVATEGIPEDVLRRITYAVVKGLKFLKEEH-NIIHRDVKPTNVLVNGNGQVKLCDFGVS----- 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 368 agANPSQSstVARTCTvrGTLAYLPEEYIKTGRL------AVDTDTFSFGVVILETLAG 420
Cdd:cd06622  151 --GNLVAS--LAKTNI--GCQSYMAPERIKSGGPnqnptyTVQSDVWSLGLSILEMALG 203
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
217-362 2.75e-10

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


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 61.58  E-value: 2.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRA--VMRNTTYAVKRLKEEADLEWTVVKQsfltEVEQLSRFRHPNIVDFAG--YCAESGFYCLVYgfLP 292
Cdd:cd06646   16 RVGSGTYGDVYKArnLHTGELAAVKIIKLEPGDDFSLIQQ----EIFMVKECKHCNIVAYFGsyLSREKLWICMEY--CG 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLEDQLHLQtqacSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLA 362
Cdd:cd06646   90 GGSLQDIYHVT----GPLSELQIAYVCRETLQGLAYLH--SKGKMHRDIKGANILLTDNGDVKLADFGVA 153
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
217-362 2.81e-10

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: 61.60  E-value: 2.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEWTVVKQsfltEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNG 294
Cdd:cd06645   18 RIGSGTYGDVYKARNVNTgeLAAIKVIKLEPGEDFAVVQQ----EIIMMKDCKHSNIVAYFGSYLRRDKLWICMEFCGGG 93
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594 295 SLEDQLHLQtqacSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLA 362
Cdd:cd06645   94 SLQDIYHVT----GPLSESQIAYVSRETLQGLYYLH--SKGKMHRDIKGANILLTDNGHVKLADFGVS 155
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
218-416 3.19e-10

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


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 61.58  E-value: 3.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTY--AVKRL--KEEADLEwtvvkqSFLTEVEQLSRFRHPNIVDFA-GYCAESGFYCLVYgFLP 292
Cdd:cd06643   13 LGDGAFGKVYKAQNKETGIlaAAKVIdtKSEEELE------DYMVEIDILASCDHPNIVKLLdAFYYENNLWILIE-FCA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLeDQLHLQTQacSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLArfsrfaganP 372
Cdd:cd06643   86 GGAV-DAVMLELE--RPLTEPQIRVVCKQTLEALVYLHENK--IIHRDLKAGNILFTLDGDIKLADFGVS---------A 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 189011594 373 SQSSTVARTCTVRGTLAYLPEEYI-----KTGRLAVDTDTFSFGVVILE 416
Cdd:cd06643  152 KNTRTLQRRDSFIGTPYWMAPEVVmcetsKDRPYDYKADVWSLGVTLIE 200
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
217-363 3.45e-10

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: 61.54  E-value: 3.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEWtvVKQSFLTEVEQLSRFRHPNIVDFagYC---AESGFYcLVYGFL 291
Cdd:cd07835    6 KIGEGTYGVVYKARDKLTgeIVALKKIRLETEDEG--VPSTAIREISLLKELNHPNIVRL--LDvvhSENKLY-LVFEFL 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 292 pngsleDQ-LHLQTQACSPLSWPQRL--DILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLAR 363
Cdd:cd07835   81 ------DLdLKKYMDSSPLTGLDPPLikSYLYQLLQGIAFCH--SHRVLHRDLKPQNLLIDTEGALKLADFGLAR 147
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
218-420 3.86e-10

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: 60.88  E-value: 3.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAvmRNTT----YAVKRLKEEADLEWTVVKQsFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPN 293
Cdd:cd14663    8 LGEGTFAKVKFA--RNTKtgesVAIKIIDKEQVAREGMVEQ-IKREIAIMKLLRHPNIVELHEVMATKTKIFFVMELVTG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 294 GSLEDQLhlqtQACSPLS------WPQRLdillgtARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLArfsrf 367
Cdd:cd14663   85 GELFSKI----AKNGRLKedkarkYFQQL------IDAVDYCH--SRGVFHRDLKPENLLLDEDGNLKISDFGLS----- 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 189011594 368 agANPSQSSTVARTCTVRGTLAYL-PEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd14663  148 --ALSEQFRQDGLLHTTCGTPNYVaPEVLARRGYDGAKADIWSCGVILFVLLAG 199
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
218-435 4.22e-10

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: 61.10  E-value: 4.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEwTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd14187   15 LGKGGFAKCYEITDADTkeVFAGKIVPKSLLLK-PHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEdQLHLQTQAcspLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAGanpsqs 375
Cdd:cd14187   94 LL-ELHKRRKA---LTEPEARYYLRQIILGCQYLH--RNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDG------ 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189011594 376 stvARTCTVRGTLAYL-PEEYIKTGRlAVDTDTFSFGVVILETLAGQRAVRTQGAKTKYLK 435
Cdd:cd14187  162 ---ERKKTLCGTPNYIaPEVLSKKGH-SFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLR 218
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
218-422 4.24e-10

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 61.04  E-value: 4.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVM-----RNTTYAVKRLKEEADLEWtvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLP 292
Cdd:cd05066   12 IGAGEFGEVCSGRLklpgkREIPVAIKTLKAGYTEKQ---RRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYME 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLEDQLHLQTQACSPLswpQRLDILLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLarfSRFAGANP 372
Cdd:cd05066   89 NGSLDAFLRKHDGQFTVI---QLVGMLRGIASGMKYL--SDMGYVHRDLAARNILVNSNLVCKVSDFGL---SRVLEDDP 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 189011594 373 SQS-STVARTCTVRGTlaylPEEYIKTGRLAVDTDTFSFGVVILETLA-GQR 422
Cdd:cd05066  161 EAAyTTRGGKIPIRWT----APEAIAYRKFTSASDVWSYGIVMWEVMSyGER 208
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
211-421 4.28e-10

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 61.59  E-value: 4.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 211 NFSEELRIGEGGFGCVYRA--VMRNTTYAVKRLkEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVY 288
Cdd:cd08229   25 NFRIEKKIGRGQFSEVYRAtcLLDGVPVALKKV-QIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 289 GFLPNGSLEDQL-HLQTQAcspLSWPQRL--DILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFs 365
Cdd:cd08229  104 ELADAGDLSRMIkHFKKQK---RLIPEKTvwKYFVQLCSALEHMH--SRRVMHRDIKPANVFITATGVVKLGDLGLGRF- 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 189011594 366 rFAGANPSQSSTVartctvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd08229  178 -FSSKTTAAHSLV-------GTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQ 225
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
218-421 4.93e-10

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: 61.50  E-value: 4.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVM--RNTTYAVKRLKEEA-----DLEWTVVKQSFLTEVEQLSRFRHPnivdfagYCA----ESGFYcl 286
Cdd:cd05620    3 LGKGSFGKVLLAELkgKGEYFAVKALKKDVvliddDVECTMVEKRVLALAWENPFLTHL-------YCTfqtkEHLFF-- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 287 VYGFLPNGSLedQLHLQTQAcsplswpqRLDILLGTARA------IQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFG 360
Cdd:cd05620   74 VMEFLNGGDL--MFHIQDKG--------RFDLYRATFYAaeivcgLQFLH--SKGIIYRDLKLDNVMLDRDGHIKIADFG 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189011594 361 LARFSRFaGANpsqsstvaRTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd05620  142 MCKENVF-GDN--------RASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQ 193
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
218-420 5.04e-10

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: 60.95  E-value: 5.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRA--VMRNTTYAVKRLKEEADLEWTVVKQSfltEVEQLSRFRH---PNIVDFAGYCAESGFYCLVYGFLP 292
Cdd:cd06917    9 VGRGSYGAVYRGyhVKTGRVVALKVLNLDTDDDDVSDIQK---EVALLSQLKLgqpKNIIKYYGSYLKGPSLWIIMDYCE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLEDQLHLQtqacsPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLArfsrfaganP 372
Cdd:cd06917   86 GGSIRTLMRAG-----PIAERYIAVIMREVLVALKFIHKDG--IIHRDIKAANILVTNTGNVKLCDFGVA---------A 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 189011594 373 SQSSTVARTCTVRGTLAYLPEEYIKTGRL-AVDTDTFSFGVVILETLAG 420
Cdd:cd06917  150 SLNQNSSKRSTFVGTPYWMAPEVITEGKYyDTKADIWSLGITTYEMATG 198
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
218-433 5.12e-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: 60.71  E-value: 5.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRA--VMRNTTYAVKRLKEeADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFyclVYGFLPNGS 295
Cdd:cd14189    9 LGKGGFARCYEMtdLATNKTYAVKVIPH-SRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAEN---IYIFLELCS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLHLQtQACSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLArfsrfAGANPSQS 375
Cdd:cd14189   85 RKSLAHIW-KARHTLLEPEVRYYLKQIISGLKYLHLKG--ILHRDLKLGNFFINENMELKVGDFGLA-----ARLEPPEQ 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 376 stvaRTCTVRGTLAYL-PEEYIKTGRlAVDTDTFSFGVVILETLAGQRAVRTQGAKTKY 433
Cdd:cd14189  157 ----RKKTICGTPNYLaPEVLLRQGH-GPESDVWSLGCVMYTLLCGNPPFETLDLKETY 210
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
218-421 5.96e-10

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: 60.39  E-value: 5.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRA--VMRNTTYAVKRL-KEEADLEWTvvkQSFLT-EVEQLSRFRHPNIVDFagYCA---ESGFYcLVYGF 290
Cdd:cd14162    8 LGHGSYAVVKKAysTKHKCKVAIKIVsKKKAPEDYL---QKFLPrEIEVIKGLKHPNLICF--YEAietTSRVY-IIMEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDQLHLQTQACSPLS---WPQRLDillgtarAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRF 367
Cdd:cd14162   82 AENGDLLDYIRKNGALPEPQArrwFRQLVA-------GVEYCH--SKGVVHRDLKCENLLLDKNNNLKITDFGFARGVMK 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 368 AGANPSQSSTvartcTVRGTLAYLPEEYIKTgrLAVD---TDTFSFGVVILETLAGQ 421
Cdd:cd14162  153 TKDGKPKLSE-----TYCGSYAYASPEILRG--IPYDpflSDIWSMGVVLYTMVYGR 202
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
212-418 6.06e-10

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: 60.98  E-value: 6.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELRIGEGGFGCVYRAvmRNTT----YAVKRLKEEADLEWTVVKqsFLTEVEQLSRFRHPNIVDFAGYCAEsgfyclv 287
Cdd:cd14049    8 FEEIARLGKGGYGKVYKV--RNKLdgqyYAIKKILIKKVTKRDCMK--VLREVKVLAGLQHPNIVGYHTAWME------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 288 ygflpngSLEDQLHLQTQACSPLSW---------------------PQRLDILLGTARAI----QFLHqdSPSLIHGDIK 342
Cdd:cd14049   77 -------HVQLMLYIQMQLCELSLWdwivernkrpceeefksapytPVDVDVTTKILQQLlegvTYIH--SMGIVHRDLK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 343 SSNVLLD-ERLMPKLGDFGLARFSRFAGANPSQSSTVARTCTVR---GTLAYLPEEYIKTGRLAVDTDTFSFGVVILETL 418
Cdd:cd14049  148 PRNIFLHgSDIHVRIGDFGLACPDILQDGNDSTTMSRLNGLTHTsgvGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF 227
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
218-432 6.71e-10

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: 60.67  E-value: 6.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVK-----RLKEEADLEWTVVKQSFLTEVEqlSRFrhpnIVDFAGYCAESGFYCLVYGF 290
Cdd:cd05608    9 LGKGGFGEVSACQMRATgkLYACKklnkkRLKKRKGYEGAMVEKRILAKVH--SRF----IVSLAYAFQTKTDLCLVMTI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDQLHLQTQACSPLSWPQRL----DILLGtaraIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLArFSR 366
Cdd:cd05608   83 MNGGDLRYHIYNVDEENPGFQEPRACfytaQIISG----LEHLHQRR--IIYRDLKPENVLLDDDGNVRISDLGLA-VEL 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189011594 367 FAGANpsqsstvaRTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAKTK 432
Cdd:cd05608  156 KDGQT--------KTKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARGEKVE 213
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
252-364 6.75e-10

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-2D is allso called Retinal Guanylyl Cyclase 1 (RETGC-1) or Rod Outer Segment membrane Guanylate Cyclase (ROS-GC). It is found in the photoreceptors of the retina where it anchors the reciprocal feedback loop between calcium and cGMP, which regulates the dark, light, and recovery phases in phototransduction. It is also found in other sensory neurons and may be a universal transduction component that plays a role in the perception of all senses. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-2D subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 60.50  E-value: 6.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 252 VKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLEDQLhlqTQACSPLSWPQRLDILLGTARAIQFLHq 331
Cdd:cd14043   39 LRPSTKNVFSKLRELRHENVNLFLGLFVDCGILAIVSEHCSRGSLEDLL---RNDDMKLDWMFKSSLLLDLIKGMRYLH- 114
                         90       100       110
                 ....*....|....*....|....*....|...
gi 189011594 332 dSPSLIHGDIKSSNVLLDERLMPKLGDFGLARF 364
Cdd:cd14043  115 -HRGIVHGRLKSRNCVVDGRFVLKITDYGYNEI 146
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
217-421 6.88e-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: 60.89  E-value: 6.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRA--VMRNTTYAVKRLkeeaDLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNG 294
Cdd:cd06656   26 KIGQGASGTVYTAidIATGQEVAIKQM----NLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEDQLhlqTQACspLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLArfsrfAGANPSQ 374
Cdd:cd06656  102 SLTDVV---TETC--MDEGQIAAVCRECLQALDFLH--SNQVIHRDIKSDNILLGMDGSVKLTDFGFC-----AQITPEQ 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 189011594 375 SstvaRTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd06656  170 S----KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGE 212
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
212-349 7.49e-10

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


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 60.50  E-value: 7.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELRIGEGGFGCVYRAVMR--NTTYAVKRLKEEadLEWTVVKQSFLTEVEQLSRF-RHPNIVDFAGYCAESGFYCLVY 288
Cdd:cd14051    2 FHEVEKIGSGEFGSVYKCINRldGCVYAIKKSKKP--VAGSVDEQNALNEVYAHAVLgKHPHVVRYYSAWAEDDHMIIQN 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189011594 289 GFLPNGSLEDQLHLQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLD 349
Cdd:cd14051   80 EYCNGGSLADAISENEKAGERFSEAELKDLLLQVAQGLKYIH--SQNLVHMDIKPGNIFIS 138
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
212-416 7.80e-10

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 60.19  E-value: 7.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELriGEGGFGCVYRAVMRNTTYAVKRLKEeadlewtVVKQ-----------SFLTEVEQLSRFRHPNIVDFAGYCAE 280
Cdd:cd05037    3 FHEHL--GQGTFTNIYDGILREVGDGRVQEVE-------VLLKvldsdhrdiseSFFETASLMSQISHKHLVKLYGVCVA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 281 SGfYCLVYGFLPNGSLEDQLHLQTQaCSPLSWpqRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLderlmPKLGDFG 360
Cdd:cd05037   74 DE-NIMVQEYVRYGPLDKYLRRMGN-NVPLSW--KLQVAKQLASALHYLEDKK--LIHGNVRGRNILL-----AREGLDG 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594 361 LARFSRFagANPSQSSTVARTCTVRGTLAYLPEEYIKTGR--LAVDTDTFSFGVVILE 416
Cdd:cd05037  143 YPPFIKL--SDPGVPITVLSREERVDRIPWIAPECLRNLQanLTIAADKWSFGTTLWE 198
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
218-416 8.27e-10

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 60.41  E-value: 8.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTY----AVKRLK----EEADLEwtvvkqSFLTEVEQLSRFRHPNIVDFAGYC---AESGFY-- 284
Cdd:cd05075    8 LGEGEFGSVMEGQLNQDDSvlkvAVKTMKiaicTRSEME------DFLSEAVCMKEFDHPNVMRLIGVClqnTESEGYps 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 285 -CLVYGFLPNGSLEDQLHLQTQACSPLSWPQRLDILLGT--ARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKLGDFGL 361
Cdd:cd05075   82 pVVILPFMKHGDLHSFLLYSRLGDCPVYLPTQMLVKFMTdiASGMEYL--SSKNFIHRDLAARNCMLNENMNVCVADFGL 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 362 ARfSRFAGANPSQsstvartctvrGTLAYLPEEYIKTGRLA-----VDTDTFSFGVVILE 416
Cdd:cd05075  160 SK-KIYNGDYYRQ-----------GRISKMPVKWIAIESLAdrvytTKSDVWSFGVTMWE 207
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
218-465 8.55e-10

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: 59.87  E-value: 8.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRN--TTYAVK---RLKEEADLewtvVKQSFLTEVEQLSRFRHPNIVD-FAGYCAESGFYCLVYgfl 291
Cdd:cd14164    8 IGEGSFSKVKLATSQKycCKVAIKivdRRRASPDF----VQKFLPRELSILRRVNHPNIVQmFECIEVANGRLYIVM--- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 pnGSLEDQLHLQTQACSPLSWPQRLDILLGTARAIQFLHQDspSLIHGDIKSSNVLL--DERLMpKLGDFGlarFSRFAG 369
Cdd:cd14164   81 --EAAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDM--NIVHRDLKCENILLsaDDRKI-KIADFG---FARFVE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 370 ANPSQSSTVArtctvrGTLAYL-PEEYIKTGRLAVDTDTFSFGVVILETLAGQ--------RAVRTQGAKTKYLKDLIED 440
Cdd:cd14164  153 DYPELSTTFC------GSRAYTpPEVILGTPYDPKKYDVWSLGVVLYVMVTGTmpfdetnvRRLRLQQRGVLYPSGVALE 226
                        250       260       270
                 ....*....|....*....|....*....|
gi 189011594 441 EAEEVGV-----TLKSTQPTLWMgVATDAW 465
Cdd:cd14164  227 EPCRALIrtllqFNPSTRPSIQQ-VAGNSW 255
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
257-421 8.70e-10

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 62.17  E-value: 8.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 257 LTEVEQLSRFRHPNIVDFAGYC-AESGFYcLVYGFLPNGSLedqlhlqTQACSPLSWPQRLDILLGTARAIQFLH-QDSP 334
Cdd:PLN00113 731 SSEIADMGKLQHPNIVKLIGLCrSEKGAY-LIHEYIEGKNL-------SEVLRNLSWERRRKIAIGIAKALRFLHcRCSP 802
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 335 SLIHGDIKSSNVLLDERLMPKLgdfglaRFSrfaganPSQSSTVARTCTVRGtlAYLPEEYIKTGRLAVDTDTFSFGVVI 414
Cdd:PLN00113 803 AVVVGNLSPEKIIIDGKDEPHL------RLS------LPGLLCTDTKCFISS--AYVAPETRETKDITEKSDIYGFGLIL 868

                 ....*..
gi 189011594 415 LETLAGQ 421
Cdd:PLN00113 869 IELLTGK 875
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
212-420 8.82e-10

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: 60.12  E-value: 8.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELrIGEGGFGCVYRAVMRNT--TYAVKRL-------KEEADLEwtvvkqsflTEVEQLSRFRHPNIVDFAGYCAESG 282
Cdd:cd14082    6 FPDEV-LGSGQFGIVYGGKHRKTgrDVAIKVIdklrfptKQESQLR---------NEVAILQQLSHPGVVNLECMFETPE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 283 FYCLVYGFLPNGSLEDQLhlqtqaCSPLS-WPQRLDILLGTA--RAIQFLHqdSPSLIHGDIKSSNVLL-DERLMP--KL 356
Cdd:cd14082   76 RVFVVMEKLHGDMLEMIL------SSEKGrLPERITKFLVTQilVALRYLH--SKNIVHCDLKPENVLLaSAEPFPqvKL 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594 357 GDFGlarFSRFAGANPSQSSTVartctvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd14082  148 CDFG---FARIIGEKSFRRSVV-------GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSG 201
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
212-441 8.84e-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: 60.30  E-value: 8.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELRIGEGGFGCVYRAVMRNT--TYAVKRLkEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAgYCAESGFY-CLVY 288
Cdd:cd05607    4 FYEFRVLGKGGFGEVCAVQVKNTgqMYACKKL-DKKRLKKKSGEKMALLEKEILEKVNSPFIVSLA-YAFETKTHlCLVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 289 GFLPNGSLEDQLHLQTQACSPLSwpqrlDILLGTAR-AIQFLHQDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrf 367
Cdd:cd05607   82 SLMNGGDLKYHIYNVGERGIEME-----RVIFYSAQiTCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAV---- 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 368 agANPSQSSTVARTctvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ---RAVRTQGAKTKYLKDLIEDE 441
Cdd:cd05607  153 --EVKEGKPITQRA----GTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRtpfRDHKEKVSKEELKRRTLEDE 223
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
218-420 9.98e-10

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: 60.75  E-value: 9.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMR--NTTYAVKRLKeeadlewtvvKQSFLTEVEQ----------LSRFRHPNIV--DFAGYCAESGF 283
Cdd:cd05603    3 IGKGSFGKVLLAKRKcdGKFYAVKVLQ----------KKTILKKKEQnhimaernvlLKNLKHPFLVglHYSFQTSEKLY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 284 YCLVYgflPNGSlEDQLHLQTQACspLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLAR 363
Cdd:cd05603   73 FVLDY---VNGG-ELFFHLQRERC--FLEPRARFYAAEVASAIGYLH--SLNIIYRDLKPENILLDCQGHVVLTDFGLCK 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 364 fsrfAGANPSQSstvarTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd05603  145 ----EGMEPEET-----TSTFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYG 192
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
217-363 1.00e-09

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: 60.65  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNT--TYAVKR----LKEEADLEWTVVKQSFLTEVEQlsrfrHPNIVD-FAGYCAESG--FYcLV 287
Cdd:cd07852   14 KLGKGAYGIVWKAIDKKTgeVVALKKifdaFRNATDAQRTFREIMFLQELND-----HPNIIKlLNVIRAENDkdIY-LV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 288 YGFLPN--------GSLEDqLHLQTqacsplswpqrldILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDF 359
Cdd:cd07852   88 FEYMETdlhaviraNILED-IHKQY-------------IMYQLLKALKYLH--SGGVIHRDLKPSNILLNSDCRVKLADF 151

                 ....
gi 189011594 360 GLAR 363
Cdd:cd07852  152 GLAR 155
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
212-421 1.00e-09

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: 60.09  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELRIGEGGFGCVYRAVMRNT--TYAVKRLK-EEADLEWTVVKQsfltEVEQLSRFRHPNIVDFAGYCAESGFYCLVY 288
Cdd:cd06641    6 FTKLEKIGKGSFGEVFKGIDNRTqkVVAIKIIDlEEAEDEIEDIQQ----EITVLSQCDSPYVTKYYGSYLKDTKLWIIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 289 GFLPNGSLEDQLHlqtqaCSPLSWPQRLDILLGTARAIQFLHQDSPslIHGDIKSSNVLLDERLMPKLGDFGLarfsrfa 368
Cdd:cd06641   82 EYLGGGSALDLLE-----PGPLDETQIATILREILKGLDYLHSEKK--IHRDIKAANVLLSEHGEVKLADFGV------- 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 189011594 369 gANPSQSSTVARTCTVrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd06641  148 -AGQLTDTQIKRN*FV-GTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGE 198
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
212-421 1.07e-09

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: 60.07  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELRIGEGGFGCVYRAVmRNTTYAVKRLK----EEADLEWTVVKQsfltEVEQLSRFRHPNIVDFAGYCAESGFYCLV 287
Cdd:cd06640    6 FTKLERIGKGSFGEVFKGI-DNRTQQVVAIKiidlEEAEDEIEDIQQ----EITVLSQCDSPYVTKYYGSYLKGTKLWII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 288 YGFLPNGSLEDQLHlqtqaCSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLArfsrf 367
Cdd:cd06640   81 MEYLGGGSALDLLR-----AGPFDEFQIATMLKEILKGLDYLH--SEKKIHRDIKAANVLLSEQGDVKLADFGVA----- 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 189011594 368 aganPSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd06640  149 ----GQLTDTQIKRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGE 198
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
218-420 1.11e-09

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 59.98  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRN-------TTYAVKRLKEEADlewTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGF 290
Cdd:cd05045    8 LGEGEFGKVVKATAFRlkgragyTTVAVKMLKENAS---SSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLIVEY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDQLHLQTQ-ACS-------------------PLSWPQRLDILLGTARAIQFLHQdsPSLIHGDIKSSNVLLDE 350
Cdd:cd05045   85 AKYGSLRSFLRESRKvGPSylgsdgnrnssyldnpderALTMGDLISFAWQISRGMQYLAE--MKLVHRDLAARNVLVAE 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189011594 351 RLMPKLGDFGLARfsrfagaNPSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILE--TLAG 420
Cdd:cd05045  163 GRKMKISDFGLSR-------DVYEEDSYVKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEivTLGG 227
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
218-397 1.12e-09

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: 59.92  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAV-MRNTTYAVKRLK-EEADLEwtvVKQSFLTEVEQLSRFRH-PNIVDFAGY--CAESGFyclVYGFLP 292
Cdd:cd14131    9 LGKGGSSKVYKVLnPKKKIYALKRVDlEGADEQ---TLQSYKNEIELLKKLKGsDRIIQLYDYevTDEDDY---LYMVME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLEDQLHLQTQACSPLS-------WPQRLDillgtarAIQFLHQDSpsLIHGDIKSSNVLL-DERLmpKLGDFGLARf 364
Cdd:cd14131   83 CGEIDLATILKKKRPKPIDpnfiryyWKQMLE-------AVHTIHEEG--IVHSDLKPANFLLvKGRL--KLIDFGIAK- 150
                        170       180       190
                 ....*....|....*....|....*....|...
gi 189011594 365 srfagANPSQSSTVARTCTVrGTLAYLPEEYIK 397
Cdd:cd14131  151 -----AIQNDTTSIVRDSQV-GTLNYMSPEAIK 177
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
218-424 1.12e-09

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: 59.98  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCV-YRAVMRNTTYAVKRL-----KEEADLEWTVVKQ------------SFLTEVEQLSRFRHPNIVDFAGYCA 279
Cdd:cd14067    1 LGQGGSGTViYRARYQGQPVAVKRFhikkcKKRTDGSADTMLKhlraadamknfsEFRQEASMLHSLQHPCIVYLIGISI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 280 ESgfYCLVYGFLPNGSLEDQLHLQTQACS--PLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVL---LDER--L 352
Cdd:cd14067   81 HP--LCFALELAPLGSLNTVLEENHKGSSfmPLGHMLTFKIAYQIAAGLAYLHKKN--IIFCDLKSDNILvwsLDVQehI 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594 353 MPKLGDFGLARFSRFAGAnpsqsstvartCTVRGTLAYLPEEYikTGRLAVD--TDTFSFGVVILETLAGQRAV 424
Cdd:cd14067  157 NIKLSDYGISRQSFHEGA-----------LGVEGTPGYQAPEI--RPRIVYDekVDMFSYGMVLYELLSGQRPS 217
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
218-416 1.19e-09

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 59.51  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT-TYAVKRLKEEADLEwtvvkQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSL 296
Cdd:cd05113   12 LGTGQFGVVKYGKWRGQyDVAIKMIKEGSMSE-----DEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 297 -----EDQLHLQTQacsplswpQRLDILLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSrfagAN 371
Cdd:cd05113   87 lnylrEMRKRFQTQ--------QLLEMCKDVCEAMEYL--ESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYV----LD 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 189011594 372 PSQSSTVARTCTVRgtlaYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd05113  153 DEYTSSVGSKFPVR----WSPPEVLMYSKFSSKSDVWAFGVLMWE 193
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
217-364 1.40e-09

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: 59.69  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNT--TYAVKRLKE-EADLewtVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPN 293
Cdd:cd07847    8 KIGEGSYGVVFKCRNRETgqIVAIKKFVEsEDDP---VIKKIALREIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEYCDH 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189011594 294 gSLEDQLHLQTQACSPLSWPQrldILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARF 364
Cdd:cd07847   85 -TVLNELEKNPRGVPEHLIKK---IIWQTLQAVNFCHKHN--CIHRDVKPENILITKQGQIKLCDFGFARI 149
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
217-421 1.44e-09

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: 59.22  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTTYAVKRLK--EEADLEWTVVkQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNG 294
Cdd:cd14121    2 KLGSGTYATVYKAYRKSGAREVVAVKcvSKSSLNKAST-ENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEDQLH----LQTQACspLSWPQRLdillgtARAIQFLHQDSPSliHGDIKSSNVLLDERLMP--KLGDFGLARFSRfa 368
Cdd:cd14121   81 DLSRFIRsrrtLPESTV--RRFLQQL------ASALQFLREHNIS--HMDLKPQNLLLSSRYNPvlKLADFGFAQHLK-- 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 189011594 369 ganPSQSSTvartcTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd14121  149 ---PNDEAH-----SLRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGR 193
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
218-420 1.50e-09

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: 59.54  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT--YAVKRLKEEADLEWTV-----VKQSFLTEVEQLSRFR-HPNIVDFAGYCAESGFYCLVYG 289
Cdd:cd14182   11 LGRGVSSVVRRCIHKPTRqeYAVKIIDITGGGSFSPeevqeLREATLKEIDILRKVSgHPNIIQLKDTYETNTFFFLVFD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLEDQLHLQTQacspLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLArfsrfag 369
Cdd:cd14182   91 LMKKGELFDYLTEKVT----LSEKETRKIMRALLEVICALH--KLNIVHRDLKPENILLDDDMNIKLTDFGFS------- 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 370 anpSQSSTVARTCTVRGTLAYLPEEYIKTGR------LAVDTDTFSFGVVILETLAG 420
Cdd:cd14182  158 ---CQLDPGEKLREVCGTPGYLAPEIIECSMddnhpgYGKEVDMWSTGVIMYTLLAG 211
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
218-400 1.56e-09

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: 59.30  E-value: 1.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMR--NTTYAVK-----RLKEEADLEWTVVKQSFLT--------------EVEQLSRFRHPNIVDFAG 276
Cdd:cd14118    2 IGKGSYGIVKLAYNEedNTLYAMKilskkKLLKQAGFFRRPPPRRKPGalgkpldpldrvyrEIAILKKLDHPNVVKLVE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 277 YC---AESGFYcLVYGFLPNGSLedqlhLQTQACSPLS----WPQRLDILLGtaraIQFLHQDSpsLIHGDIKSSNVLLD 349
Cdd:cd14118   82 VLddpNEDNLY-MVFELVDKGAV-----MEVPTDNPLSeetaRSYFRDIVLG----IEYLHYQK--IIHRDIKPSNLLLG 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 189011594 350 ERLMPKLGDFGLArfSRFAGANPSQSSTVartctvrGTLAYLPEEYIKTGR 400
Cdd:cd14118  150 DDGHVKIADFGVS--NEFEGDDALLSSTA-------GTPAFMAPEALSESR 191
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
218-421 1.91e-09

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: 59.54  E-value: 1.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEA-----DLEWTVVKQSFLteveQLSRfRHPNIVD-FAGYCAESGFYcLVYG 289
Cdd:cd05570    3 LGKGSFGKVMLAERKKTdeLYAIKVLKKEViieddDVECTMTEKRVL----ALAN-RHPFLTGlHACFQTEDRLY-FVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLedQLHLQTQacsplswpQRLD----------ILLgtarAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDF 359
Cdd:cd05570   77 YVNGGDL--MFHIQRA--------RRFTeerarfyaaeICL----ALQFLHERG--IIYRDLKLDNVLLDAEGHIKIADF 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 360 GLARFSRFAGAnpsqsstvaRTCTVRGTLAYL-PE--EYIKTGRlAVDTdtFSFGVVILETLAGQ 421
Cdd:cd05570  141 GMCKEGIWGGN---------TTSTFCGTPDYIaPEilREQDYGF-SVDW--WALGVLLYEMLAGQ 193
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
218-425 2.11e-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: 58.82  E-value: 2.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEWTVVKqsfltEVEQLSRFRHPNIVD-FAGYCAESGfYCLVYGFLPNG 294
Cdd:cd14006    1 LGRGRFGVVKRCIEKATgrEFAAKFIPKRDKKKEAVLR-----EISILNQLQHPRIIQlHEAYESPTE-LVLILELCSGG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEDQL---HLQTQACSPLSWPQRLDillgtarAIQFLHQDSpsLIHGDIKSSNVLLDERLMP--KLGDFGLARfsrfag 369
Cdd:cd14006   75 ELLDRLaerGSLSEEEVRTYMRQLLE-------GLQYLHNHH--ILHLDLKPENILLADRPSPqiKIIDFGLAR------ 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189011594 370 anpsQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVV--IL-------------ETLAGQRAVR 425
Cdd:cd14006  140 ----KLNPGEELKEIFGTPEFVAPEIVNGEPVSLATDMWSIGVLtyVLlsglspflgeddqETLANISACR 206
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
218-419 2.44e-09

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 59.04  E-value: 2.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRA-------VMRNTTYAVKRLKEEA-DLEwtvvKQSFLTEVEQLSRF-RHPNIVDFAGYCAESGF----- 283
Cdd:cd05054   15 LGRGAFGKVIQAsafgidkSATCRTVAVKMLKEGAtASE----HKALMTELKILIHIgHHLNVVNLLGACTKPGGplmvi 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 284 --YC-----------LVYGFLPNGSLEDQLHLQTQAC-----SPLSWPQRLDILLGTARAIQFLhqDSPSLIHGDIKSSN 345
Cdd:cd05054   91 veFCkfgnlsnylrsKREEFVPYRDKGARDVEEEEDDdelykEPLTLEDLICYSFQVARGMEFL--ASRKCIHRDLAARN 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594 346 VLLDERLMPKLGDFGLARfsrfagaNPSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLA 419
Cdd:cd05054  169 ILLSENNVVKICDFGLAR-------DIYKDPDYVRKGDARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFS 235
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
218-421 2.95e-09

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 58.51  E-value: 2.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRN-------TTYAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGF 290
Cdd:cd05032   14 LGQGSFGMVYEGLAKGvvkgepeTRVAIKTVNENASMR---ERIEFLNEASVMKEFNCHHVVRLLGVVSTGQPTLVVMEL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDQLHLQ---TQACSPLSWPQRLDIL---LGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLAR- 363
Cdd:cd05032   91 MAKGDLKSYLRSRrpeAENNPGLGPPTLQKFIqmaAEIADGMAYLA--AKKFVHRDLAARNCMVAEDLTVKIGDFGMTRd 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 364 -----FSRFAGanpsqsstvARTCTVRgtlaYLPEEYIKTGRLAVDTDTFSFGVVILE--TLAGQ 421
Cdd:cd05032  169 iyetdYYRKGG---------KGLLPVR----WMAPESLKDGVFTTKSDVWSFGVVLWEmaTLAEQ 220
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
214-422 3.27e-09

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 58.42  E-value: 3.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 214 EELRIGEGGFGCV----YRAVMRNTTYAVKRLKEEADlewTVVKQSFLTEVEQLSRFRHPNIVDFAGYCaESGFYCLVYG 289
Cdd:cd05115    8 DEVELGSGNFGCVkkgvYKMRKKQIDVAIKVLKQGNE---KAVRDEMMREAQIMHQLDNPYIVRMIGVC-EAEALMLVME 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLEDQLHLQTQAcsplswpqrldilLGTARAIQFLHQDS--------PSLIHGDIKSSNVLLDERLMPKLGDFGL 361
Cdd:cd05115   84 MASGGPLNKFLSGKKDE-------------ITVSNVVELMHQVSmgmkyleeKNFVHRDLAARNVLLVNQHYAKISDFGL 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189011594 362 arfSRFAGANPSQSStvARTCTvRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLA-GQR 422
Cdd:cd05115  151 ---SKALGADDSYYK--ARSAG-KWPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSyGQK 206
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
218-523 3.47e-09

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 58.39  E-value: 3.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMR--NTTY---AVKRLKeeADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAES------GFYCL 286
Cdd:cd05074   17 LGKGEFGSVREAQLKseDGSFqkvAVKMLK--ADIFSSSDIEEFLREAACMKEFDHPNVIKLIGVSLRSrakgrlPIPMV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 287 VYGFLPNGSLEDQLHLQTQACSPLSWPQR--LDILLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARf 364
Cdd:cd05074   95 ILPFMKHGDLHTFLLMSRIGEEPFTLPLQtlVRFMIDIASGMEYL--SSKNFIHRDLAARNCMLNENMTVCVADFGLSK- 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 365 SRFAGANPSQsstvartctvrGTLAYLPEEYIKTGRLA-----VDTDTFSFGVVILEtlagqraVRTQGAktkylkdlie 439
Cdd:cd05074  172 KIYSGDYYRQ-----------GCASKLPVKWLALESLAdnvytTHSDVWAFGVTMWE-------IMTRGQ---------- 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 440 deaeevgvtlkstqpTLWMGVATdawtapiaAQIYKKHLDSRPGPCPPQLGLALAQLACCCMHRRAKKRPPMTQVYKRLE 519
Cdd:cd05074  224 ---------------TPYAGVEN--------SEIYNYLIKGNRLKQPPDCLEDVYELMCQCWSPEPKCRPSFQHLRDQLE 280

                 ....
gi 189011594 520 GLQA 523
Cdd:cd05074  281 LIWG 284
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
218-418 3.73e-09

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


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 58.11  E-value: 3.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEWTVVKQSFL-TEVEQLSRFRHPNIVDFAGyC---AESGFYCLVYGFL 291
Cdd:cd06653   10 LGRGAFGEVYLCYDADTgrELAVKQVPFDPDSQETSKEVNALeCEIQLLKNLRHDRIVQYYG-ClrdPEEKKLSIFVEYM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 PNGSLEDQLHLQTQACSPLSWPQRLDILLGtaraIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfagan 371
Cdd:cd06653   89 PGGSVKDQLKAYGALTENVTRRYTRQILQG----VSYLH--SNMIVHRDIKGANILRDSAGNVKLGDFGASK-------- 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 189011594 372 psQSSTVARTCT----VRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETL 418
Cdd:cd06653  155 --RIQTICMSGTgiksVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEML 203
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
215-416 3.96e-09

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 58.16  E-value: 3.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 215 ELRIGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAES--GFYC--LVYGF 290
Cdd:cd14032    6 DIELGRGSFKTVYKGLDTETWVEVAWCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWESCakGKRCivLVTEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDQLHlQTQACSP---LSWPQRLdillgtARAIQFLHQDSPSLIHGDIKSSNVLLDERLMP-KLGDFGLARFSR 366
Cdd:cd14032   86 MTSGTLKTYLK-RFKVMKPkvlRSWCRQI------LKGLLFLHTRTPPIIHRDLKCDNIFITGPTGSvKIGDLGLATLKR 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 189011594 367 FAGANpsqsstvartcTVRGTLAYL-PEEYIKTGRLAVdtDTFSFGVVILE 416
Cdd:cd14032  159 ASFAK-----------SVIGTPEFMaPEMYEEHYDESV--DVYAFGMCMLE 196
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
217-422 4.10e-09

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: 58.20  E-value: 4.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYC---AESGFYCLVYgFL 291
Cdd:cd06621    8 SLGEGAGGSVTKCRLRNTktIFALKTITTDPNPD---VQKQILRELEINKSCASPYIVKYYGAFldeQDSSIGIAME-YC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 PNGSLE---DQLHLQTQACS--PLswpqrLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLA--RF 364
Cdd:cd06621   84 EGGSLDsiyKKVKKKGGRIGekVL-----GKIAESVLKGLSYLHSRK--IIHRDIKPSNILLTRKGQVKLCDFGVSgeLV 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594 365 SRFAGanpsqsstvartcTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILEtLAGQR 422
Cdd:cd06621  157 NSLAG-------------TFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLE-VAQNR 200
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
218-362 5.51e-09

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 58.22  E-value: 5.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWtvvkqSFLTEVEQLSRFRHPNIVDFAGYCAESGFYC----LVYGFLPN 293
Cdd:cd14142   13 IGKGRYGEVWRGQWQGESVAVKIFSSRDEKSW-----FRETEIYNTVLLRHENILGFIASDMTSRNSCtqlwLITHYHEN 87
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 294 GSLEDqlHLQTQacsPLSWPQRLDILLGTARAIQFLH------QDSPSLIHGDIKSSNVLLDERLMPKLGDFGLA 362
Cdd:cd14142   88 GSLYD--YLQRT---TLDHQEMLRLALSAASGLVHLHteifgtQGKPAIAHRDLKSKNILVKSNGQCCIADLGLA 157
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
218-362 5.82e-09

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 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: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 57.69  E-value: 5.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVY----RAVMRNTTYAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPN 293
Cdd:cd05087    5 IGHGWFGKVFlgevNSGLSSTQVVVKELKASASVQ---DQMQFLEEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEFCPL 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189011594 294 GSLEDQLH----LQTQACSPLSWPQrldilLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLMPKLGDFGLA 362
Cdd:cd05087   82 GDLKGYLRscraAESMAPDPLTLQR-----MACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLS 149
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
218-420 6.38e-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: 57.72  E-value: 6.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFG----CVYRAVmrNTTYAVKRLKEEadlewtvvKQSFLTEVEQLSRF-RHPNIVDFAGYCAESGFYCLVYGFLP 292
Cdd:cd14178   11 IGIGSYSvckrCVHKAT--STEYAVKIIDKS--------KRDPSEEIEILLRYgQHPNIITLKDVYDDGKFVYLVMELMR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLEDQlhLQTQACspLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVL-LDERLMP---KLGDFGLARFSRfa 368
Cdd:cd14178   81 GGELLDR--ILRQKC--FSEREASAVLCTITKTVEYLH--SQGVVHRDLKPSNILyMDESGNPesiRICDFGFAKQLR-- 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 189011594 369 ganpSQSSTVARTCTVRGTLAylPEEYIKTGRLAVdTDTFSFGVVILETLAG 420
Cdd:cd14178  153 ----AENGLLMTPCYTANFVA--PEVLKRQGYDAA-CDIWSLGILLYTMLAG 197
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
218-416 6.73e-09

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: 57.74  E-value: 6.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAV-MRNTT--YAVKRLK---EEADLEWTVVKQsfLTEVEQLSRFRHPNIVDFAGYCAESGF-----YCL 286
Cdd:cd07862    9 IGEGAYGKVFKARdLKNGGrfVALKRVRvqtGEEGMPLSTIRE--VAVLRHLETFEHPNVVRLFDVCTVSRTdretkLTL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 287 VYGFLPngslEDQLHLQTQACSPLSWPQRL-DILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFS 365
Cdd:cd07862   87 VFEHVD----QDLTTYLDKVPEPGVPTETIkDMMFQLLRGLDFLH--SHRVVHRDLKPQNILVTSSGQIKLADFGLARIY 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 189011594 366 RFAGAnpsqsstvarTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd07862  161 SFQMA----------LTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAE 201
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
216-421 7.22e-09

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: 57.69  E-value: 7.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 216 LRIGEGGFG--CVYRAVMRNTTYAVKRLkeeaDLEWTVVKQSFLTEVEQLSRFRHPNIVD-FAGYCAESGFYCLVYgFLP 292
Cdd:cd06659   27 VKIGEGSTGvvCIAREKHSGRQVAVKMM----DLRKQQRRELLFNEVVIMRDYQHPNVVEmYKSYLVGEELWVLME-YLQ 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLEDQLHlQTQacspLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGL-ARFSRFAgan 371
Cdd:cd06659  102 GGALTDIVS-QTR----LNEEQIATVCEAVLQALAYLH--SQGVIHRDIKSDSILLTLDGRVKLSDFGFcAQISKDV--- 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 189011594 372 PSQSSTVartctvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd06659  172 PKRKSLV-------GTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGE 214
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
217-363 7.30e-09

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 57.52  E-value: 7.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMR--NTTYAVKRLKEEADLEWtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFlpng 294
Cdd:PLN00009   9 KIGEGTYGVVYKARDRvtNETIALKKIRLEQEDEG--VPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVFEY---- 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189011594 295 sLEDQLHLQTQACSPLSWPQRL--DILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMP-KLGDFGLAR 363
Cdd:PLN00009  83 -LDLDLKKHMDSSPDFAKNPRLikTYLYQILRGIAYCH--SHRVLHRDLKPQNLLIDRRTNAlKLADFGLAR 151
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
218-416 7.99e-09

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: 57.18  E-value: 7.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT-TYAVKRLKEEADLEwtvvkQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSL 296
Cdd:cd05114   12 LGSGLFGVVRLGKWRAQyKVAIKAIREGAMSE-----EDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENGCL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 297 EDQLHLQTQACSPlswpqrlDILLGTAR----AIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFsrfaganp 372
Cdd:cd05114   87 LNYLRQRRGKLSR-------DMLLSMCQdvceGMEYLERNN--FIHRDLAARNCLVNDTGVVKVSDFGMTRY-------- 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 189011594 373 SQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd05114  150 VLDDQYTSSSGAKFPVKWSPPEVFNYSKFSSKSDVWSFGVLMWE 193
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
212-352 8.36e-09

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 57.24  E-value: 8.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELRIGEGGFGCVYRAVMR--NTTYAVKRLKEEadLEWTVVKQSFLTEVEQLSRF-RHPNIVDFAGYCAESGFYCLVY 288
Cdd:cd14139    2 FLELEKIGVGEFGSVYKCIKRldGCVYAIKRSMRP--FAGSSNEQLALHEVYAHAVLgHHPHVVRYYSAWAEDDHMIIQN 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594 289 GFLPNGSLEDQLHLQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERL 352
Cdd:cd14139   80 EYCNGGSLQDAISENTKSGNHFEEPELKDILLQVSMGLKYIH--NSGLVHLDIKPSNIFICHKM 141
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
218-420 9.15e-09

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 57.33  E-value: 9.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVM---------RNTTYAVKRLKEEA---DLewtvvkQSFLTEVEQLSRF-RHPNIVDFAGYCAESGFY 284
Cdd:cd05098   21 LGEGCFGQVVLAEAigldkdkpnRVTKVAVKMLKSDAtekDL------SDLISEMEMMKMIgKHKNIINLLGACTQDGPL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 285 CLVYGFLPNGSLEDQLHLQ---------TQACSP---LSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERL 352
Cdd:cd05098   95 YVIVEYASKGNLREYLQARrppgmeycyNPSHNPeeqLSSKDLVSCAYQVARGMEYLA--SKKCIHRDLAARNVLVTEDN 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 353 MPKLGDFGLARfsrfagaNPSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILE--TLAG 420
Cdd:cd05098  173 VMKIADFGLAR-------DIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEifTLGG 235
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
215-422 9.33e-09

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The EphA10 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 56.86  E-value: 9.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 215 ELRIGEGGFGCVYRAVM-----RNTTYAVKRLKEEADLEWtvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYG 289
Cdd:cd05064   10 ERILGTGRFGELCRGCLklpskRELPVAIHTLRAGCSDKQ---RRGFLAEALTLGQFDHSNIVRLEGVITRGNTMMIVTE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLEDQLHLQTqacSPLSWPQRLDILLGTARAIQFLHQdsPSLIHGDIKSSNVLLDERLMPKLGDFGlaRFSRfag 369
Cdd:cd05064   87 YMSNGALDSFLRKHE---GQLVAGQLMGMLPGLASGMKYLSE--MGYVHKGLAAHKVLVNSDLVCKISGFR--RLQE--- 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 189011594 370 anpSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLA-GQR 422
Cdd:cd05064  157 ---DKSEAIYTTMSGKSPVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSyGER 207
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
211-416 9.57e-09

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 57.09  E-value: 9.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 211 NFSEELRIGEGGFGCVYRAVMRN-------TTYAVKRLKEEADlewTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGF 283
Cdd:cd05046    6 NLQEITTLGRGEFGEVFLAKAKGieeeggeTLVLVKALQKTKD---ENLQSEFRRELDMFRKLSHKNVVRLLGLCREAEP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 284 YCLVYGFLPNGSLEDQLHL-----QTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGD 358
Cdd:cd05046   83 HYMILEYTDLGDLKQFLRAtkskdEKLKPPPLSTKQKVALCTQIALGMDHLS--NARFVHRDLAARNCLVSSQREVKVSL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189011594 359 FGLAR--FSRfaganpsqsstvaRTCTVRGTLA---YLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd05046  161 LSLSKdvYNS-------------EYYKLRNALIplrWLAPEAVQEDDFSTKSDVWSFGVLMWE 210
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
218-416 9.69e-09

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 57.33  E-value: 9.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGC---VYRAVMRNT-------TYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAES--GFYc 285
Cdd:cd14011    1 VASAGPGLpwkIYNGSKKSTkqevsvfVFEKKQLEEYSKRDREQILELLKRGVKQLTRLRHPRILTVQHPLEESreSLA- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 286 LVYGFLpNGSLEDQLHLQTQACSP---LSWPQRLDI-----LLGTARAIQFLHQDSpSLIHGDIKSSNVLLDERLMPKLG 357
Cdd:cd14011   80 FATEPV-FASLANVLGERDNMPSPppeLQDYKLYDVeikygLLQISEALSFLHNDV-KLVHGNICPESVVINSNGEWKLA 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 358 DFGlarfsrFAGANPSQSSTVARTCTVRGTLA--------YLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd14011  158 GFD------FCISSEQATDQFPYFREYDPNLPplaqpnlnYLAPEYILSKTCDPASDMFSLGVLIYA 218
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
215-416 9.80e-09

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 57.04  E-value: 9.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 215 ELRIGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAE--SGFYC--LVYGF 290
Cdd:cd14031   15 DIELGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESvlKGKKCivLVTEL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDQLHlQTQACSP---LSWPQRLdillgtARAIQFLHQDSPSLIHGDIKSSNVLLDERLMP-KLGDFGLARFSR 366
Cdd:cd14031   95 MTSGTLKTYLK-RFKVMKPkvlRSWCRQI------LKGLQFLHTRTPPIIHRDLKCDNIFITGPTGSvKIGDLGLATLMR 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 189011594 367 FAGANpsqsstvartcTVRGTLAYL-PEEYIKTGRLAVdtDTFSFGVVILE 416
Cdd:cd14031  168 TSFAK-----------SVIGTPEFMaPEMYEEHYDESV--DVYAFGMCMLE 205
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
207-421 1.01e-08

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: 57.36  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 207 QGTCNFseeLRIGEGGFGCVYRAVMRNT--TYAVKRLkeeaDLEWTVVKQSFLTEVEQLSRFRHPNIVD-FAGYCAESGF 283
Cdd:cd06658   22 EYLDSF---IKIGEGSTGIVCIATEKHTgkQVAVKKM----DLRKQQRRELLFNEVVIMRDYHHENVVDmYNSYLVGDEL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 284 YcLVYGFLPNGSLEDQLhlqtqACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLAr 363
Cdd:cd06658   95 W-VVMEFLEGGALTDIV-----THTRMNEEQIATVCLSVLRALSYLH--NQGVIHRDIKSDSILLTSDGRIKLSDFGFC- 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594 364 fSRFAGANPSQSSTVartctvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd06658  166 -AQVSKEVPKRKSLV-------GTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGE 215
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
212-444 1.02e-08

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: 56.96  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELRIGEGGFGCVYRAVMRNT--TYAVKRLkEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYG 289
Cdd:cd05630    2 FRQYRVLGKGGFGEVCACQVRATgkMYACKKL-EKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLEDQLHLQTQAcsplSWPQRLDILLGT--ARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFSrf 367
Cdd:cd05630   81 LMNGGDLKFHIYHMGQA----GFPEARAVFYAAeiCCGLEDLHRER--IVYRDLKPENILLDDHGHIRISDLGLAVHV-- 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 368 aganPSQSSTVARTctvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAKTKY--LKDLIEDEAEE 444
Cdd:cd05630  153 ----PEGQTIKGRV----GTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKReeVERLVKEVPEE 223
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
218-420 1.05e-08

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: 57.03  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT--YAVKRLKEEadlewTVVK----QSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFL 291
Cdd:cd14209    9 LGTGSFGRVMLVRHKETGnyYAMKILDKQ-----KVVKlkqvEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVMEYV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 PNGSLEDQLHLQTQACSPLSWPQRLDILLgtarAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsRFAGan 371
Cdd:cd14209   84 PGGEMFSHLRRIGRFSEPHARFYAAQIVL----AFEYLH--SLDLIYRDLKPENLLIDQQGYIKVTDFGFAK--RVKG-- 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 189011594 372 psqsstvaRTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd14209  154 --------RTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAG 194
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
218-362 1.08e-08

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 subfamily 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).


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 56.88  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRA-VMRNTTYA---VKRLKEEAD-LEwtvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLP 292
Cdd:cd14206    5 IGNGWFGKVILGeIFSDYTPAqvvVKELRVSAGpLE----QRKFISEAQPYRSLQHPNILQCLGLCTETIPFLLIMEFCQ 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594 293 NGSLEDQLHLQTQA--CSPLSWPQRLDIL--LGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLMPKLGDFGLA 362
Cdd:cd14206   81 LGDLKRYLRAQRKAdgMTPDLPTRDLRTLqrMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLS 154
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
211-420 1.19e-08

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: 57.06  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 211 NFSEELRIGEGGFGCVY--RAVMRNTTYAVKRLK--EEADLEWTvvkQSFLTEVEQLSRFRHPNIVDFagYCAE--SGFY 284
Cdd:cd05612    2 DFERIKTIGTGTFGRVHlvRDRISEHYYALKVMAipEVIRLKQE---QHVHNEKRVLKEVSHPFIIRL--FWTEhdQRFL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 285 CLVYGFLPNGSLEDQLHLQTQACSPLSWPQRLDILLgtarAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARf 364
Cdd:cd05612   77 YMLMEYVPGGELFSYLRNSGRFSNSTGLFYASEIVC----ALEYLH--SKEIVYRDLKPENILLDKEGHIKLTDFGFAK- 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 189011594 365 srfaganpsqsSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd05612  150 -----------KLRDRTWTLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVG 194
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
218-420 1.34e-08

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


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 56.48  E-value: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMR--NTTYAVKRLKEEADLEWTVV--KQSFLTEV---EQLSRFRHPNIVDFAGYCAES-GF------ 283
Cdd:cd14005    8 LGKGGFGTVYSGVRIrdGLPVAVKFVPKSRVTEWAMIngPVPVPLEIallLKASKPGVPGVIRLLDWYERPdGFllimer 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 284 ---------YCLVYGFLPngslEDQL-HLQTQAcsplswpqrldillgtARAIQFLHQDSpsLIHGDIKSSNVLLD-ERL 352
Cdd:cd14005   88 pepcqdlfdFITERGALS----ENLArIIFRQV----------------VEAVRHCHQRG--VLHRDIKDENLLINlRTG 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189011594 353 MPKLGDFGLARFSRfaganpsqsstvaRTC--TVRGTLAYLPEEYIKTGRLAVDTDT-FSFGVVILETLAG 420
Cdd:cd14005  146 EVKLIDFGCGALLK-------------DSVytDFDGTRVYSPPEWIRHGRYHGRPATvWSLGILLYDMLCG 203
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
218-421 1.35e-08

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: 57.12  E-value: 1.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEA-----DLEWTVVKQSFLTeveqLSRfRHPNIVdfAGYCA----ESGFYCL 286
Cdd:cd05591    3 LGKGSFGKVMLAERKGTdeVYAIKVLKKDVilqddDVDCTMTEKRILA----LAA-KHPFLT--ALHSCfqtkDRLFFVM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 287 VYgflPNGSledQLHLQTQACSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFSR 366
Cdd:cd05591   76 EY---VNGG---DLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHG--VIYRDLKLDNILLDAEGHCKLADFGMCKEGI 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 367 FAGanpsqsstvARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd05591  148 LNG---------KTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQ 193
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
208-421 1.35e-08

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: 1.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 208 GTCNFSEELRIGEGGFGCVYRAVMRNTT---YAVKRLKEEadlewTVVKQSFL--TEVEQLSRFRHPNIVDFAGYCAESG 282
Cdd:cd14201    4 GDFEYSRKDLVGHGAFAVVFKGRHRKKTdweVAIKSINKK-----NLSKSQILlgKEIKILKELQHENIVALYDVQEMPN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 283 FYCLVYGFLPNGSLEDQLhlqtQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLD---------ERLM 353
Cdd:cd14201   79 SVFLVMEYCNGGDLADYL----QAKGTLSEDTIRVFLQQIAAAMRILH--SKGIIHRDLKPQNILLSyasrkkssvSGIR 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594 354 PKLGDFGLARFsrfaganpSQSSTVArtCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd14201  153 IKIADFGFARY--------LQSNMMA--ATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGK 210
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
218-418 1.56e-08

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 56.39  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMR--NTTY---AVKRLKeeADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFY------CL 286
Cdd:cd05035    7 LGEGEFGSVMEAQLKqdDGSQlkvAVKTMK--VDIHTYSEIEEFLSEAACMKDFDHPNVMRLIGVCFTASDLnkppspMV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 287 VYGFLPNGSLEDQLHLQTQACSPLSWPQR--LDILLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARf 364
Cdd:cd05035   85 ILPFMKHGDLHSYLLYSRLGGLPEKLPLQtlLKFMVDIAKGMEYL--SNRNFIHRDLAARNCMLDENMTVCVADFGLSR- 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 365 SRFAGANPSQsstvartctvrGTLAYLPEEYIKTGRLA-----VDTDTFSFGVVILETL 418
Cdd:cd05035  162 KIYSGDYYRQ-----------GRISKMPVKWIALESLAdnvytSKSDVWSFGVTMWEIA 209
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
218-421 1.82e-08

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: 56.64  E-value: 1.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT-----TYAVKRLKEEadlewTVV---KQSFLTEVEQ--LSRFRHPNIVDFAGYCAESGFYCLV 287
Cdd:cd05584    4 LGKGGYGKVFQVRKTTGsdkgkIFAMKVLKKA-----SIVrnqKDTAHTKAERniLEAVKHPFIVDLHYAFQTGGKLYLI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 288 YGFLPNGSLEDQLH-----LQTQACSPLSwpqrlDILLgtarAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLA 362
Cdd:cd05584   79 LEYLSGGELFMHLEregifMEDTACFYLA-----EITL----ALGHLHSLG--IIYRDLKPENILLDAQGHVKLTDFGLC 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 363 RFSRFAGanpsqsstvARTCTVRGTLAYL-PEEYIKTGRlAVDTDTFSFGVVILETLAGQ 421
Cdd:cd05584  148 KESIHDG---------TVTHTFCGTIEYMaPEILTRSGH-GKAVDWWSLGALMYDMLTGA 197
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
218-416 1.83e-08

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 56.33  E-value: 1.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVkqsflTEVEQLSRFRHPNIVDF-AGYCAESGFYC---LVYGFLPN 293
Cdd:cd14144    3 VGKGRYGEVWKGKWRGEKVAVKIFFTTEEASWFRE-----TEIYQTVLMRHENILGFiAADIKGTGSWTqlyLITDYHEN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 294 GSLEDQLhlqtqACSPLSWPQRLDILLGTARAIQFLH------QDSPSLIHGDIKSSNVLLDERLMPKLGDFGLArfSRF 367
Cdd:cd14144   78 GSLYDFL-----RGNTLDTQSMLKLAYSAACGLAHLHteifgtQGKPAIAHRDIKSKNILVKKNGTCCIADLGLA--VKF 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 189011594 368 AganpSQSSTVARTCTVR-GTLAYLPEEYI--KTGRLAVD----TDTFSFGVVILE 416
Cdd:cd14144  151 I----SETNEVDLPPNTRvGTKRYMAPEVLdeSLNRNHFDaykmADMYSFGLVLWE 202
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
215-416 2.15e-08

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 56.21  E-value: 2.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 215 ELRIGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDF--AGYCAESGFYC--LVYGF 290
Cdd:cd14030   30 DIEIGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFydSWESTVKGKKCivLVTEL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDQL-HLQTQACSPL-SWPQRLdillgtARAIQFLHQDSPSLIHGDIKSSNVLLDERLMP-KLGDFGLARFSRF 367
Cdd:cd14030  110 MTSGTLKTYLkRFKVMKIKVLrSWCRQI------LKGLQFLHTRTPPIIHRDLKCDNIFITGPTGSvKIGDLGLATLKRA 183
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 189011594 368 AGANpsqsstvartcTVRGTLAYL-PEEYIKTGRLAVdtDTFSFGVVILE 416
Cdd:cd14030  184 SFAK-----------SVIGTPEFMaPEMYEEKYDESV--DVYAFGMCMLE 220
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
218-363 2.18e-08

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 56.54  E-value: 2.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAV--MRNTTYAVKRLKEeadLEWTVVKQSFLTEVEQLSRFRHPNIVDF------AGYCAESGFYcLVYG 289
Cdd:cd07849   13 IGEGAYGMVCSAVhkPTGQKVAIKKISP---FEHQTYCLRTLREIKILLRFKHENIIGIldiqrpPTFESFKDVY-IVQE 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189011594 290 FLpngslEDQLH--LQTQacsPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLAR 363
Cdd:cd07849   89 LM-----ETDLYklIKTQ---HLSNDHIQYFLYQILRGLKYIH--SANVLHRDLKPSNLLLNTNCDLKICDFGLAR 154
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
218-522 2.36e-08

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: 56.06  E-value: 2.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFG----CVYRAVMRNT--TYAVKRLKEEADLEwtvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGF--YCLVYG 289
Cdd:cd05081   12 LGKGNFGsvelCRYDPLGDNTgaLVAVKQLQHSGPDQ----QRDFQREIQILKALHSDFIVKYRGVSYGPGRrsLRLVME 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLEDQLHLQTQACSPlswpqRLDILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARF----- 364
Cdd:cd05081   88 YLPSGCLRDFLQRHRARLDA-----SRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLlpldk 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 365 SRFAGANPSQSStvartctvrgTLAYLPEEyIKTGRLAVDTDTFSFGVVILETLAgqRAVRTQGAKTKYLKdliedeaee 444
Cdd:cd05081  163 DYYVVREPGQSP----------IFWYAPES-LSDNIFSRQSDVWSFGVVLYELFT--YCDKSCSPSAEFLR--------- 220
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594 445 vgvtlkstqptlWMGVATDawtAPIAAQIYKKHLDSRPGPCPPQLGLALAQLACCCMHRRAKKRPPMTQVYKRLEGLQ 522
Cdd:cd05081  221 ------------MMGCERD---VPALCRLLELLEEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSALGPQLDMLW 283
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
218-364 2.81e-08

Catalytic domain of Cyclin-Dependent protein Kinase 8-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 CDK8, CDC2L6, and similar proteins. CDK8 functions 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-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. 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-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: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 56.14  E-value: 2.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT----YAVKRLKEEADlEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYC--LVYGFl 291
Cdd:cd07842    8 IGRGTYGRVYKAKRKNGKdgkeYAIKKFKGDKE-QYTGISQSACREIALLRELKHENVVSLVEVFLEHADKSvyLLFDY- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 pngsLEDQL------HLQTQACS-------PLSWpQRLDillgtarAIQFLHqdSPSLIHGDIKSSNVLL----DERLMP 354
Cdd:cd07842   86 ----AEHDLwqiikfHRQAKRVSippsmvkSLLW-QILN-------GIHYLH--SNWVLHRDLKPANILVmgegPERGVV 151
                        170
                 ....*....|
gi 189011594 355 KLGDFGLARF 364
Cdd:cd07842  152 KIGDLGLARL 161
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
211-363 2.95e-08

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: 55.78  E-value: 2.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 211 NFSEELRIGEGGFGCVYRAVMRNT--TYAVKRL--KEEADLewtvvkqsF----LTEVEQLSRFRHPNIV---DFA-GYC 278
Cdd:cd07866    9 DYEILGKLGEGTFGEVYKARQIKTgrVVALKKIlmHNEKDG--------FpitaLREIKILKKLKHPNVVpliDMAvERP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 279 AESGFYCL-VYGFLP------NGSLEDQ-LHLQTqacsplswPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDE 350
Cdd:cd07866   81 DKSKRKRGsVYMVTPymdhdlSGLLENPsVKLTE--------SQIKCYMLQLLEGINYLHENH--ILHRDIKAANILIDN 150
                        170
                 ....*....|...
gi 189011594 351 RLMPKLGDFGLAR 363
Cdd:cd07866  151 QGILKIADFGLAR 163
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
218-420 3.07e-08

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: 55.87  E-value: 3.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVY--RAVMR---NTTYAVKRLKEeADLEwtvVKQSFLTEVEQ--LSRFRHPNIVDFA-GYCAESGFYcLVYG 289
Cdd:cd05582    3 LGQGSFGKVFlvRKITGpdaGTLYAMKVLKK-ATLK---VRDRVRTKMERdiLADVNHPFIVKLHyAFQTEGKLY-LILD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLEDQLH---LQTQAcsplswpqrlDI---LLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLAR 363
Cdd:cd05582   78 FLRGGDLFTRLSkevMFTEE----------DVkfyLAELALALDHLH--SLGIIYRDLKPENILLDEDGHIKLTDFGLSK 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 364 FSRFaganpsqssTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd05582  146 ESID---------HEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTG 193
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
218-363 3.10e-08

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: 55.99  E-value: 3.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAV--MRNTTYAVKRLkeeADLEWTVV--KQSfLTEVEQLSRFRHPNIV---DFAGYCAESGF---YcLV 287
Cdd:cd07834    8 IGSGAYGVVCSAYdkRTGRKVAIKKI---SNVFDDLIdaKRI-LREIKILRHLKHENIIgllDILRPPSPEEFndvY-IV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 288 YGFLP---------NGSLEDQlHLQT---QACsplswpqrldillgtaRAIQFLHqdSPSLIHGDIKSSNVLLDERLMPK 355
Cdd:cd07834   83 TELMEtdlhkviksPQPLTDD-HIQYflyQIL----------------RGLKYLH--SAGVIHRDLKPSNILVNSNCDLK 143

                 ....*...
gi 189011594 356 LGDFGLAR 363
Cdd:cd07834  144 ICDFGLAR 151
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
218-439 3.35e-08

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: 55.34  E-value: 3.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT--YAVK-----RLKEEADLewtvvkqsFLTEVEQLSRFRHPNIVD-FAGYCAESGFYcLVYG 289
Cdd:cd14185    8 IGDGNFAVVKECRHWNENqeYAMKiidksKLKGKEDM--------IESEILIIKSLSHPNIVKlFEVYETEKEIY-LILE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLEDQLHLQTQACSPLSWPQRLDIllgtARAIQFLHqdSPSLIHGDIKSSNVLL----DERLMPKLGDFGLARFs 365
Cdd:cd14185   79 YVRGGDLFDAIIESVKFTEHDAALMIIDL----CEALVYIH--SKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKY- 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594 366 rfaganpsqssTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAKTKYLKDLIE 439
Cdd:cd14185  152 -----------VTGPIFTVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPERDQEELFQIIQ 214
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
217-362 3.44e-08

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 55.53  E-value: 3.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWtvvkqsFL-TEVEQLSRFRHPNIVDF-AGYCAESGFYC---LVYGFL 291
Cdd:cd14143    2 SIGKGRFGEVWRGRWRGEDVAVKIFSSREERSW------FReAEIYQTVMLRHENILGFiAADNKDNGTWTqlwLVSDYH 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 292 PNGSLEDqlHLQTqacSPLSWPQRLDILLGTARAIQFLH------QDSPSLIHGDIKSSNVLLDERLMPKLGDFGLA 362
Cdd:cd14143   76 EHGSLFD--YLNR---YTVTVEGMIKLALSIASGLAHLHmeivgtQGKPAIAHRDLKSKNILVKKNGTCCIADLGLA 147
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
218-421 3.53e-08

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: 56.14  E-value: 3.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEeadleWTVVKQS----FLTEVEQLSRFRHPNIVDFagYCA---ESGFYcLVY 288
Cdd:cd05573    9 IGRGAFGEVWLVRDKDTgqVYAMKILRK-----SDMLKREqiahVRAERDILADADSPWIVRL--HYAfqdEDHLY-LVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 289 GFLPNGSLedqlhlqtqacspLSWPQRLDILL-GTAR--------AIQFLHQdsPSLIHGDIKSSNVLLDERLMPKLGDF 359
Cdd:cd05573   81 EYMPGGDL-------------MNLLIKYDVFPeETARfyiaelvlALDSLHK--LGFIHRDIKPDNILLDADGHIKLADF 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 360 GLA---------------------RFSRFAGANPSQSSTVARTCTVrGTLAYL-PEEYIKTGrLAVDTDTFSFGVVILET 417
Cdd:cd05573  146 GLCtkmnksgdresylndsvntlfQDNVLARRRPHKQRRVRAYSAV-GTPDYIaPEVLRGTG-YGPECDWWSLGVILYEM 223

                 ....
gi 189011594 418 LAGQ 421
Cdd:cd05573  224 LYGF 227
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
218-420 3.83e-08

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 55.79  E-value: 3.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVM---------RNTTYAVKRLKEEA---DLewtvvkQSFLTEVEQLSRF-RHPNIVDFAGYCAESGFY 284
Cdd:cd05101   32 LGEGCFGQVVMAEAvgidkdkpkEAVTVAVKMLKDDAtekDL------SDLVSEMEMMKMIgKHKNIINLLGACTQDGPL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 285 CLVYGFLPNGSLEDQLH------------LQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERL 352
Cdd:cd05101  106 YVIVEYASKGNLREYLRarrppgmeysydINRVPEEQMTFKDLVSCTYQLARGMEYLA--SQKCIHRDLAARNVLVTENN 183
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 353 MPKLGDFGLARfsrfagaNPSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILE--TLAG 420
Cdd:cd05101  184 VMKIADFGLAR-------DINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEifTLGG 246
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
218-409 4.09e-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: 54.96  E-value: 4.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVyRAVMRNTT---YAVK-----RLKEEADLEWTVVKqsfltEVEQLSRFRHPNIVDFAG--YCAESGFYCLV 287
Cdd:cd14119    1 LGEGSYGKV-KEVLDTETlcrRAVKilkkrKLRRIPNGEANVKR-----EIQILRRLNHRNVIKLVDvlYNEEKQKLYMV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 288 YGFLpNGSLEDQLHLQTQACSPLSwpQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLL--DERLmpKLGDFGLARF- 364
Cdd:cd14119   75 MEYC-VGGLQEMLDSAPDKRLPIW--QAHGYFVQLIDGLEYLH--SQGIIHKDIKPGNLLLttDGTL--KISDFGVAEAl 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 189011594 365 SRFAGANpsqsstvaRTCTVRGTLAYLPEEyiktgrLAVDTDTFS 409
Cdd:cd14119  148 DLFAEDD--------TCTTSQGSPAFQPPE------IANGQDSFS 178
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
218-416 4.11e-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: 55.35  E-value: 4.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTY--AVKRLK---EEADLEWTVVKQsfLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLP 292
Cdd:cd07863    8 IGVGAYGTVYKARDPHSGHfvALKSVRvqtNEDGLPLSTVRE--VALLKRLEAFDHPNIVRLMDVCATSRTDRETKVTLV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLEDQLHLQTQACSPLSWPQRL--DILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFsrfaga 370
Cdd:cd07863   86 FEHVDQDLRTYLDKVPPPGLPAETikDLMRQFLRGLDFLHANC--IVHRDLKPENILVTSGGQVKLADFGLARI------ 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 189011594 371 npsQSSTVARTCTVRgTLAYLPEEYIKTGRLAVDTDTFSFGVVILE 416
Cdd:cd07863  158 ---YSCQMALTPVVV-TLWYRAPEVLLQSTYATPVDMWSVGCIFAE 199
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
218-418 4.29e-08

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


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 55.05  E-value: 4.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEWTVVKQSFLT-EVEQLSRFRHPNIVDFAGYCAESGFYCL--VYGFLP 292
Cdd:cd06652   10 LGQGAFGRVYLCYDADTgrELAVKQVQFDPESPETSKEVNALEcEIQLLKNLLHERIVQYYGCLRDPQERTLsiFMEYMP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLEDQLHLQTQACSPLSWPQRLDILLGtaraIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfaganp 372
Cdd:cd06652   90 GGSIKDQLKSYGALTENVTRKYTRQILEG----VHYLH--SNMIVHRDIKGANILRDSVGNVKLGDFGASK--------- 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 189011594 373 sQSSTVARTCT----VRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETL 418
Cdd:cd06652  155 -RLQTICLSGTgmksVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEML 203
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
218-362 5.01e-08

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: 54.64  E-value: 5.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT--YAVK-----RLKEEADLewtvVKqsflTEVEQLSRFRHPNIVD-FAGYCAESGFYcLVYG 289
Cdd:cd14095    8 IGDGNFAVVKECRDKATDkeYALKiidkaKCKGKEHM----IE----NEVAILRRVKHPNIVQlIEEYDTDTELY-LVME 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 290 FLPNGSLEDQLHLQTQacspLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLL----DERLMPKLGDFGLA 362
Cdd:cd14095   79 LVKGGDLFDAITSSTK----FTERDASRMVTDLAQALKYLH--SLSIVHRDIKPENLLVveheDGSKSLKLADFGLA 149
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
212-432 5.25e-08

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: 55.36  E-value: 5.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELRIGEGGFGCVYRAVMRNT--TYAVKRLkEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYG 289
Cdd:cd05632    4 FRQYRVLGKGGFGEVCACQVRATgkMYACKRL-EKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDALCLVLT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLedQLHLQTQAcSPLSWPQRL-----DILLGtaraIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARf 364
Cdd:cd05632   83 IMNGGDL--KFHIYNMG-NPGFEEERAlfyaaEILCG----LEDLHREN--TVYRDLKPENILLDDYGHIRISDLGLAV- 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594 365 srfagANPSQSSTVARTctvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAKTK 432
Cdd:cd05632  153 -----KIPEGESIRGRV----GTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVK 211
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
201-394 5.29e-08

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


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 55.07  E-value: 5.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 201 PFCEISQgtcNFSEELRIGEGGFGCVYRAVMRNTT--YAVKRLKEEADlewtvvKQSF----LTEVEQLSRFRHPNIVDF 274
Cdd:cd07865    6 PFCDEVS---KYEKLAKIGQGTFGEVFKARHRKTGqiVALKKVLMENE------KEGFpitaLREIKILQLLKHENVVNL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 275 AGYCA---------ESGFYcLVYGFLPNgsleDQLHLQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSN 345
Cdd:cd07865   77 IEICRtkatpynryKGSIY-LVFEFCEH----DLAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIH--RNKILHRDMKAAN 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 189011594 346 VLLDERLMPKLGDFGLAR-FSRFAGANPSQSST-VArtctvrgTLAYLPEE 394
Cdd:cd07865  150 ILITKDGVLKLADFGLARaFSLAKNSQPNRYTNrVV-------TLWYRPPE 193
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
218-420 5.33e-08

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: 55.06  E-value: 5.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMR--NTTYAVKRLKEEAD-LEwtvvKQSFLTEVEQLSRFRH-PNIVDFAGYCAESGfYCLVYGFLPN 293
Cdd:cd06616   14 IGRGAFGTVNKMLHKpsGTIMAVKRIRSTVDeKE----QKRLLMDLDVVMRSSDcPYIVKFYGALFREG-DCWICMELMD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 294 GSLED---QLHLQTQACSPLswpqrlDIL----LGTARAIQFLHQDSpSLIHGDIKSSNVLLDERLMPKLGDFGLARFsr 366
Cdd:cd06616   89 ISLDKfykYVYEVLDSVIPE------EILgkiaVATVKALNYLKEEL-KIIHRDVKPSNILLDRNGNIKLCDFGISGQ-- 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594 367 faganpsQSSTVARTCTVrGTLAYLPEEYIKTGRLA----VDTDTFSFGVVILETLAG 420
Cdd:cd06616  160 -------LVDSIAKTRDA-GCRPYMAPERIDPSASRdgydVRSDVWSLGITLYEVATG 209
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
218-360 5.46e-08

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 52.06  E-value: 5.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRA--VMRNTTYAVKRLKEEADLEWTVVKQsfLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd13968    1 MGEGASAKVFWAegECTTIGVAVKIGDDVNNEEGEDLES--EMDILRRLKGLELNIPKVLVTEDVDGPNILLMELVKGGT 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 296 LEDQLhlqTQACSPLSWPQRldILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFG 360
Cdd:cd13968   79 LIAYT---QEEELDEKDVES--IMYQLAECMRLLH--SFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
218-420 5.53e-08

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: 55.31  E-value: 5.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKeeadlewtvvKQSFLtEVEQLSRFR----------HPNIVDFagYCA---ESG 282
Cdd:cd05599    9 IGRGAFGEVRLVRKKDTghVYAMKKLR----------KSEML-EKEQVAHVRaerdilaeadNPWVVKL--YYSfqdEEN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 283 FYcLVYGFLPNGSLedqlhlqtqacspLSWPQRLDIL---------LGTARAIQFLHQdsPSLIHGDIKSSNVLLDERLM 353
Cdd:cd05599   76 LY-LIMEFLPGGDM-------------MTLLMKKDTLteeetrfyiAETVLAIESIHK--LGYIHRDIKPDNLLLDARGH 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 354 PKLGDFGLARfsrfaGANPSQ--SSTVartctvrGTLAYL-PEEYIKTGrLAVDTDTFSFGVVILETLAG 420
Cdd:cd05599  140 IKLSDFGLCT-----GLKKSHlaYSTV-------GTPDYIaPEVFLQKG-YGKECDWWSLGVIMYEMLIG 196
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
215-420 5.54e-08

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 55.21  E-value: 5.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 215 ELR--IGEGGFGCVYRAVMRNTT--YAVKRLKEEADLEWTVVkQSFLTEVEQLSRFRHPNIVD-FAGYCAESGFYcLVYG 289
Cdd:PTZ00263  21 EMGetLGTGSFGRVRIAKHKGTGeyYAIKCLKKREILKMKQV-QHVAQEKSILMELSHPFIVNmMCSFQDENRVY-FLLE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLEDqlHLQTQACSP--LSWPQRLDILLgtarAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrf 367
Cdd:PTZ00263  99 FVVGGELFT--HLRKAGRFPndVAKFYHAELVL----AFEYLH--SKDIIYRDLKPENLLLDNKGHVKVTDFGFAK---- 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 189011594 368 aganpsqsSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:PTZ00263 167 --------KVPDRTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAG 211
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
212-420 5.93e-08

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely expressed in many tissues. It 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Despite this, the presumed pseudokinase (repeat 1) domain of Jak2 exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Inactivation of the repeat 1 domain increased Jak2 basal activity, suggesting that it modulates the kinase activity of the C-terminal catalytic (repeat 2) domain. The Jak2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270663 [Multi-domain]  Cd Length: 262  Bit Score: 54.57  E-value: 5.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELriGEGGFGCVYRAVMR-----NTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCL 286
Cdd:cd05078    3 FNESL--GQGTFTKIFKGIRRevgdyGQLHETEVLLKVLDKAHRNYSESFFEAASMMSQLSHKHLVLNYGVCVCGDENIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 287 VYGFLPNGSLEDQLHlQTQACSPLSWpqRLDILLGTARAIQFLHQDspSLIHGDIKSSNVLLDERLMPKLGDFGLARFSr 366
Cdd:cd05078   81 VQEYVKFGSLDTYLK-KNKNCINILW--KLEVAKQLAWAMHFLEEK--TLVHGNVCAKNILLIREEDRKTGNPPFIKLS- 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 367 fagaNPSQSSTVARTCTVRGTLAYLPEEYIKTGR-LAVDTDTFSFGVVILETLAG 420
Cdd:cd05078  155 ----DPGISITVLPKDILLERIPWVPPECIENPKnLSLATDKWSFGTTLWEICSG 205
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
253-509 7.40e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 55.39  E-value: 7.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 253 KQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVygfLPNGSLEDQLHLQTQACSPLSwpQRLDILLGTARAIQFLHQD 332
Cdd:PHA03212 127 RGGTATEAHILRAINHPSIIQLKGTFTYNKFTCLI---LPRYKTDLYCYLAAKRNIAIC--DILAIERSVLRAIQYLHEN 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 333 spSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAGANpsqsstvaRTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGV 412
Cdd:PHA03212 202 --RIIHRDIKAENIFINHPGDVCLGDFGAACFPVDINAN--------KYYGWAGTIATNAPELLARDPYGPAVDIWSAGI 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 413 VILETLAGQRAVrtqgaktkYLKDLIE---DEAEEVGVTLKSTqptlwmGVATDAWtaPIAAQ-----IYK---KHLDSR 481
Cdd:PHA03212 272 VLFEMATCHDSL--------FEKDGLDgdcDSDRQIKLIIRRS------GTHPNEF--PIDAQanldeIYIglaKKSSRK 335
                        250       260       270
                 ....*....|....*....|....*....|...
gi 189011594 482 PGPCPP-----QLGLALAQLACCCMHRRAKKRP 509
Cdd:PHA03212 336 PGSRPLwtnlyELPIDLEYLICKMLAFDAHHRP 368
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
218-438 8.10e-08

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: 54.23  E-value: 8.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEadlEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd14183   14 IGDGNFAVVKECVERSTgrEYALKIINKS---KCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMELVKGGD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLhlqtqaCSPLSWPQR--LDILLGTARAIQFLHqdSPSLIHGDIKSSNVLL----DERLMPKLGDFGLArfsrfag 369
Cdd:cd14183   91 LFDAI------TSTNKYTERdaSGMLYNLASAIKYLH--SLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLA------- 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 370 anpsqSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAKTKYLKDLI 438
Cdd:cd14183  156 -----TVVDGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVLFDQI 219
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
220-363 8.56e-08

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: 54.38  E-value: 8.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 220 EGGFGCVYRAVMRNttyavKRLKEEADLEWTVVKQS-------FLTEVEQLSRFRHPNIVDFAGYCAE-SGFYCLVYGFL 291
Cdd:cd05043   16 EGTFGRIFHGILRD-----EKGKEEEVLVKTVKDHAseiqvtmLLQESSLLYGLSHQNLLPILHVCIEdGEKPMVLYPYM 90
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594 292 PNGSLedQLHLQTQACSPLSWPQRLD----ILLGT--ARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLAR 363
Cdd:cd05043   91 NWGNL--KLFLQQCRLSEANNPQALStqqlVHMALqiACGMSYLH--RRGVIHKDIAARNCVIDDELQVKITDNALSR 164
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
218-421 8.84e-08

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: 54.23  E-value: 8.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT--YAVKRLKEEADLEwtVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd07848    9 VGEGAYGVVLKCRHKETKeiVAIKKFKDSEENE--EVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEKNM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLHLQTQACsplswPQRL-DILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfagaNPSQ 374
Cdd:cd07848   87 LELLEEMPNGVP-----PEKVrSYIYQLIKAIHWCHKND--IVHRDIKPENLLISHNDVLKLCDFGFAR-------NLSE 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 189011594 375 SSTVARTCTVrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd07848  153 GSNANYTEYV-ATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQ 198
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
204-421 9.50e-08

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 54.20  E-value: 9.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 204 EISQGTCNFSEELriGEGGFGCVYRAVMRN-------TTYAVKRLKEEADLEWTVvkqSFLTEVEQLSRFRHPNIVDFAG 276
Cdd:cd05061    2 EVSREKITLLREL--GQGSFGMVYEGNARDiikgeaeTRVAVKTVNESASLRERI---EFLNEASVMKGFTCHHVVRLLG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 277 YCAESGFYCLVYGFLPNGSLEDQLH-LQTQA-CSPLSWPQRLDILLGTARAIQ--FLHQDSPSLIHGDIKSSNVLLDERL 352
Cdd:cd05061   77 VVSKGQPTLVVMELMAHGDLKSYLRsLRPEAeNNPGRPPPTLQEMIQMAAEIAdgMAYLNAKKFVHRDLAARNCMVAHDF 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 353 MPKLGDFGLAR------FSRFAGanpsqsstvartctvRGTL--AYLPEEYIKTGRLAVDTDTFSFGVVILE--TLAGQ 421
Cdd:cd05061  157 TVKIGDFGMTRdiyetdYYRKGG---------------KGLLpvRWMAPESLKDGVFTTSSDMWSFGVVLWEitSLAEQ 220
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
217-421 1.02e-07

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: 53.71  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMR--NTTYAVKRLKEEADLEWTVvkQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNG 294
Cdd:cd14097    8 KLGQGSFGVVIEATHKetQTKWAIKKINREKAGSSAV--KLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMELCEDG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEDQLHLQTQacspLSWPQRLDILLGTARAIQFLHQDspSLIHGDIKSSNVLL-------DERLMPKLGDFGLARFSRF 367
Cdd:cd14097   86 ELKELLLRKGF----FSENETRHIIQSLASAVAYLHKN--DIVHRDLKLENILVkssiidnNDKLNIKVTDFGLSVQKYG 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 189011594 368 AGANPSQSstvarTCtvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd14097  160 LGEDMLQE-----TC---GTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGE 205
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
218-445 1.10e-07

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


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 53.86  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAV-MRNTTY-AVKrlKEEADLEWT-VVKQSF----LTEVEQLSRFRHPNIVD-FAGYCAESGFYCLVYG 289
Cdd:cd13990    8 LGKGGFSEVYKAFdLVEQRYvACK--IHQLNKDWSeEKKQNYikhaLREYEIHKSLDHPRIVKlYDVFEIDTDSFCTVLE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLEdqLHLQTQAcsplSWPQRL--DILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLMP---KLGDFGLarf 364
Cdd:cd13990   86 YCDGNDLD--FYLKQHK----SIPEREarSIIMQVVSALKYLNEIKPPIIHYDLKPGNILLHSGNVSgeiKITDFGL--- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 365 SRFAGANPSQSSTVARTCTVRGTLAYLPEEYIKTG----RLAVDTDTFSFGVVILETLAGQRAVRTQGAKTKYLKDLIED 440
Cdd:cd13990  157 SKIMDDESYNSDGMELTSQGAGTYWYLPPECFVVGktppKISSKVDVWSVGVIFYQMLYGRKPFGHNQSQEAILEENTIL 236

                 ....*
gi 189011594 441 EAEEV 445
Cdd:cd13990  237 KATEV 241
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
326-454 1.19e-07

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 54.88  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 326 IQFL----HQDSPSLIHGDIKSSNVLLDERLMPKLGDFGlarFSRFAGAnpSQSSTVART-CtvrGTLAYLPEEYIKTGR 400
Cdd:PTZ00283 150 IQVLlavhHVHSKHMIHRDIKSANILLCSNGLVKLGDFG---FSKMYAA--TVSDDVGRTfC---GTPYYVAPEIWRRKP 221
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594 401 LAVDTDTFSFGVVILETLAGQRAV----------RTQGAKTKYLKDLIEDEAEEVGVTLKSTQP 454
Cdd:PTZ00283 222 YSKKADMFSLGVLLYELLTLKRPFdgenmeevmhKTLAGRYDPLPPSISPEMQEIVTALLSSDP 285
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
218-416 1.22e-07

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 53.79  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMR-----NTTYAVKRLKEEADLEWTVvkQSFLTEVEQLSRFRHPNIVDFAGYCAESGFY-----CLV 287
Cdd:cd14204   15 LGEGEFGSVMEGELQqpdgtNHKVAVKTMKLDNFSQREI--EEFLSEAACMKDFNHPNVIRLLGVCLEVGSQripkpMVI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 288 YGFLPNGSLEDQLHLQTQACSPLSWPQR--LDILLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfS 365
Cdd:cd14204   93 LPFMKYGDLHSFLLRSRLGSGPQHVPLQtlLKFMIDIALGMEYL--SSRNFLHRDLAARNCMLRDDMTVCVADFGLSK-K 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 189011594 366 RFAGANPSQsstvartctvrGTLAYLPEEYIKTGRLA-----VDTDTFSFGVVILE 416
Cdd:cd14204  170 IYSGDYYRQ-----------GRIAKMPVKWIAVESLAdrvytVKSDVWAFGVTMWE 214
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
218-420 1.31e-07

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: 54.17  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT--YAVKRLKEEADLEWTVVKQSfLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd05574    9 LGKGDVGRVYLVRLKGTGklFAMKVLDKEEMIKRNKVKRV-LTEREILATLDHPFLPTLYASFQTSTHLCFVMDYCPGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLHLQTQACSPLSWPQ--RLDILLgtarAIQFLHqdSPSLIHGDIKSSNVLLDE--RLMpkLGDFGLA--------- 362
Cdd:cd05574   88 LFRLLQKQPGKRLPEEVARfyAAEVLL----ALEYLH--LLGFVYRDLKPENILLHEsgHIM--LTDFDLSkqssvtppp 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189011594 363 -RFSRFAGANPSQS----------STVARTCTVRGTLAYLPEEYIK-TGR-LAVdtDTFSFGVVILETLAG 420
Cdd:cd05574  160 vRKSLRKGSRRSSVksieketfvaEPSARSNSFVGTEEYIAPEVIKgDGHgSAV--DWWTLGILLYEMLYG 228
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
211-421 1.37e-07

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: 53.85  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 211 NFSEELRIGEGGFGCVYRAVMRNTT--YAVKRLKEEA-----DLEWTVV---------KQSFLTEVEqlSRFRHPNIVDF 274
Cdd:cd05616    1 DFNFLMVLGKGSFGKVMLAERKGTDelYAVKILKKDVviqddDVECTMVekrvlalsgKPPFLTQLH--SCFQTMDRLYF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 275 agycaesgfyclVYGFLPNGSLedqlHLQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMP 354
Cdd:cd05616   79 ------------VMEYVNGGDL----MYHIQQVGRFKEPHAVFYAAEIAIGLFFLQ--SKGIIYRDLKLDNVMLDSEGHI 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 355 KLGDFGLARFSRFAGANpsqsstvarTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd05616  141 KIADFGMCKENIWDGVT---------TKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQ 198
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
218-363 1.74e-07

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: 53.91  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEADlEWTVVKQSfLTEVEQLSRFRHPNIVdfagycaesgfyCLVYGFLPNGS 295
Cdd:cd07855   13 IGSGAYGVVCSAIDTKSgqKVAIKKIPNAFD-VVTTAKRT-LRELKILRHFKHDNII------------AIRDILRPKVP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LED-------------QLHLQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLA 362
Cdd:cd07855   79 YADfkdvyvvldlmesDLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIH--SANVIHRDLKPSNLLVNENCELKIGDFGMA 156

                 .
gi 189011594 363 R 363
Cdd:cd07855  157 R 157
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
215-420 1.88e-07

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


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 52.90  E-value: 1.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 215 ELRIGEGGFGCVYRAVMRNT--TYAVKRLKeeadlewtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLP 292
Cdd:cd13991   11 QLRIGRGSFGEVHRMEDKQTgfQCAVKKVR---------LEVFRAEELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLeDQLhLQTQACSPLSwpQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLL-DERLMPKLGDFGLARFSRFAGan 371
Cdd:cd13991   82 GGSL-GQL-IKEQGCLPED--RALHYLGQALEGLEYLH--SRKILHGDVKADNVLLsSDGSDAFLCDFGHAECLDPDG-- 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 189011594 372 psQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd13991  154 --LGKSLFTGDYIPGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNG 200
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
298-360 1.91e-07

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 52.88  E-value: 1.91e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 298 DQLH--LQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFG 360
Cdd:cd13975   85 ERLHrdLYTGIKAGLSLEERLQIALDVVEGIRFLH--SQGLVHRDIKLKNVLLDKKNRAKITDLG 147
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
218-421 1.98e-07

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: 53.46  E-value: 1.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT--YAVKRLK-------EEADlewtvvkqSFLTE---VEQLSRFRHPNIVDFAGYCAESGFYC 285
Cdd:cd05589    7 LGRGHFGKVLLAEYKPTGelFAIKALKkgdiiarDEVE--------SLMCEkriFETVNSARHPFLVNLFACFQTPEHVC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 286 LVYGFLPNGSLedQLHLQTQ-----------ACsplswpqrldILLGtaraIQFLHQDSpsLIHGDIKSSNVLLDERLMP 354
Cdd:cd05589   79 FVMEYAAGGDL--MMHIHEDvfsepravfyaAC----------VVLG----LQFLHEHK--IVYRDLKLDNLLLDTEGYV 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 355 KLGDFGLARFSRFAGanpsqsstvARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd05589  141 KIADFGLCKEGMGFG---------DRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGE 198
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
216-421 2.26e-07

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: 53.10  E-value: 2.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 216 LRIGEGGFGCVYRAVMRNT--TYAVKRLkeeaDLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPN 293
Cdd:cd06657   26 IKIGEGSTGIVCIATVKSSgkLVAVKKM----DLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 294 GSLEDQLhlqtqACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLArfsrfaganPS 373
Cdd:cd06657  102 GALTDIV-----THTRMNEEQIAAVCLAVLKALSVLH--AQGVIHRDIKSDSILLTHDGRVKLSDFGFC---------AQ 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 189011594 374 QSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd06657  166 VSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGE 213
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
217-416 2.36e-07

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 53.12  E-value: 2.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWtvVKQsflTEVEQLSRFRHPNIV-----DFAGYCAESGFYcLVYGFL 291
Cdd:cd14220    2 QIGKGRYGEVWMGKWRGEKVAVKVFFTTEEASW--FRE---TEIYQTVLMRHENILgfiaaDIKGTGSWTQLY-LITDYH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 PNGSLEDQLHlqtqaCSPLSWPQRLDILLGTARAIQFLH------QDSPSLIHGDIKSSNVLLDERLMPKLGDFGLA-RF 364
Cdd:cd14220   76 ENGSLYDFLK-----CTTLDTRALLKLAYSAACGLCHLHteiygtQGKPAIAHRDLKSKNILIKKNGTCCIADLGLAvKF 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 365 SrfaganpSQSSTVARTCTVR-GTLAYLPEEYIKTG------RLAVDTDTFSFGVVILE 416
Cdd:cd14220  151 N-------SDTNEVDVPLNTRvGTKRYMAPEVLDESlnknhfQAYIMADIYSFGLIIWE 202
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
217-420 2.44e-07

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: 52.51  E-value: 2.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRA--VMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNG 294
Cdd:cd14070    9 KLGEGSFAKVREGlhAVTGEKVAIKVIDKKKAKKDSYVTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVMELCPGG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEDQLHLQtqacsplswpQRLD------ILLGTARAIQFLHQdsPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFA 368
Cdd:cd14070   89 NLMHRIYDK----------KRLEerearrYIRQLVSAVEHLHR--AGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGIL 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 189011594 369 GAnpsqSSTVARTCtvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd14070  157 GY----SDPFSTQC---GSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTG 201
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
239-420 2.86e-07

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: 52.45  E-value: 2.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 239 KRLKEEADLEWTVVKQSFLTEVeqlsrFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLEDQLhlqtQACSPLSWPQRLDI 318
Cdd:cd14077   48 KRLEKEISRDIRTIREAALSSL-----LNHPHICRLRDFLRTPNHYYMLFEYVDGGQLLDYI----ISHGKLKEKQARKF 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 319 LLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFSRfaganpsqSSTVART-CtvrGTLAYLPEEYIK 397
Cdd:cd14077  119 ARQIASALDYLHRNS--IVHRDLKIENILISKSGNIKIIDFGLSNLYD--------PRRLLRTfC---GSLYFAAPELLQ 185
                        170       180
                 ....*....|....*....|....
gi 189011594 398 TGR-LAVDTDTFSFGVVILETLAG 420
Cdd:cd14077  186 AQPyTGPEVDVWSFGVVLYVLVCG 209
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
218-420 3.02e-07

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


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 52.20  E-value: 3.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEWTVVKQsfltEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd14114   10 LGTGAFGVVHRCTERATgnNFAAKFIMTPHESDKETVRK----EIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLSGGE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLhlqTQACSPLSWPQRLDILLGTARAIQFLHQDspSLIHGDIKSSNVLLDERLMP--KLGDFGLArfsrfAGANPS 373
Cdd:cd14114   86 LFERI---AAEHYKMSEAEVINYMRQVCEGLCHMHEN--NIVHLDIKPENIMCTTKRSNevKLIDFGLA-----THLDPK 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 189011594 374 QSSTVartctVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd14114  156 ESVKV-----TTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSG 197
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
218-418 3.47e-07

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: 52.39  E-value: 3.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEWTVVKQSFLT-EVEQLSRFRHPNIVDFAGYCAESGFYCLV--YGFLP 292
Cdd:cd06651   15 LGQGAFGRVYLCYDVDTgrELAAKQVQFDPESPETSKEVSALEcEIQLLKNLQHERIVQYYGCLRDRAEKTLTifMEYMP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLEDQLHLQTQACSPLSWPQRLDILLGtaraIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRfagaNP 372
Cdd:cd06651   95 GGSVKDQLKAYGALTESVTRKYTRQILEG----MSYLH--SNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQ----TI 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 189011594 373 SQSSTVARTCTvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETL 418
Cdd:cd06651  165 CMSGTGIRSVT--GTPYWMSPEVISGEGYGRKADVWSLGCTVVEML 208
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
218-421 3.70e-07

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: 52.78  E-value: 3.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT--YAVKRLKEEA-----DLEWTVV---------KQSFLTEVEqlSRFRHPNIVDFagycaes 281
Cdd:cd05587    4 LGKGSFGKVMLAERKGTDelYAIKILKKDViiqddDVECTMVekrvlalsgKPPFLTQLH--SCFQTMDRLYF------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 282 gfyclVYGFLPNGSLedqlHLQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGL 361
Cdd:cd05587   75 -----VMEYVNGGDL----MYHIQQVGKFKEPVAVFYAAEIAVGLFFLH--SKGIIYRDLKLDNVMLDAEGHIKIADFGM 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 362 ARFSRFAGANpsqsstvarTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd05587  144 CKEGIFGGKT---------TRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQ 194
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
212-420 3.82e-07

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


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 52.27  E-value: 3.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEElRIGEGGFG-CVYRAVMRNTTYAVKRLKEE----ADLEWTVVKQSFLteveqlsrfrHPNIVDFagYCAES--GFY 284
Cdd:cd13982    4 FSPK-VLGYGSEGtIVFRGTFDGRPVAVKRLLPEffdfADREVQLLRESDE----------HPNVIRY--FCTEKdrQFL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 285 CLVYGFLPnGSLEDqlHLQTQACSPL---SWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLD-----ERLMPKL 356
Cdd:cd13982   71 YIALELCA-ASLQD--LVESPRESKLflrPGLEPVRLLRQIASGLAHLH--SLNIVHRDLKPQNILIStpnahGNVRAMI 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 357 GDFGLARfsRFAGAnpsqSSTVARTCTVRGTLAYLPEEYI---KTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd13982  146 SDFGLCK--KLDVG----RSSFSRRSGVAGTSGWIAPEMLsgsTKRRQTRAVDIFSLGCVFYYVLSG 206
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
218-414 4.87e-07

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: 51.49  E-value: 4.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRN-TTYAVK-----RLKEEADLewTVVKQsfltEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFL 291
Cdd:cd14161   11 LGKGTYGRVKKARDSSgRLVAIKsirkdRIKDEQDL--LHIRR----EIEIMSSLNHPHIISVYEVFENSSKIVIVMEYA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 PNGSLEDQLHLQtqacSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFSRfagan 371
Cdd:cd14161   85 SRGDLYDYISER----QRLSELEARHFFRQIVSAVHYCHANG--IVHRDLKLENILLDANGNIKIADFGLSNLYN----- 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 189011594 372 psQSSTVARTCtvrGTLAYLPEEyIKTGR--LAVDTDTFSFGVVI 414
Cdd:cd14161  154 --QDKFLQTYC---GSPLYASPE-IVNGRpyIGPEVDSWSLGVLL 192
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
218-420 5.00e-07

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: 51.61  E-value: 5.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEA---DLewTVVKqsflTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLP 292
Cdd:cd14078   11 IGSGGFAKVKLATHILTgeKVAIKIMDKKAlgdDL--PRVK----TEIEALKNLSHQHICRLYHVIETDNKIFMVLEYCP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLEDQLHLQTQacspLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLArfsrfagANP 372
Cdd:cd14078   85 GGELFDYIVAKDR----LSEDEARVFFRQIVSAVAYVH--SQGYAHRDLKPENLLLDEDQNLKLIDFGLC-------AKP 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 189011594 373 SQSSTVA-RTCTvrGTLAYLPEEYIKTGR-LAVDTDTFSFGVVILETLAG 420
Cdd:cd14078  152 KGGMDHHlETCC--GSPAYAAPELIQGKPyIGSEADVWSMGVLLYALLCG 199
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
218-420 5.12e-07

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 52.29  E-value: 5.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTY---AVKRLKEEADLEWTVVKQSFlTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNG 294
Cdd:PTZ00426  38 LGTGSFGRVILATYKNEDFppvAIKRFEKSKIIKQKQVDHVF-SERKILNYINHPFCVNLYGSFKDESYLYLVLEFVIGG 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEDQLHLQTQacsplsWPQRLDILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRfaganpsq 374
Cdd:PTZ00426 117 EFFTFLRRNKR------FPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVD-------- 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 189011594 375 sstvARTCTVRGTLAYL-PEEYIKTGRlAVDTDTFSFGVVILETLAG 420
Cdd:PTZ00426 183 ----TRTYTLCGTPEYIaPEILLNVGH-GKAADWWTLGIFIYEILVG 224
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
206-533 5.17e-07

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: 52.34  E-value: 5.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 206 SQGTCNFSEELRIGEGGFGCVYRAVMRNT--TYAVKRLKEE-----ADLEWTVVKQSFLtevEQLSRfrHPNIVDF-AGY 277
Cdd:cd05618   16 SLGLQDFDLLRVIGRGSYAKVLLVRLKKTerIYAMKVVKKElvnddEDIDWVQTEKHVF---EQASN--HPFLVGLhSCF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 278 CAESGFYcLVYGFLPNGSLedQLHLQTQACSPLSWPQRldILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLG 357
Cdd:cd05618   91 QTESRLF-FVIEYVNGGDL--MFHMQRQRKLPEEHARF--YSAEISLALNYLHERG--IIYRDLKLDNVLLDSEGHIKLT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 358 DFGLARfsrfAGANPSQSstvarTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAKTKYLKDl 437
Cdd:cd05618  164 DYGMCK----EGLRPGDT-----TSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQN- 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 438 IEDEAEEVgVTLKSTQPTLWMGVAtdawtapiAAQIYKKHLDSRPGP---CPPQLGLALAQlacccmhrrakKRPPMTQV 514
Cdd:cd05618  234 TEDYLFQV-ILEKQIRIPRSLSVK--------AASVLKSFLNKDPKErlgCHPQTGFADIQ-----------GHPFFRNV 293
                        330       340
                 ....*....|....*....|
gi 189011594 515 -YKRLEGLQAVPPWKLEVAG 533
Cdd:cd05618  294 dWDLMEQKQVVPPFKPNISG 313
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
218-422 5.66e-07

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: 51.66  E-value: 5.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFG--CVYRAVMRNTTYAVK-----RLKEEadlewtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGF 290
Cdd:cd08221    8 LGRGAFGeaVLYRKTEDNSLVVWKevnlsRLSEK-------ERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDQLHLQTQACspLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFSrfaga 370
Cdd:cd08221   81 CNGGNLHDKIAQQKNQL--FPEEVVLWYLYQIVSAVSHIHKAG--ILHRDIKTLNIFLTKADLVKLGDFGISKVL----- 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 189011594 371 npSQSSTVARTCTvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQR 422
Cdd:cd08221  152 --DSESSMAESIV--GTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKR 199
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
218-420 6.22e-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: 51.94  E-value: 6.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT--YAVKRLKEEadlewtvvKQSFLTEVEQLSRF-RHPNIVDFAGYCAESGFYCLVYGFLPNG 294
Cdd:cd14177   12 IGVGSYSVCKRCIHRATNmeFAVKIIDKS--------KRDPSEEIEILMRYgQHPNIITLKDVYDDGRYVYLVTELMKGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEDQlhLQTQACspLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVL-LDERLMP---KLGDFGLARFSRfaga 370
Cdd:cd14177   84 ELLDR--ILRQKF--FSEREASAVLYTITKTVDYLH--CQGVVHRDLKPSNILyMDDSANAdsiRICDFGFAKQLR---- 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 189011594 371 npSQSSTVARTCTVRGTLAylPEEYIKTGRLAVdTDTFSFGVVILETLAG 420
Cdd:cd14177  154 --GENGLLLTPCYTANFVA--PEVLMRQGYDAA-CDIWSLGVLLYTMLAG 198
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
218-366 6.42e-07

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


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 51.48  E-value: 6.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRL-KEEADLEwtvvkqsflTEVEQLSRF-RHPNIVDFAGYCAESGFYCLVYGFLPN 293
Cdd:cd14091    8 IGKGSYSVCKRCIHKATgkEYAVKIIdKSKRDPS---------EEIEILLRYgQHPNIITLRDVYDDGNSVYLVTELLRG 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 294 GSLEDQLHLQTQacspLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLL-DERLMP---KLGDFGLARFSR 366
Cdd:cd14091   79 GELLDRILRQKF----FSEREASAVMKTLTKTVEYLHSQG--VVHRDLKPSNILYaDESGDPeslRICDFGFAKQLR 149
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
218-433 6.86e-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: 51.17  E-value: 6.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRA--VMRNTTYAVKrLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFyclVYGFLPNGS 295
Cdd:cd14188    9 LGKGGFAKCYEMtdLTTNKVYAAK-IIPHSRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKEN---IYILLEYCS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLHLqTQACSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLArfsrfAGANPSQS 375
Cdd:cd14188   85 RRSMAHI-LKARKVLTEPEVRYYLRQIVSGLKYLHEQE--ILHRDLKLGNFFINENMELKVGDFGLA-----ARLEPLEH 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594 376 stvaRTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAKTKY 433
Cdd:cd14188  157 ----RRRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETY 210
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
218-364 6.99e-07

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: 51.73  E-value: 6.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEW---TVVKqsfltEVEQLSRFRHPNIV----------DFAGYCAESG 282
Cdd:cd07864   15 IGEGTYGQVYKAKDKDTgeLVALKKVRLDNEKEGfpiTAIR-----EIKILRQLNHRSVVnlkeivtdkqDALDFKKDKG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 283 FYCLVYGFLPN---GSLEDQL--HLQTQACSPLSwpQRLDillgtarAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLG 357
Cdd:cd07864   90 AFYLVFEYMDHdlmGLLESGLvhFSEDHIKSFMK--QLLE-------GLNYCHKKN--FLHRDIKCSNILLNNKGQIKLA 158

                 ....*..
gi 189011594 358 DFGLARF 364
Cdd:cd07864  159 DFGLARL 165
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
218-438 7.13e-07

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: 51.19  E-value: 7.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLkeeaDLEWTVVKQSFL-TEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNG 294
Cdd:cd14184    9 IGDGNFAVVKECVERSTgkEFALKII----DKAKCCGKEHLIeNEVSILRRVKHPNIIMLIEEMDTPAELYLVMELVKGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLEDQLHLQTQacsplsWPQR--LDILLGTARAIQFLHqdSPSLIHGDIKSSNVLL----DERLMPKLGDFGLArfsrfa 368
Cdd:cd14184   85 DLFDAITSSTK------YTERdaSAMVYNLASALKYLH--GLCIVHRDIKPENLLVceypDGTKSLKLGDFGLA------ 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189011594 369 ganpsqssTVAR--TCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAKTKYLKDLI 438
Cdd:cd14184  151 --------TVVEgpLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQEDLFDQI 214
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
218-364 7.59e-07

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: 51.23  E-value: 7.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVK-----RLKEEADLewtvvkQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGF 290
Cdd:cd14073    9 LGKGTYGKVKLAIERATgrEVAIKsikkdKIEDEQDM------VRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEY 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594 291 LPNGSLEDQLhlqtQACSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARF 364
Cdd:cd14073   83 ASGGELYDYI----SERRRLPEREARRIFRQIVSAVHYCHKNG--VVHRDLKLENILLDQNGNAKIADFGLSNL 150
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
218-416 8.90e-07

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: 51.15  E-value: 8.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRN--TTYAVKRLK------EEADLEWTVVKqsflteveqlSRFRHPNIVDFAG--YCAES---GFY 284
Cdd:cd06639   30 IGKGTYGKVYKVTNKKdgSLAAVKILDpisdvdEEIEAEYNILR----------SLPNHPNVVKFYGmfYKADQyvgGQL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 285 CLVYGFLPNGSLEDQLHlqtqacSPLSWPQRLD------ILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGD 358
Cdd:cd06639  100 WLVLELCNGGSVTELVK------GLLKCGQRLDeamisyILYGALLGLQHLHNNR--IIHRDVKGNNILLTTEGGVKLVD 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189011594 359 FGLArfsrfaganPSQSSTVARTCTVRGTLAYLPEEYIKTGR-----LAVDTDTFSFGVVILE 416
Cdd:cd06639  172 FGVS---------AQLTSARLRRNTSVGTPFWMAPEVIACEQqydysYDARCDVWSLGITAIE 225
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
218-420 1.02e-06

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: 50.83  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT---YAVKRLKEEadlewTVVK-QSFLT-EVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLP 292
Cdd:cd14120    1 IGHGAFAVVFKGRHRKKPdlpVAIKCITKK-----NLSKsQNLLGkEIKILKELSHENVVALLDCQETSSSVYLVMEYCN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLEDQLHLQTQacspLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLL--DERLMP-------KLGDFGLAR 363
Cdd:cd14120   76 GGDLADYLQAKGT----LSEDTIRVFLQQIAAAMKALH--SKGIVHRDLKPQNILLshNSGRKPspndirlKIADFGFAR 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594 364 FsrfaganpSQSSTVART-CtvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd14120  150 F--------LQDGMMAATlC---GSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTG 196
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
218-420 1.04e-06

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: 51.17  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT--YAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIV--DFAGYCAESGFYCLVYgflPN 293
Cdd:cd05602   15 IGKGSFGKVLLARHKSDEkfYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVglHFSFQTTDKLYFVLDY---IN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 294 GSlEDQLHLQTQACspLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfagANPS 373
Cdd:cd05602   92 GG-ELFYHLQRERC--FLEPRARFYAAEIASALGYLH--SLNIVYRDLKPENILLDSQGHIVLTDFGLCK------ENIE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 189011594 374 QSSTVARTCtvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd05602  161 PNGTTSTFC---GTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYG 204
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
248-365 1.05e-06

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 50.56  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 248 EWTVVK-QSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLEDQLHLQTQACSPLSwpQRLDILLGTARAI 326
Cdd:cd14057   30 DVTTRIsRDFNEEYPRLRIFSHPNVLPVLGACNSPPNLVVISQYMPYGSLYNVLHEGTGVVVDQS--QAVKFALDIARGM 107
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 189011594 327 QFLHQDSPSLIHGDIKSSNVLLDERLMPKLgDFGLARFS 365
Cdd:cd14057  108 AFLHTLEPLIPRHHLNSKHVMIDEDMTARI-NMADVKFS 145
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
211-363 1.05e-06

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: 50.94  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 211 NFSEELRIGEGGFGCVYRAVMRNTT--YAVKRLKEEADlEWTvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVY 288
Cdd:cd07836    1 NFKQLEKLGEGTYATVYKGRNRTTGeiVALKEIHLDAE-EGT--PSTAIREISLMKELKHENIVRLHDVIHTENKLMLVF 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 289 GFLpNGSLEDQLHLQTQACsPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLAR 363
Cdd:cd07836   78 EYM-DKDLKKYMDTHGVRG-ALDPNTVKSFTYQLLKGIAFCHENR--VLHRDLKPQNLLINKRGELKLADFGLAR 148
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
218-450 1.27e-06

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 50.83  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAV-MRNTTYAVKRLkEEADLEWTVVKQS-----FLTEVEQLSRFRHPNIVDFAGYCA-ESGFYCLVYGF 290
Cdd:cd14040   14 LGRGGFSEVYKAFdLYEQRYAAVKI-HQLNKSWRDEKKEnyhkhACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEdqLHLQTQACspLSWPQRLDILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLM---PKLGDFGLarfSRF 367
Cdd:cd14040   93 CEGNDLD--FYLKQHKL--MSEKEARSIVMQIVNALRYLNEIKPPIIHYDLKPGNILLVDGTAcgeIKITDFGL---SKI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 368 AGANPSQSSTVARTCTVRGTLAYLPEEYIKTG----RLAVDTDTFSFGVVILETLAGQRAVRTQGAKTKYLKDLIEDEAE 443
Cdd:cd14040  166 MDDDSYGVDGMDLTSQGAGTYWYLPPECFVVGkeppKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTILKAT 245

                 ....*..
gi 189011594 444 EVGVTLK 450
Cdd:cd14040  246 EVQFPVK 252
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
218-420 1.28e-06

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: 50.30  E-value: 1.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEwtvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd14190   12 LGGGKFGKVHTCTEKRTglKLAAKVINKQNSKD----KEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLhlqTQACSPLSWPQRLDILLGTARAIQFLHQdsPSLIHGDIKSSNVLLDERL--MPKLGDFGLARfsRFagaNPS 373
Cdd:cd14190   88 LFERI---VDEDYHLTEVDAMVFVRQICEGIQFMHQ--MRVLHLDLKPENILCVNRTghQVKIIDFGLAR--RY---NPR 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 189011594 374 QSSTVARtctvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd14190  158 EKLKVNF-----GTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSG 199
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
253-419 1.34e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 51.03  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 253 KQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVygfLPNGSlEDQLHLQTQACSPLSWPQRLDILLGTARAIQFLHQD 332
Cdd:PHA03209 101 KGTTLIEAMLLQNVNHPSVIRMKDTLVSGAITCMV---LPHYS-SDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQ 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 333 SpsLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAGANpsqsstvartCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGV 412
Cdd:PHA03209 177 R--IIHRDVKTENIFINDVDQVCIGDLGAAQFPVVAPAF----------LGLAGTVETNAPEVLARDKYNSKADIWSAGI 244

                 ....*..
gi 189011594 413 VILETLA 419
Cdd:PHA03209 245 VLFEMLA 251
pknD PRK13184
serine/threonine-protein kinase PknD;
218-443 1.36e-06

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 51.69  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRA--VMRNTTYAVKRLKEeaDL-EWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESG--FYCLVY--GF 290
Cdd:PRK13184  10 IGKGGMGEVYLAydPVCSRRVALKKIRE--DLsENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDpvYYTMPYieGY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 -----LPN----GSLEDQLHLQTqacsplSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGL 361
Cdd:PRK13184  88 tlkslLKSvwqkESLSKELAEKT------SVGAFLSIFHKICATIEYVH--SKGVLHRDLKPDNILLGLFGEVVILDWGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 362 ARFSRF---------AGANPSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAKTK 432
Cdd:PRK13184 160 AIFKKLeeedlldidVDERNICYSSMTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKI 239
                        250
                 ....*....|.
gi 189011594 433 YLKDLIEDEAE 443
Cdd:PRK13184 240 SYRDVILSPIE 250
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
218-440 1.43e-06

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: 50.85  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCV--YRAVMRNTTYAVKRLKEEADLEWTVVKQSfLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd05593   23 LGKGTFGKVilVREKASGKYYAMKILKKEVIIAKDEVAHT-LTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGE 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLHLQTQACSPLSWPQRLDILlgtaRAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfagANPSQS 375
Cdd:cd05593  102 LFFHLSRERVFSEDRTRFYGAEIV----SALDYLH--SGKIVYRDLKLENLMLDKDGHIKITDFGLCK------EGITDA 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 376 STVARTCtvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAKTKYLKDLIED 440
Cdd:cd05593  170 ATMKTFC---GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMED 231
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
218-420 1.49e-06

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: 50.73  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVY--RAVMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd05604    4 IGKGSFGKVLlaKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVNGGE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LedQLHLQTQACSPlsWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfagANPSQS 375
Cdd:cd05604   84 L--FFHLQRERSFP--EPRARFYAAEIASALGYLH--SINIVYRDLKPENILLDSQGHIVLTDFGLCK------EGISNS 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 189011594 376 STVARTCtvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd05604  152 DTTTTFC---GTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYG 193
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
218-420 1.56e-06

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


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 50.01  E-value: 1.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTtyavkrlKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLE 297
Cdd:cd13995   12 IPRGAFGKVYLAQDTKT-------KKRMACKLIPVEQFKPSDVEIQACFRHENIAELYGALLWEETVHLFMEAGEGGSVL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 298 DQLhlqtQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSN-VLLDERLMpkLGDFGLArfsrfaganPSQSS 376
Cdd:cd13995   85 EKL----ESCGPMREFEIIWVTKHVLKGLDFLH--SKNIIHHDIKPSNiVFMSTKAV--LVDFGLS---------VQMTE 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 189011594 377 TVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd13995  148 DVYVPKDLRGTEIYMSPEVILCRGHNTKADIYSLGATIIHMQTG 191
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
218-421 1.62e-06

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: 50.77  E-value: 1.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT--YAVKRLKEEA-----DLEWTVVKQSFLTEVEQlsrfrhPNIVDFAGYCAES--GFYcLVY 288
Cdd:cd05615   18 LGKGSFGKVMLAERKGSDelYAIKILKKDVviqddDVECTMVEKRVLALQDK------PPFLTQLHSCFQTvdRLY-FVM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 289 GFLPNGSLedQLHLQTqaCSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFA 368
Cdd:cd05615   91 EYVNGGDL--MYHIQQ--VGKFKEPQAVFYAAEISVGLFFLHKKG--IIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVE 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 189011594 369 GANpsqsstvarTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd05615  165 GVT---------TRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQ 208
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
218-439 1.97e-06

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: 50.45  E-value: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAV------MRNTTYAVKRLKEEADLEWTVvkqSFLTEVEQLSRFRHPNIVDFAGYCAESGFYcLVYGFL 291
Cdd:cd05110   15 LGSGAFGTVYKGIwvpegeTVKIPVAIKILNETTGPKANV---EFMDEALIMASMDHPHLVRLLGVCLSPTIQ-LVTQLM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 PNGSLEDQLHLQTQACSP---LSWPQRLdillgtARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFsrFA 368
Cdd:cd05110   91 PHGCLLDYVHEHKDNIGSqllLNWCVQI------AKGMMYLEERR--LVHRDLAARNVLVKSPNHVKITDFGLARL--LE 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189011594 369 GANPSQSSTVARTctvrgTLAYLPEEYIKTGRLAVDTDTFSFGVVILE--TLAGQravRTQGAKTKYLKDLIE 439
Cdd:cd05110  161 GDEKEYNADGGKM-----PIKWMALECIHYRKFTHQSDVWSYGVTIWElmTFGGK---PYDGIPTREIPDLLE 225
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
218-421 2.05e-06

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 50.53  E-value: 2.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLK-EEADLEWTVVKQ---------SFLTEVEQLSRFRHPNIVDFAGYCAESGFYC 285
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTgkIVAIKKVKiIEISNDVTKDRQlvgmcgihfTTLRELKIMNEIKHENIMGLVDVYVEGDFIN 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 286 LVYGFLpNGSLEDQLHLQTQacspLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfs 365
Cdd:PTZ00024  97 LVMDIM-ASDLKKVVDRKIR----LTESQVKCILLQILNGLNVLH--KWYFMHRDLSPANIFINSKGICKIADFGLAR-- 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189011594 366 RFagANPSQSSTVARTCTVRGTLAYL----------PEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:PTZ00024 168 RY--GYPPYSDTLSKDETMQRREEMTskvvtlwyraPELLMGAEKYHFAVDMWSVGCIFAELLTGK 231
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
218-420 2.21e-06

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 50.40  E-value: 2.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRA---------VMRNTTYAVKRLKEEA---DLewtvvkQSFLTEVEQLSRF-RHPNIVDFAGYCAESGFY 284
Cdd:cd05100   20 LGEGCFGQVVMAeaigidkdkPNKPVTVAVKMLKDDAtdkDL------SDLVSEMEMMKMIgKHKNIINLLGACTQDGPL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 285 CLVYGFLPNGSLEDQLHLQT--------QAC----SPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERL 352
Cdd:cd05100   94 YVLVEYASKGNLREYLRARRppgmdysfDTCklpeEQLTFKDLVSCAYQVARGMEYLA--SQKCIHRDLAARNVLVTEDN 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 353 MPKLGDFGLARfsrfagaNPSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILE--TLAG 420
Cdd:cd05100  172 VMKIADFGLAR-------DVHNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEifTLGG 234
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
217-421 2.38e-06

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: 50.01  E-value: 2.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVY--RAVMRNTTYAVK--RLKEEADLEWTVVKqsfltEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLp 292
Cdd:cd07871   12 KLGEGTYATVFkgRSKLTENLVALKeiRLEHEEGAPCTAIR-----EVSLLKNLKHANIVTLHDIIHTERCLTLVFEYL- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 ngslEDQLHLQTQACSPLSWPQRLDILL-GTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfAGAN 371
Cdd:cd07871   86 ----DSDLKQYLDNCGNLMSMHNVKIFMfQLLRGLSYCHKRK--ILHRDLKPQNLLINEKGELKLADFGLAR----AKSV 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 189011594 372 PSQ--SSTVArtctvrgTLAYLPEE-YIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd07871  156 PTKtySNEVV-------TLWYRPPDvLLGSTEYSTPIDMWGVGCILYEMATGR 201
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
217-463 2.45e-06

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: 49.99  E-value: 2.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVY--RAVMRNTTYAVK--RLKEEADLEWTVVKqsfltEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLp 292
Cdd:cd07872   13 KLGEGTYATVFkgRSKLTENLVALKeiRLEHEEGAPCTAIR-----EVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYL- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 ngslEDQLHLQTQACSPLSWPQRLDILL-GTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfAGAN 371
Cdd:cd07872   87 ----DKDLKQYMDDCGNIMSMHNVKIFLyQILRGLAYCHRRK--VLHRDLKPQNLLINERGELKLADFGLAR----AKSV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 372 PSQSSTVARTctvrgTLAYLPEE-YIKTGRLAVDTDTFSFGVVILETLAGqravrtqgaKTKYLKDLIEDEAEEVGVTLK 450
Cdd:cd07872  157 PTKTYSNEVV-----TLWYRPPDvLLGSSEYSTQIDMWGVGCIFFEMASG---------RPLFPGSTVEDELHLIFRLLG 222
                        250
                 ....*....|...
gi 189011594 451 STQPTLWMGVATD 463
Cdd:cd07872  223 TPTEETWPGISSN 235
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
212-420 2.61e-06

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: 49.82  E-value: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELRIGEGGFGCVYRAVMRNTT--YAVKRLKEEADlewtvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYG 289
Cdd:cd14085    5 FEIESELGRGATSVVYRCRQKGTQkpYAVKKLKKTVD------KKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLEDQLHLQTQACSPLSWPQRLDILlgtaRAIQFLHQDspSLIHGDIKSSNVLL-----DERLmpKLGDFGLARF 364
Cdd:cd14085   79 LVTGGELFDRIVEKGYYSERDAADAVKQIL----EAVAYLHEN--GIVHRDLKPENLLYatpapDAPL--KIADFGLSKI 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 189011594 365 SrfaganPSQSSTVartcTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd14085  151 V------DQQVTMK----TVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCG 196
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
218-528 2.77e-06

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: 49.66  E-value: 2.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLkeeadlEWTVVKQS-----FLTEVEQLSRFRHPNIVDFAgYCAES-GFYCLVYG 289
Cdd:cd05605    8 LGKGGFGEVCACQVRATgkMYACKKL------EKKRIKKRkgeamALNEKQILEKVNSRFVVSLA-YAYETkDALCLVLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLedQLHLQTQACSPLSwPQRL-----DILLGtaraIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLArf 364
Cdd:cd05605   81 IMNGGDL--KFHIYNMGNPGFE-EERAvfyaaEITCG----LEHLHSER--IVYRDLKPENILLDDHGHVRISDLGLA-- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 365 srfaganpsqsSTVARTCTVR---GTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAKTKYlkdliede 441
Cdd:cd05605  150 -----------VEIPEGETIRgrvGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKR-------- 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 442 aEEVGVTLKSTQPTLwmgvatDAWTAPIAAQIYKKHLDSRPGpcppqlglalAQLACCCMHRRAKKRPPMTQV--YKRLE 519
Cdd:cd05605  211 -EEVDRRVKEDQEEY------SEKFSEEAKSICSQLLQKDPK----------TRLGCRGEGAEDVKSHPFFKSinFKRLE 273

                 ....*....
gi 189011594 520 GLQAVPPWK 528
Cdd:cd05605  274 AGLLEPPFV 282
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
218-363 2.81e-06

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: 49.88  E-value: 2.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT--YAVKRLKEEADLEWTVVKQsFLTEVEQLSRFRHPNIVDFAgYCAESGFYC-LVYGFLPNG 294
Cdd:cd05610   12 ISRGAFGKVYLGRKKNNSklYAVKVVKKADMINKNMVHQ-VQAERDALALSKSPFIVHLY-YSLQSANNVyLVMEYLIGG 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 295 SLEDQLHLQTQACSPLSwpqrLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLAR 363
Cdd:cd05610   90 DVKSLLHIYGYFDEEMA----VKYISEVALALDYLHRHG--IIHRDLKPDNMLISNEGHIKLTDFGLSK 152
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
218-439 2.99e-06

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


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 49.19  E-value: 2.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAV--MRNT--TYAVKRLKEEADLEwtVVKQSFLTEVEQLSRFRHPNIVDFAGYC-AESgfYCLVYGFLP 292
Cdd:cd05116    3 LGSGNFGTVKKGYyqMKKVvkTVAVKILKNEANDP--ALKDELLREANVMQQLDNPYIVRMIGICeAES--WMLVMEMAE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NGSLEDQLhlqtQACSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFSRfAGANP 372
Cdd:cd05116   79 LGPLNKFL----QKNRHVTEKNITELVHQVSMGMKYLEESN--FVHRDLAARNVLLVTQHYAKISDFGLSKALR-ADENY 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594 373 SQSSTvartcTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLA-GQRAVRtqGAKTKYLKDLIE 439
Cdd:cd05116  152 YKAQT-----HGKWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYK--GMKGNEVTQMIE 212
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
204-421 3.03e-06

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (IGF-1 or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 49.65  E-value: 3.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 204 EISQGTCNFSEELriGEGGFGCVYRAVMR-------NTTYAVKRLKEEADLEWTVvkqSFLTEVEQLSRFRHPNIVDFAG 276
Cdd:cd05062    2 EVAREKITMSREL--GQGSFGMVYEGIAKgvvkdepETRVAIKTVNEAASMRERI---EFLNEASVMKEFNCHHVVRLLG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 277 YCAESGFYCLVYGFLPNGSLEDQLH--LQTQACSPLSWPQRLDILLGTARAIQ--FLHQDSPSLIHGDIKSSNVLLDERL 352
Cdd:cd05062   77 VVSQGQPTLVIMELMTRGDLKSYLRslRPEMENNPVQAPPSLKKMIQMAGEIAdgMAYLNANKFVHRDLAARNCMVAEDF 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189011594 353 MPKLGDFGLARfsrfagaNPSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILE--TLAGQ 421
Cdd:cd05062  157 TVKIGDFGMTR-------DIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEiaTLAEQ 220
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
218-486 3.07e-06

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: 49.61  E-value: 3.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLkEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd05631    8 LGKGGFGEVCACQVRATgkMYACKKL-EKKRIKKRKGEAMALNEKRILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LedQLHLQTQACSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLArfsrfaganpsqs 375
Cdd:cd05631   87 L--KFHIYNMGNPGFDEQRAIFYAAELCCGLEDLQRER--IVYRDLKPENILLDDRGHIRISDLGLA------------- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 376 STVARTCTVR---GTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAKTKY-------------LKDLIE 439
Cdd:cd05631  150 VQIPEGETVRgrvGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKReevdrrvkedqeeYSEKFS 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 189011594 440 DEAEEVGVTLKSTQPTLWMGV----ATDAWTAPIAAQIYKKHLDS---RPGPCP 486
Cdd:cd05631  230 EDAKSICRMLLTKNPKERLGCrgngAAGVKQHPIFKNINFKRLEAnmlEPPFCP 283
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
211-364 3.24e-06

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 49.38  E-value: 3.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 211 NFSEELRIGEGGFGCVYRAV-MR-NTTYAVKrlkeeadLEWTVVKQSFLT-EVEQLSRFRH----PNIVDFAgycAESGF 283
Cdd:cd14016    1 RYKLVKKIGSGSFGEVYLGIdLKtGEEVAIK-------IEKKDSKHPQLEyEAKVYKLLQGgpgiPRLYWFG---QEGDY 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 284 YCLVYGFLpnG-SLEDQLhlqtQACSP-LSW-------PQRLDIllgtaraIQFLHqdSPSLIHGDIKSSNVLLDERLMP 354
Cdd:cd14016   71 NVMVMDLL--GpSLEDLF----NKCGRkFSLktvlmlaDQMISR-------LEYLH--SKGYIHRDIKPENFLMGLGKNS 135
                        170
                 ....*....|...
gi 189011594 355 K---LGDFGLARF 364
Cdd:cd14016  136 NkvyLIDFGLAKK 148
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
218-414 3.46e-06

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 49.48  E-value: 3.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEWTVVKQSF--LTEVEQlsrfRHPNIVDFAGYCAESGfycLVYGFLPN 293
Cdd:cd13977    8 VGRGSYGVVYEAVVRRTgaRVAVKKIRCNAPENVELALREFwaLSSIQR----QHPNVIQLEECVLQRD---GLAQRMSH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 294 GSLEDQLHLQT-----------QACSPLS-W-------------------PQR---LDILLGTARAIQFLHQDSpsLIHG 339
Cdd:cd13977   81 GSSKSDLYLLLvetslkgercfDPRSACYlWfvmefcdggdmneyllsrrPDRqtnTSFMLQLSSALAFLHRNQ--IVHR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 340 DIKSSNVLLDERL---MPKLGDFGLARFSRFAGANPSQSSTV--ARTCTVRGTLAYLPEEyIKTGRLAVDTDTFSFGVVI 414
Cdd:cd13977  159 DLKPDNILISHKRgepILKVADFGLSKVCSGSGLNPEEPANVnkHFLSSACGSDFYMAPE-VWEGHYTAKADIFALGIII 237
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
218-419 3.81e-06

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 49.62  E-value: 3.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRA----VMRNTTY---AVKRLKEEADL-EWtvvkQSFLTEVEQLSRF-RHPNIVDFAGYCAESGF----- 283
Cdd:cd14207   15 LGRGAFGKVVQAsafgIKKSPTCrvvAVKMLKEGATAsEY----KALMTELKILIHIgHHLNVVNLLGACTKSGGplmvi 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 284 --YClVYG------------FLPN--GSLEDQLHLQTQACSPL-SWPQRLDILLGT------------------------ 322
Cdd:cd14207   91 veYC-KYGnlsnylkskrdfFVTNkdTSLQEELIKEKKEAEPTgGKKKRLESVTSSesfassgfqedkslsdveeeeeds 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 323 --------------------ARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfagaNPSQSSTVARTC 382
Cdd:cd14207  170 gdfykrpltmedlisysfqvARGMEFL--SSRKCIHRDLAARNILLSENNVVKICDFGLAR-------DIYKNPDYVRKG 240
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 189011594 383 TVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLA 419
Cdd:cd14207  241 DARLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFS 277
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
218-420 3.97e-06

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


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 48.86  E-value: 3.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEE--ADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPN 293
Cdd:cd14194   13 LGSGQFAVVKKCREKSTglQYAAKFIKKRrtKSSRRGVSREDIEREVSILKEIQHPNVITLHEVYENKTDVILILELVAG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 294 GSLEDQLHLQtqacSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMP----KLGDFGLARfsRFAG 369
Cdd:cd14194   93 GELFDFLAEK----ESLTEEEATEFLKQILNGVYYLH--SLQIAHFDLKPENIMLLDRNVPkpriKIIDFGLAH--KIDF 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 189011594 370 ANPSQSstvartctVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd14194  165 GNEFKN--------IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSG 207
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
218-367 4.51e-06

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 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: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 48.71  E-value: 4.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRA-VMRNTTYA---VKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPN 293
Cdd:cd05086    5 IGNGWFGKVLLGeIYTGTSVArvvVKELKASANPK---EQDDFLQQGEPYYILQHPNILQCVGQCVEAIPYLLVFEFCDL 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 294 GSLE-----DQLHLQTQACSPLSwpQRLDILLGTARAIQFLHqdspSLIHGDIKSSNVLLDERLMPKLGDFGLArFSRF 367
Cdd:cd05086   82 GDLKtylanQQEKLRGDSQIMLL--QRMACEIAAGLAHMHKH----NFLHSDLALRNCYLTSDLTVKVGDYGIG-FSRY 153
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
218-413 5.00e-06

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: 48.38  E-value: 5.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVK--RLKEEADlewtvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPN 293
Cdd:cd14103    1 LGRGKFGTVYRCVEKATgkELAAKfiKCRKAKD------REDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 294 GSL-----EDQLHLQTQACSpLSWPQRLDillgtarAIQFLHQDspSLIHGDIKSSNVLLDERL--MPKLGDFGLARFsr 366
Cdd:cd14103   75 GELfervvDDDFELTERDCI-LFMRQICE-------GVQYMHKQ--GILHLDLKPENILCVSRTgnQIKIIDFGLARK-- 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 189011594 367 fagANPSQSSTVArtctvRGTLAYLPEEYIKTGRLAVDTDTFSFGVV 413
Cdd:cd14103  143 ---YDPDKKLKVL-----FGTPEFVAPEVVNYEPISYATDMWSVGVI 181
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
218-420 6.39e-06

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: 48.49  E-value: 6.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT--YAVKRLKEEAdLEWTvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd14167   11 LGTGAFSEVVLAEEKRTQklVAIKCIAKKA-LEGK--ETSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQL---HLQTQACSPLSWPQRLDillgtarAIQFLHqdSPSLIHGDIKSSNVL---LDERLMPKLGDFGLARFSrfag 369
Cdd:cd14167   88 LFDRIvekGFYTERDASKLIFQILD-------AVKYLH--DMGIVHRDLKPENLLyysLDEDSKIMISDFGLSKIE---- 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 189011594 370 anpSQSSTVARTCtvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd14167  155 ---GSGSVMSTAC---GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCG 199
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
218-438 6.75e-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: 48.42  E-value: 6.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMR--NTTYAVKRLKE----------------------EADLEWTVVKQSFLTEVEQLSRFRHPNIVD 273
Cdd:cd14199   10 IGKGSYGVVKLAYNEddNTYYAMKVLSKkklmrqagfprrppprgaraapEGCTQPRGPIERVYQEIAILKKLDHPNVVK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 274 FAGYC---AESGFYcLVYGFLPNGSLedqlhLQTQACSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDE 350
Cdd:cd14199   90 LVEVLddpSEDHLY-MVFELVKQGPV-----MEVPTLKPLSEDQARFYFQDLIKGIEYLHYQK--IIHRDVKPSNLLVGE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 351 RLMPKLGDFGLArfSRFAGANPSQSSTVartctvrGTLAYLPEEYIKTGR------------LAVDTDTFSFGVVIL--- 415
Cdd:cd14199  162 DGHIKIADFGVS--NEFEGSDALLTNTV-------GTPAFMAPETLSETRkifsgkaldvwaMGVTLYCFVFGQCPFmde 232
                        250       260       270
                 ....*....|....*....|....*....|
gi 189011594 416 ETLAGQRAVRTQGAK-------TKYLKDLI 438
Cdd:cd14199  233 RILSLHSKIKTQPLEfpdqpdiSDDLKDLL 262
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
204-421 8.05e-06

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: 48.48  E-value: 8.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 204 EISQ--GTCNFSEELRIGEGGFGCVY--RAVMRNTTYAVKRLKEE-----ADLEWTVVKQSFLtevEQLSRfrHPNIVDF 274
Cdd:cd05617    7 KISQglGLQDFDLIRVIGRGSYAKVLlvRLKKNDQIYAMKVVKKElvhddEDIDWVQTEKHVF---EQASS--NPFLVGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 275 -AGYCAESGFYcLVYGFLPNGSLedQLHLQTQACSPLSWPQ--RLDILLgtarAIQFLHQDSpsLIHGDIKSSNVLLDER 351
Cdd:cd05617   82 hSCFQTTSRLF-LVIEYVNGGDL--MFHMQRQRKLPEEHARfyAAEICI----ALNFLHERG--IIYRDLKLDNVLLDAD 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 352 LMPKLGDFGLARfsrfAGANPSQSstvarTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd05617  153 GHIKLTDYGMCK----EGLGPGDT-----TSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGR 213
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
218-414 8.15e-06

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: 47.85  E-value: 8.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMR--NTTYAVK---RLKEEADlewtVVKQSFLTEVEQLSRFRHPNIVD-FAGYCAESGFYCLVYGFL 291
Cdd:cd14165    9 LGEGSYAKVKSAYSErlKCNVAIKiidKKKAPDD----FVEKFLPRELEILARLNHKSIIKtYEIFETSDGKVYIVMELG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 PNGSLEDqlHLQTQACSPLSWPQRLDILLgtARAIQFLHQdsPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfaGAN 371
Cdd:cd14165   85 VQGDLLE--FIKLRGALPEDVARKMFHQL--SSAIKYCHE--LDIVHRDLKCENLLLDKDFNIKLTDFGFSK-----RCL 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 189011594 372 PSQSSTVARTCTVRGTLAYLPEEYIKTgrLAVD---TDTFSFGVVI 414
Cdd:cd14165  154 RDENGRIVLSKTFCGSAAYAAPEVLQG--IPYDpriYDIWSLGVIL 197
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
211-430 9.72e-06

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


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 48.13  E-value: 9.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 211 NFSEELRIGEGGFGCVYRAVMRNTTYAVKRLKEEADLEwTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGF 290
Cdd:cd06650    6 DFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIK-PAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDQLHLQTQAcsplswPQRL--DILLGTARAIQFLhQDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFA 368
Cdd:cd06650   85 MDGGSLDQVLKKAGRI------PEQIlgKVSIAVIKGLTYL-REKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDS 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189011594 369 GANpsqsstvartcTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAK 430
Cdd:cd06650  158 MAN-----------SFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAK 208
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
212-420 1.06e-05

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: 47.69  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELRIGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEwtvvKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYG 289
Cdd:cd14191    4 YDIEERLGSGKFGQVFRLVEKKTkkVWAGKFFKAYSAKE----KENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLEDQL-----HLQTQACsplswpqrLDILLGTARAIQFLHQDspSLIHGDIKSSNVLLDERLMP--KLGDFGLA 362
Cdd:cd14191   80 MVSGGELFERIidedfELTEREC--------IKYMRQISEGVEYIHKQ--GIVHLDLKPENIMCVNKTGTkiKLIDFGLA 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594 363 RFSRFAGAnpsqsstvarTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd14191  150 RRLENAGS----------LKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSG 197
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
217-363 1.06e-05

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: 48.08  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVY--RAVMRNTTYAVK--RLKEEADLEWTVVKqsfltEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLp 292
Cdd:cd07873    9 KLGEGTYATVYkgRSKLTDNLVALKeiRLEHEEGAPCTAIR-----EVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYL- 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189011594 293 ngslEDQLHLQTQACSPLSWPQRLDILL-GTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLAR 363
Cdd:cd07873   83 ----DKDLKQYLDDCGNSINMHNVKLFLfQLLRGLAYCHRRK--VLHRDLKPQNLLINERGELKLADFGLAR 148
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
218-464 1.11e-05

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: 48.11  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT--YAVK----RLKEEADLEWTVVKqsfLTEveqlsrfRHPNIVDFAGYCAESGFYCLVYGFL 291
Cdd:cd14179   15 LGEGSFSICRKCLHKKTNqeYAVKivskRMEANTQREIAALK---LCE-------GHPNIVKLHEVYHDQLHTFLVMELL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 PNGSLEDQLHLQTQacspLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLL---DERLMPKLGDFGLARFsrfa 368
Cdd:cd14179   85 KGGELLERIKKKQH----FSETEASHIMRKLVSAVSHMH--DVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFARL---- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 369 gaNPSQSSTVARTCTvrgTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGaktkylKDLIEDEAEEVGVT 448
Cdd:cd14179  155 --KPPDNQPLKTPCF---TLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHD------KSLTCTSAEEIMKK 223
                        250       260
                 ....*....|....*....|
gi 189011594 449 LK----STQPTLWMGVATDA 464
Cdd:cd14179  224 IKqgdfSFEGEAWKNVSQEA 243
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
214-420 1.18e-05

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: 47.69  E-value: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 214 EELriGEGGFGCVYRAVMRNT--TYAVKRLKEE--ADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYG 289
Cdd:cd14195   11 EEL--GSGQFAIVRKCREKGTgkEYAAKFIKKRrlSSSRRGVSREEIEREVNILREIQHPNIITLHDIFENKTDVVLILE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLEDQLhLQTQACSPLSWPQRLDILLGtarAIQFLHqdSPSLIHGDIKSSNVLLDERLMP----KLGDFGLARfs 365
Cdd:cd14195   89 LVSGGELFDFL-AEKESLTEEEATQFLKQILD---GVHYLH--SKRIAHFDLKPENIMLLDKNVPnpriKLIDFGIAH-- 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 366 RFAGANPSQSstvartctVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd14195  161 KIEAGNEFKN--------IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSG 207
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
218-421 1.21e-05

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: 48.08  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCV--YRAVMRNTTYAVKRLKEEADLEWTVVKQSfLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd05595    3 LGKGTFGKVilVREKATGRYYAMKILRKEVIIAKDEVAHT-VTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LedQLHLQTQACsplsWPQRLDILLGT--ARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfagANPS 373
Cdd:cd05595   82 L--FFHLSRERV----FTEDRARFYGAeiVSALEYLH--SRDVVYRDIKLENLMLDKDGHIKITDFGLCK------EGIT 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 189011594 374 QSSTVARTCtvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd05595  148 DGATMKTFC---GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGR 192
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
325-430 1.28e-05

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: 47.39  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 325 AIQFLHQdsPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsRFAganpsqSSTVARTCTVRGTLAYLPEEYIKTGRLAVD 404
Cdd:cd05583  111 ALEHLHK--LGIIYRDIKLENILLDSEGHVVLTDFGLSK--EFL------PGENDRAYSFCGTIEYMAPEVVRGGSDGHD 180
                         90       100
                 ....*....|....*....|....*...
gi 189011594 405 --TDTFSFGVVILETLAGQRAVRTQGAK 430
Cdd:cd05583  181 kaVDWWSLGVLTYELLTGASPFTVDGER 208
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
217-416 1.30e-05

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 47.74  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVkqsflTEVEQLSRFRHPNIV-----DFAGYCAESGFYcLVYGFL 291
Cdd:cd14219   12 QIGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRE-----TEIYQTVLMRHENILgfiaaDIKGTGSWTQLY-LITDYH 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 PNGSLEDQLHlqtqaCSPLSWPQRLDILLGTARAIQFLH------QDSPSLIHGDIKSSNVLLDERLMPKLGDFGLArfS 365
Cdd:cd14219   86 ENGSLYDYLK-----STTLDTKAMLKLAYSSVSGLCHLHteifstQGKPAIAHRDLKSKNILVKKNGTCCIADLGLA--V 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594 366 RFAganpSQSSTVARTCTVR-GTLAYLPEEYIKTG------RLAVDTDTFSFGVVILE 416
Cdd:cd14219  159 KFI----SDTNEVDIPPNTRvGTKRYMPPEVLDESlnrnhfQSYIMADMYSFGLILWE 212
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
209-421 1.32e-05

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: 47.95  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 209 TCNFSEELRIGEGGFG--CVYRAVMRNTTYAVKRLKEEadLEWTVVKQSFLTEVEQLSRFRHPNIVdfagycaesgfyCL 286
Cdd:cd07856    9 TTRYSDLQPVGMGAFGlvCSARDQLTGQNVAVKKIMKP--FSTPVLAKRTYRELKLLKHLRHENII------------SL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 287 VYGFLpnGSLED----------QLHLQTQAcSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKL 356
Cdd:cd07856   75 SDIFI--SPLEDiyfvtellgtDLHRLLTS-RPLEKQFIQYFLYQILRGLKYVH--SAGVIHRDLKPSNILVNENCDLKI 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 357 GDFGLARFsrfaganpsQSSTVARTCTVRGTLAylPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd07856  150 CDFGLARI---------QDPQMTGYVSTRYYRA--PEIMLTWQKYDVEVDIWSAGCIFAEMLEGK 203
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
218-420 1.36e-05

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: 48.07  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCV--YRAVMRNTTYAVKRLKEeadleWTVVKQS----FLTEVEQLSRFRHPNIVD-FAGYCAESGFYcLVYGF 290
Cdd:cd05621   60 IGRGAFGEVqlVRHKASQKVYAMKLLSK-----FEMIKRSdsafFWEERDIMAFANSPWVVQlFCAFQDDKYLY-MVMEY 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGsleDQLHLQTQACSPLSWPQ--RLDILLgtarAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfa 368
Cdd:cd05621  134 MPGG---DLVNLMSNYDVPEKWAKfyTAEVVL----ALDAIH--SMGLIHRDVKPDNMLLDKYGHLKLADFGTCM----- 199
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 189011594 369 ganPSQSSTVARTCTVRGTLAYLPEEYIKT----GRLAVDTDTFSFGVVILETLAG 420
Cdd:cd05621  200 ---KMDETGMVHCDTAVGTPDYISPEVLKSqggdGYYGRECDWWSVGVFLFEMLVG 252
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
218-478 1.44e-05

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: 47.57  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTT--YAVKRLKEEADLEWTVVKQSfLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd05585    2 IGKGSFGKVMQVRKKDTSriYALKTIRKAHIVSRSEVTHT-LAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDqlHLQTQACSPLSWPQ--RLDILLgtarAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFsrfagaNPS 373
Cdd:cd05585   81 LFH--HLQREGRFDLSRARfyTAELLC----ALECLH--KFNVIYRDLKPENILLDYTGHIALCDFGLCKL------NMK 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 374 QSStvaRTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAKTKYLK---------DLIEDEAEE 444
Cdd:cd05585  147 DDD---KTNTFCGTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKilqeplrfpDGFDRDAKD 223
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 189011594 445 VGVTLKSTQPTLWMGV--ATDAWTAPIAAQIYKKHL 478
Cdd:cd05585  224 LLIGLLNRDPTKRLGYngAQEIKNHPFFDQIDWKRL 259
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
217-460 1.55e-05

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: 47.38  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNT----TYAVKRLKEEADLEWTVVKQSFLteveqLSRFRHPNIVDFAGYCAESGFYCLVYGFL- 291
Cdd:cd07869   12 KLGEGSYATVYKGKSKVNgklvALKVIRLQEEEGTPFTAIREASL-----LKGLKHANIVLLHDIIHTKETLTLVFEYVh 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 ----------PNGSLEDQLHLqtqacsplswpqrldILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGL 361
Cdd:cd07869   87 tdlcqymdkhPGGLHPENVKL---------------FLFQLLRGLSYIHQRY--ILHRDLKPQNLLISDTGELKLADFGL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 362 ARfsrfAGANPSQSSTVARTctvrgTLAYLPEE-YIKTGRLAVDTDTFSFGVVILETLAGQRAVRTqgaktkyLKDlIED 440
Cdd:cd07869  150 AR----AKSVPSHTYSNEVV-----TLWYRPPDvLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPG-------MKD-IQD 212
                        250       260
                 ....*....|....*....|
gi 189011594 441 EAEEVGVTLKSTQPTLWMGV 460
Cdd:cd07869  213 QLERIFLVLGTPNEDTWPGV 232
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
218-435 1.68e-05

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: 47.75  E-value: 1.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVyRAVMRNTTYAVKRLKeeadlewtVVKQSFLTEVEQLSRFRHPN--IVDFAGYCAESGFYC--------LV 287
Cdd:cd05627   10 IGRGAFGEV-RLVQKKDTGHIYAMK--------ILRKADMLEKEQVAHIRAERdiLVEADGAWVVKMFYSfqdkrnlyLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 288 YGFLPNGSLEDQLHLQtqacSPLSWPQRLDILLGTARAIQFLHQdsPSLIHGDIKSSNVLLDERLMPKLGDFGL------ 361
Cdd:cd05627   81 MEFLPGGDMMTLLMKK----DTLSEEATQFYIAETVLAIDAIHQ--LGFIHRDIKPDNLLLDAKGHVKLSDFGLctglkk 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 362 ---ARFSRFAGANPSQSSTVARTCTVR-----------------GTLAYL-PEEYIKTGRLAVdTDTFSFGVVILETLAG 420
Cdd:cd05627  155 ahrTEFYRNLTHNPPSDFSFQNMNSKRkaetwkknrrqlaystvGTPDYIaPEVFMQTGYNKL-CDWWSLGVIMYEMLIG 233
                        250
                 ....*....|....*
gi 189011594 421 QRAVRTQGAKTKYLK 435
Cdd:cd05627  234 YPPFCSETPQETYRK 248
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
218-445 1.90e-05

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 47.36  E-value: 1.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQS-----FLTEVEQLSRFRHPNIVDFAGYCA-ESGFYCLVYGFL 291
Cdd:cd14041   14 LGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKEnyhkhACREYRIHKELDHPRIVKLYDYFSlDTDSFCTVLEYC 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 PNGSLEdqLHLQTQACspLSWPQRLDILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLM---PKLGDFGLARFsrFA 368
Cdd:cd14041   94 EGNDLD--FYLKQHKL--MSEKEARSIIMQIVNALKYLNEIKPPIIHYDLKPGNILLVNGTAcgeIKITDFGLSKI--MD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 369 GANPSQSSTVARTCTVRGTLAYLPEEYIKTG----RLAVDTDTFSFGVVILETLAGQRAVRTQGAKTKYLKDLIEDEAEE 444
Cdd:cd14041  168 DDSYNSVDGMELTSQGAGTYWYLPPECFVVGkeppKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQENTILKATE 247

                 .
gi 189011594 445 V 445
Cdd:cd14041  248 V 248
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
215-364 2.63e-05

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: 46.23  E-value: 2.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 215 ELRIGEGGFGCVYRAVMRNTTYAVK-RLKEEADLEWTVVKQSFlTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPN 293
Cdd:cd14071    5 ERTIGKGNFAVVKLARHRITKTEVAiKIIDKSQLDEENLKKIY-REVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYASN 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189011594 294 GSLEDQLHLQTQACSPLSWPQRLDILLgtarAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARF 364
Cdd:cd14071   84 GEIFDYLAQHGRMSEKEARKKFWQILS----AVEYCHKRH--IVHRDLKAENLLLDANMNIKIADFGFSNF 148
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
214-440 3.21e-05

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


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 46.26  E-value: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 214 EELriGEGGFGCVYRavMRN----TTYAVKRLKeeADLEWTVVKQsFLTEVEQLSRFRH-PNIVDFAG---------YCA 279
Cdd:cd06617    7 EEL--GRGAYGVVDK--MRHvptgTIMAVKRIR--ATVNSQEQKR-LLMDLDISMRSVDcPYTVTFYGalfregdvwICM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 280 ESGFYCLvYGFLPNgSLEDQLHLQTQACSplswpqrlDILLGTARAIQFLHQDSpSLIHGDIKSSNVLLDERLMPKLGDF 359
Cdd:cd06617   80 EVMDTSL-DKFYKK-VYDKGLTIPEDILG--------KIAVSIVKALEYLHSKL-SVIHRDVKPSNVLINRNGQVKLCDF 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 360 GLARFsrfaganpsQSSTVARTCTVrGTLAYLPEEYIKTGRLA----VDTDTFSFGVVILETLAGQRAVRTQGAKTKYLK 435
Cdd:cd06617  149 GISGY---------LVDSVAKTIDA-GCKPYMAPERINPELNQkgydVKSDVWSLGITMIELATGRFPYDSWKTPFQQLK 218

                 ....*
gi 189011594 436 DLIED 440
Cdd:cd06617  219 QVVEE 223
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
259-400 3.26e-05

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: 46.48  E-value: 3.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 259 EVEQLSRFRHPNIVDFAGYC---AESGFYcLVYGFLPNGSLedqlhLQTQACSPLSWPQ-RL---DILLGtaraIQFLHQ 331
Cdd:cd14200   73 EIAILKKLDHVNIVKLIEVLddpAEDNLY-MVFDLLRKGPV-----MEVPSDKPFSEDQaRLyfrDIVLG----IEYLHY 142
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 332 DSpsLIHGDIKSSNVLLDERLMPKLGDFGLArfSRFAGANPSQSSTVartctvrGTLAYL-PEEYIKTGR 400
Cdd:cd14200  143 QK--IVHRDIKPSNLLLGDDGHVKIADFGVS--NQFEGNDALLSSTA-------GTPAFMaPETLSDSGQ 201
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
259-417 3.46e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 46.81  E-value: 3.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 259 EVEQLSRFRHPNIVDFAGYCAESGFYCLVygfLPNGSLEDQLHLQTQAcSPLSWPQRLDILLGTARAIQFLHQDSpsLIH 338
Cdd:PHA03211 210 EARLLRRLSHPAVLALLDVRVVGGLTCLV---LPKYRSDLYTYLGARL-RPLGLAQVTAVARQLLSAIDYIHGEG--IIH 283
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 339 GDIKSSNVLLDERLMPKLGDFGLARFSRFAGANPSQSStvartctVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILET 417
Cdd:PHA03211 284 RDIKTENVLVNGPEDICLGDFGAACFARGSWSTPFHYG-------IAGTVDTNAPEVLAGDPYTPSVDIWSAGLVIFEA 355
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
218-420 3.71e-05

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: 46.09  E-value: 3.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEeadleWTVVKQSFLTEVEQ----LSRFRHPNIVDFAGYCAESGFYCLVYGFL 291
Cdd:cd14081    9 LGKGQTGLVKLAKHCVTgqKVAIKIVNK-----EKLSKESVLMKVEReiaiMKLIEHPNVLKLYDVYENKKYLYLVLEYV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 PNGSLEDQLhlqtQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFsrfagan 371
Cdd:cd14081   84 SGGELFDYL----VKKGRLTEKEARKFFRQIISALDYCH--SHSICHRDLKPENLLLDEKNNIKIADFGMASL------- 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 189011594 372 pSQSSTVART-CtvrGTLAYLPEEYIK----TGRLAvdtDTFSFGVVILETLAG 420
Cdd:cd14081  151 -QPEGSLLETsC---GSPHYACPEVIKgekyDGRKA---DIWSCGVILYALLVG 197
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
325-421 3.76e-05

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: 46.53  E-value: 3.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 325 AIQFLHQdsPSLIHGDIKSSNVLLDERLMPKLGDFGLArfsrfagANPSQSSTVARTCTVrGTLAYL-PE-----EYIKT 398
Cdd:cd05601  114 AIHSLHS--MGYVHRDIKPENILIDRTGHIKLADFGSA-------AKLSSDKTVTSKMPV-GTPDYIaPEvltsmNGGSK 183
                         90       100
                 ....*....|....*....|...
gi 189011594 399 GRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd05601  184 GTYGVECDWWSLGIVAYEMLYGK 206
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
214-420 4.03e-05

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: 45.94  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 214 EELriGEGGFGCVYRAVMRNT--TYAVKRLKEE--ADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYG 289
Cdd:cd14105   11 EEL--GSGQFAVVKKCREKSTglEYAAKFIKKRrsKASRRGVSREDIEREVSILRQVLHPNIITLHDVFENKTDVVLILE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLEDqlHLQTQACspLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMP----KLGDFGLARFS 365
Cdd:cd14105   89 LVAGGELFD--FLAEKES--LSEEEATEFLKQILDGVNYLH--TKNIAHFDLKPENIMLLDKNVPipriKLIDFGLAHKI 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 366 RFAGANPSqsstvartctVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd14105  163 EDGNEFKN----------IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSG 207
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
218-421 4.06e-05

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


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 46.02  E-value: 4.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRA--VMRNTTYAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGS 295
Cdd:cd06619    9 LGHGNGGTVYKAyhLLTRRILAVKVIPLDITVE---LQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGGS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LEDQLHLQTQACSplswpqrlDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfaganpSQS 375
Cdd:cd06619   86 LDVYRKIPEHVLG--------RIAVAVVKGLTYLW--SLKILHRDVKPSNMLVNTRGQVKLCDFGVST---------QLV 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 189011594 376 STVARTCTvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd06619  147 NSIAKTYV--GTNAYMAPERISGEQYGIHSDVWSLGISFMELALGR 190
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
218-420 4.80e-05

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: 46.15  E-value: 4.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVyRAVMRNTTYAVKRLKEEADLEwtVVKQS---FLTEVEQLSRFRHPNIVDFAGYCAESGFYC-LVYGFLPN 293
Cdd:cd05622   81 IGRGAFGEV-QLVRHKSTRKVYAMKLLSKFE--MIKRSdsaFFWEERDIMAFANSPWVVQLFYAFQDDRYLyMVMEYMPG 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 294 GsleDQLHLQTQACSPLSWPQ--RLDILLgtarAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAGan 371
Cdd:cd05622  158 G---DLVNLMSNYDVPEKWARfyTAEVVL----ALDAIH--SMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEG-- 226
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 189011594 372 psqsstVARTCTVRGTLAYLPEEYIKT----GRLAVDTDTFSFGVVILETLAG 420
Cdd:cd05622  227 ------MVRCDTAVGTPDYISPEVLKSqggdGYYGRECDWWSVGVFLYEMLVG 273
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
249-429 5.19e-05

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


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 45.68  E-value: 5.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 249 WTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLEDQLHLQTQacspLSWPQRLDILLGTARAIQF 328
Cdd:cd14110   39 KPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPELLYNLAERNS----YSEAEVTDYLWQILSAVDY 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 329 LHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFsrfagANPSQSSTVARTCTVRGTLAylPEeyIKTGRLAV-DTDT 407
Cdd:cd14110  115 LH--SRRILHLDLRSENMIITEKNLLKIVDLGNAQP-----FNQGKVLMTDKKGDYVETMA--PE--LLEGQGAGpQTDI 183
                        170       180
                 ....*....|....*....|..
gi 189011594 408 FSFGVVILETLAGQRAVRTQGA 429
Cdd:cd14110  184 WAIGVTAFIMLSADYPVSSDLN 205
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
212-364 5.26e-05

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 45.78  E-value: 5.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELRIGEGGFGCVYRAVMR------NTTYAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYc 285
Cdd:cd05108    9 FKKIKVLGSGAFGTVYKGLWIpegekvKIPVAIKELREATSPK---ANKEILDEAYVMASVDNPHVCRLLGICLTSTVQ- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 286 LVYGFLPNGSLEDQLHL-QTQACSP--LSWPQRLdillgtARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLA 362
Cdd:cd05108   85 LITQLMPFGCLLDYVREhKDNIGSQylLNWCVQI------AKGMNYLEDRR--LVHRDLAARNVLVKTPQHVKITDFGLA 156

                 ..
gi 189011594 363 RF 364
Cdd:cd05108  157 KL 158
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
215-419 6.89e-05

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) 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. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 45.33  E-value: 6.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 215 ELR----IGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQSFlTEVEQ----LSRFRHPNIVDFAGYCAESGFYcL 286
Cdd:cd05111    8 ELRklkvLGSGVFGTVHKGIWIPEGDSIKIPVAIKVIQDRSGRQSF-QAVTDhmlaIGSLDHAYIVRLLGICPGASLQ-L 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 287 VYGFLPNGSLEDQLHLQTQACSP---LSWPQRLdillgtARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLAR 363
Cdd:cd05111   86 VTQLLPLGSLLDHVRQHRGSLGPqllLNWCVQI------AKGMYYLEEHR--MVHRNLAARNVLLKSPSQVQVADFGVAD 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 189011594 364 FsrfagANPSQSSTVARtcTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLA 419
Cdd:cd05111  158 L-----LYPDDKKYFYS--EAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMT 206
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
218-421 7.20e-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: 7.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTY--AVKRL-----KEE-----ADLEwtVVKQSFLTeveqlsrfrhPNIVDFAGY-------- 277
Cdd:cd06618   23 IGSGTCGQVYKMRHKKTGHvmAVKQMrrsgnKEEnkrilMDLD--VVLKSHDC----------PYIVKCYGYfitdsdvf 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 278 -CAESGFYCLvygflpngsleDQLHLQTQacSPLswPQRLdilLG--TARAIQFLH--QDSPSLIHGDIKSSNVLLDERL 352
Cdd:cd06618   91 iCMELMSTCL-----------DKLLKRIQ--GPI--PEDI---LGkmTVSIVKALHylKEKHGVIHRDVKPSNILLDESG 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189011594 353 MPKLGDFGLARFsrfagANPSQSSTVARTCTvrgtlAYLPEEYI---KTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd06618  153 NVKLCDFGISGR-----LVDSKAKTRSAGCA-----AYMAPERIdppDNPKYDIRADVWSLGISLVELATGQ 214
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
214-420 1.06e-04

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: 44.72  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 214 EELriGEGGFGCVYRAVMRNTT--YAVK-------------RLKEEADLewtvvkqsflteveqLSRFRHPNIVDFAGYC 278
Cdd:cd14086    7 EEL--GKGAFSVVRRCVQKSTGqeFAAKiintkklsardhqKLEREARI---------------CRLLKHPNIVRLHDSI 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 279 AESGFYCLVYGFLPNGSLEDQL---HLQTQACSPLSWPQRLDillgtarAIQFLHQDspSLIHGDIKSSNVLLDERLMP- 354
Cdd:cd14086   70 SEEGFHYLVFDLVTGGELFEDIvarEFYSEADASHCIQQILE-------SVNHCHQN--GIVHRDLKPENLLLASKSKGa 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189011594 355 --KLGDFGLArfSRFAGANPSQSStvartctVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd14086  141 avKLADFGLA--IEVQGDQQAWFG-------FAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVG 199
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
212-436 1.08e-04

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: 45.05  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELRIGEGGFGCVY--RAVMRNTTYAVK-----RLKEEADLEWTVVKQSFLTEVeqlSRFRHPNIVdfagyCAESGFY 284
Cdd:cd05633    7 FSVHRIIGRGGFGEVYgcRKADTGKMYAMKcldkkRIKMKQGETLALNERIMLSLV---STGDCPFIV-----CMTYAFH 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 285 -----CLVYGFLPNGSLedQLHLQTQACsplsWPQRLDILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLMPKLGDF 359
Cdd:cd05633   79 tpdklCFILDLMNGGDL--HYHLSQHGV----FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDL 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189011594 360 GLArfSRFAGANPSQSStvartctvrGTLAYLPEEYIKTGRlAVDT--DTFSFGVVILETLAGQRAVRTQGAKTKYLKD 436
Cdd:cd05633  153 GLA--CDFSKKKPHASV---------GTHGYMAPEVLQKGT-AYDSsaDWFSLGCMLFKLLRGHSPFRQHKTKDKHEID 219
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
218-416 1.13e-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: 44.62  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMR--NTTYAVKRLK------EEADLEWTVVKQsfLTEveqlsrfrHPNIVDFAGYcaesgFY----- 284
Cdd:cd06638   26 IGKGTYGKVFKVLNKknGSKAAVKILDpihdidEEIEAEYNILKA--LSD--------HPNVVKFYGM-----YYkkdvk 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 285 -----CLVYGFLPNGSLEDQLHLQTQACSPLSWPQRLDILLGTARAIQFLHQDSPslIHGDIKSSNVLLDERLMPKLGDF 359
Cdd:cd06638   91 ngdqlWLVLELCNGGSVTDLVKGFLKRGERMEEPIIAYILHEALMGLQHLHVNKT--IHRDVKGNNILLTTEGGVKLVDF 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189011594 360 GLArfsrfaganPSQSSTVARTCTVRGTLAYLPEEYIKTGRlAVDT------DTFSFGVVILE 416
Cdd:cd06638  169 GVS---------AQLTSTRLRRNTSVGTPFWMAPEVIACEQ-QLDStydarcDVWSLGITAIE 221
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
215-420 1.15e-04

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


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 44.73  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 215 ELRIGEGGFGCVYRAVMRNTTYAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNG 294
Cdd:cd06615    8 ELGAGNGGVVTKVLHRPSGLIMARKLIHLEIKPA---IRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICMEHMDGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLeDQLhLQTQACSPLSWPQRldILLGTARAIQFLhQDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAGANpsq 374
Cdd:cd06615   85 SL-DQV-LKKAGRIPENILGK--ISIAVLRGLTYL-REKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMAN--- 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 189011594 375 sSTVartctvrGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd06615  157 -SFV-------GTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIG 194
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
217-421 1.31e-04

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: 44.57  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 217 RIGEGGFGCVYRAVMRNTTYAVK----RLKEEADLEWTVVKQSFLteveqLSRFRHPNIVDFAGYCAESGFYCLVYGFLP 292
Cdd:cd07870    7 KLGEGSYATVYKGISRINGQLVAlkviSMKTEEGVPFTAIREASL-----LKGLKHANIVLLHDIIHTKETLTFVFEYMH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 293 NgsleDQLHLQTQACSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfAGANP 372
Cdd:cd07870   82 T----DLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQH--ILHRDLKPQNLLISYLGELKLADFGLAR----AKSIP 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 189011594 373 SQ--SSTVArtctvrgTLAYLPEE-YIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd07870  152 SQtySSEVV-------TLWYRPPDvLLGATDYSSALDIWGAGCIFIEMLQGQ 196
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
212-420 1.73e-04

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: 43.81  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 212 FSEELRIGEGGFGCVYRAVMRNT--TYAVKRLKEEadlewtVVKQSFLT-EVEQLSRFRHPNIVDFAGYCAESGFYCLVY 288
Cdd:cd14113    9 YSEVAELGRGRFSVVKKCDQRGTkrAVATKFVNKK------LMKRDQVThELGVLQSLQHPQLVGLLDTFETPTSYILVL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 289 GFLPNGSLEDQLhlqtqacspLSW----PQRLDILLGTA-RAIQFLHqdSPSLIHGDIKSSNVLLDERLMP---KLGDFG 360
Cdd:cd14113   83 EMADQGRLLDYV---------VRWgnltEEKIRFYLREIlEALQYLH--NCRIAHLDLKPENILVDQSLSKptiKLADFG 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 361 LArfsrfaganpSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd14113  152 DA----------VQLNTTYYIHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSG 201
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
324-363 1.74e-04

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: 44.38  E-value: 1.74e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 189011594 324 RAIQFLHqdSPSLIHGDIKSSNVLLD-ERLMPKLGDFGLAR 363
Cdd:cd07854  125 RGLKYIH--SANVLHRDLKPANVFINtEDLVLKIGDFGLAR 163
PK_MADML cd14035
Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to ...
261-416 1.77e-04

Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. MADML has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. It may play an important role in embryonic eye development. The MADML 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: 270937 [Multi-domain]  Cd Length: 263  Bit Score: 43.76  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 261 EQLSRFRHPNIVDFAGYCAE----SGFYCLVYGFLPNGSLEdQLHLQTQ----ACSPLSWPQRLDILLGtarAIQFLHQD 332
Cdd:cd14035   47 ENLTLVDHPNIVKFHKYWLDvkdnHARVVFITEYVSSGSLK-QFLKKTKknhkTMNARAWKRWCTQILS---ALSYLHSC 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 333 SPSLIHGDIKSSNVLLDERLMPKLGDFgLARFSRFAGANPSQSSTVARTCTVRGTLAYLPEEYiktGRLAVDT--DTFSF 410
Cdd:cd14035  123 EPPIIHGNLTSDTIFIQHNGLIKIGSV-WHRLFVNVLPEGGVRGPLRQEREELRNLHFFPPEY---GSCEDGTavDIFSF 198

                 ....*.
gi 189011594 411 GVVILE 416
Cdd:cd14035  199 GMCALE 204
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
218-421 2.02e-04

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: 44.23  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEeadleWTVVKQSflteveQLSRFRHPNIVDFAGYCA----------ESGFYC 285
Cdd:cd05624   80 IGRGAFGEVAVVKMKNTerIYAMKILNK-----WEMLKRA------ETACFREERNVLVNGDCQwittlhyafqDENYLY 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 286 LVYGFLPNGSL-------EDQLhlqtqacsplswPQRLD--ILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKL 356
Cdd:cd05624  149 LVMDYYVGGDLltllskfEDKL------------PEDMArfYIGEMVLAIHSIHQLH--YVHRDIKPDNVLLDMNGHIRL 214
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 357 GDFGlarfsrfAGANPSQSSTVARTCTVrGTLAYLPEEYIKT-----GRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd05624  215 ADFG-------SCLKMNDDGTVQSSVAV-GTPDYISPEILQAmedgmGKYGPECDWWSLGVCMYEMLYGE 276
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
218-430 2.56e-04

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function 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. The KSR2 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: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 43.46  E-value: 2.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTyAVKRLKEEADLEWTVvkQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLE 297
Cdd:cd14153    8 IGKGRFGQVYHGRWHGEV-AIRLIDIERDNEEQL--KAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 298 DQLHlqtQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMpKLGDFGLARFSRFAGANPSQSst 377
Cdd:cd14153   85 SVVR---DAKVVLDVNKTRQIAQEIVKGMGYLH--AKGILHKDLKSKNVFYDNGKV-VITDFGLFTISGVLQAGRRED-- 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189011594 378 vaRTCTVRGTLAYLPEEYIKtgRLAVDT-----------DTFSFGVVILETLAGQRAVRTQGAK 430
Cdd:cd14153  157 --KLRIQSGWLCHLAPEIIR--QLSPETeedklpfskhsDVFAFGTIWYELHAREWPFKTQPAE 216
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
218-420 2.57e-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: 43.55  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVY--RAVMRNTTYAVKRLKEEADLEwTVVKQsfltEVEQLSRF-RHPNIVDFAGYCAESGfyclvygflPNG 294
Cdd:cd06637   14 VGNGTYGQVYkgRHVKTGQLAAIKVMDVTGDEE-EEIKQ----EINMLKKYsHHRNIATYYGAFIKKN---------PPG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 sLEDQLHLQTQACSPLSWPQRLDILLGTA--------------RAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFG 360
Cdd:cd06637   80 -MDDQLWLVMEFCGAGSVTDLIKNTKGNTlkeewiayicreilRGLSHLHQHK--VIHRDIKGQNVLLTENAEVKLVDFG 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189011594 361 L-ARFSRfaganpsqssTVARTCTVRGTLAYLPEEYIKT-----GRLAVDTDTFSFGVVILETLAG 420
Cdd:cd06637  157 VsAQLDR----------TVGRRNTFIGTPYWMAPEVIACdenpdATYDFKSDLWSLGITAIEMAEG 212
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
218-421 2.57e-04

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: 43.95  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEE-----ADLEWTVVKQSFLtevEQLSRfrHPNIVDF-AGYCAESGFYcLVYG 289
Cdd:cd05588    3 IGRGSYAKVLMVELKKTkrIYAMKVIKKElvnddEDIDWVQTEKHVF---ETASN--HPFLVGLhSCFQTESRLF-FVIE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLedQLHLQTQACSPLSWPQ--RLDILLgtarAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARfsrf 367
Cdd:cd05588   77 FVNGGDL--MFHMQRQRRLPEEHARfySAEISL----ALNFLHEKG--IIYRDLKLDNVLLDSEGHIKLTDYGMCK---- 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 189011594 368 AGANPSQSstvarTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd05588  145 EGLRPGDT-----TSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGR 193
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
214-420 2.82e-04

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: 43.49  E-value: 2.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 214 EELRIGEGGFGCVYRAVMRNT--TYAVKRLKEE---ADLEWTVVKQSFLTEVEQlsrfRHPNIVDFAGYCAESGFYCLVY 288
Cdd:cd14106   12 ESTPLGRGKFAVVRKCIHKETgkEYAAKFLRKRrrgQDCRNEILHEIAVLELCK----DCPRVVNLHEVYETRSELILIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 289 GFLPNGSLedQLHLQTQACSPLSWPQRL--DILlgtaRAIQFLHQDSpsLIHGDIKSSNVLL-----DERLmpKLGDFGL 361
Cdd:cd14106   88 ELAAGGEL--QTLLDEEECLTEADVRRLmrQIL----EGVQYLHERN--IVHLDLKPQNILLtsefpLGDI--KLCDFGI 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189011594 362 ARFsrfaganpsqsstVARTCTVR---GTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd14106  158 SRV-------------IGEGEEIReilGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTG 206
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
333-422 3.58e-04

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 43.85  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 333 SPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfagaNPSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGV 412
Cdd:PTZ00267 187 SRKMMHRDLKSANIFLMPTGIIKLGDFGFSK-------QYSDSVSLDVASSFCGTPYYLAPELWERKRYSKKADMWSLGV 259
                         90
                 ....*....|
gi 189011594 413 VILETLAGQR 422
Cdd:PTZ00267 260 ILYELLTLHR 269
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
218-363 3.60e-04

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: 43.50  E-value: 3.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCV---YRAVMRNTTyAVKRLKEEadLEWTVVKQSFLTEVEQLSRFRHPNIVDfagycaesgfycLVYGFLPNG 294
Cdd:cd07878   23 VGSGAYGSVcsaYDTRLRQKV-AVKKLSRP--FQSLIHARRTYRELRLLKHMKHENVIG------------LLDVFTPAT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 295 SLED--QLHLQTQ----------ACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLA 362
Cdd:cd07878   88 SIENfnEVYLVTNlmgadlnnivKCQKLSDEHVQFLIYQLLRGLKYIH--SAGIIHRDLKPSNVAVNEDCELRILDFGLA 165

                 .
gi 189011594 363 R 363
Cdd:cd07878  166 R 166
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
325-430 3.62e-04

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: 43.07  E-value: 3.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 325 AIQFLHQdsPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsRFAganpsqSSTVARTCTVRGTLAYLPEEYIKTGRLAVD 404
Cdd:cd05613  117 ALEHLHK--LGIIYRDIKLENILLDSSGHVVLTDFGLSK--EFL------LDENERAYSFCGTIEYMAPEIVRGGDSGHD 186
                         90       100
                 ....*....|....*....|....*...
gi 189011594 405 --TDTFSFGVVILETLAGQRAVRTQGAK 430
Cdd:cd05613  187 kaVDWWSLGVLMYELLTGASPFTVDGEK 214
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
308-419 3.65e-04

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 43.43  E-value: 3.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 308 SPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfagaNPSQSSTVARTCTVRGT 387
Cdd:cd05102  167 SPLTMEDLICYSFQVARGMEFLA--SRKCIHRDLAARNILLSENNVVKICDFGLAR-------DIYKDPDYVRKGSARLP 237
                         90       100       110
                 ....*....|....*....|....*....|..
gi 189011594 388 LAYLPEEYIKTGRLAVDTDTFSFGVVILETLA 419
Cdd:cd05102  238 LKWMAPESIFDKVYTTQSDVWSFGVLLWEIFS 269
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
218-363 3.72e-04

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: 43.13  E-value: 3.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIV---DFAGYCAESGF---YcLVYgfl 291
Cdd:cd07858   13 IGRGAYGIVCSAKNSETNEKVAIKKIANAFDNRIDAKRTLREIKLLRHLDHENVIaikDIMPPPHREAFndvY-IVY--- 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189011594 292 pngSLED-QLHLQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLAR 363
Cdd:cd07858   89 ---ELMDtDLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIH--SANVLHRDLKPSNLLLNANCDLKICDFGLAR 156
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
252-416 4.43e-04

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like 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: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 42.52  E-value: 4.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 252 VKQSFltevEQLSRFRHPNIVDFAGYC----AESGFYCLVYGFLPNGSLEDQLHLQTQACSPL---SWPQRLDILLGtar 324
Cdd:cd13984   42 IRAVF----DNLIQLDHPNIVKFHRYWtdvqEEKARVIFITEYMSSGSLKQFLKKTKKNHKTMnekSWKRWCTQILS--- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 325 AIQFLHQDSPSLIHGDIKSSNVLLDERLMPKLGDFGlarfsrfaganPSQSSTVARTC-TVRGTLAYLPEEYIKTGRLAV 403
Cdd:cd13984  115 ALSYLHSCDPPIIHGNLTCDTIFIQHNGLIKIGSVA-----------PDAIHNHVKTCrEEHRNLHFFAPEYGYLEDVTT 183
                        170
                 ....*....|...
gi 189011594 404 DTDTFSFGVVILE 416
Cdd:cd13984  184 AVDIYSFGMCALE 196
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
325-421 4.83e-04

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: 42.72  E-value: 4.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 325 AIQFLHQdsPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAGanpsqssTVARTCTVrGTLAYLPEEYIK-----TG 399
Cdd:cd05597  114 AIDSIHQ--LGYVHRDIKPDNVLLDRNGHIRLADFGSCLKLREDG-------TVQSSVAV-GTPDYISPEILQamedgKG 183
                         90       100
                 ....*....|....*....|..
gi 189011594 400 RLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd05597  184 RYGPECDWWSLGVCMYEMLYGE 205
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
211-430 5.18e-04

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


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 42.73  E-value: 5.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 211 NFSEELRIGEGGFGCVYRAVMRNTTYAVKRLKEEADLEwTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGF 290
Cdd:cd06649    6 DFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIK-PAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 291 LPNGSLEDQLHLQTQACSPLSWPQRLDILLGTARaIQFLHQdspsLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAGA 370
Cdd:cd06649   85 MDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAY-LREKHQ----IMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMA 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 371 NpsqsstvartcTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAK 430
Cdd:cd06649  160 N-----------SFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAK 208
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
218-372 5.27e-04

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: 42.78  E-value: 5.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCV----YRAVMRNTTYAVKRLKEEADLEwTVVKQSfLTEVEQLSRFR-HPNIV-----DFAGYCAESGFYClv 287
Cdd:cd07857    8 LGQGAYGIVcsarNAETSEEETVAIKKITNVFSKK-ILAKRA-LRELKLLRHFRgHKNITclydmDIVFPGNFNELYL-- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 288 YGFLpngsLEDQLHLQTQACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLAR-FSR 366
Cdd:cd07857   84 YEEL----MEADLHQIIRSGQPLTDAHFQSFIYQILCGLKYIH--SANVLHRDLKPGNLLVNADCELKICDFGLARgFSE 157

                 ....*.
gi 189011594 367 FAGANP 372
Cdd:cd07857  158 NPGENA 163
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
218-421 5.36e-04

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: 42.72  E-value: 5.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDfagycaesgfycLVYGFLPNGSLE 297
Cdd:cd07877   25 VGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIG------------LLDVFTPARSLE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 298 D--QLHLQTQ----------ACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFS 365
Cdd:cd07877   93 EfnDVYLVTHlmgadlnnivKCQKLTDDHVQFLIYQILRGLKYIH--SADIIHRDLKPSNLAVNEDCELKILDFGLARHT 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 366 rfagaNPSQSSTVArtctvrgTLAY-LPEEYIKTGRLAVDTDTFSFGVVILETLAGQ 421
Cdd:cd07877  171 -----DDEMTGYVA-------TRWYrAPEIMLNWMHYNQTVDIWSVGCIMAELLTGR 215
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
330-433 6.03e-04

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: 42.42  E-value: 6.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 330 HQDSPSLIHGDIKSSNVLLDERLMPKLGDFGLArfSRFAGANPSQSStvartctvrGTLAYLPEEYIKTGrLAVDT--DT 407
Cdd:cd05606  113 HMHNRFIVYRDLKPANILLDEHGHVRISDLGLA--CDFSKKKPHASV---------GTHGYMAPEVLQKG-VAYDSsaDW 180
                         90       100
                 ....*....|....*....|....*.
gi 189011594 408 FSFGVVILETLAGQRAVRTQGAKTKY 433
Cdd:cd05606  181 FSLGCMLYKLLKGHSPFRQHKTKDKH 206
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
323-419 6.33e-04

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 42.66  E-value: 6.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 323 ARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfagaNPSQSSTVARTCTVRGTLAYLPEEYIKTGRLA 402
Cdd:cd05103  189 AKGMEFLA--SRKCIHRDLAARNILLSENNVVKICDFGLAR-------DIYKDPDYVRKGDARLPLKWMAPETIFDRVYT 259
                         90
                 ....*....|....*..
gi 189011594 403 VDTDTFSFGVVILETLA 419
Cdd:cd05103  260 IQSDVWSFGVLLWEIFS 276
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
259-372 7.50e-04

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: 41.94  E-value: 7.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 259 EVEQLSRFRHPNIVD-FAGYCAESGFYcLVYGFLPNGSLEDQLHLQTQACSPLSWPQRLDILLgtarAIQFLHQDSpsLI 337
Cdd:cd14075   51 EISSMEKLHHPNIIRlYEVVETLSKLH-LVMEYASGGELYTKISTEGKLSESEAKPLFAQIVS----AVKHMHENN--II 123
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 189011594 338 HGDIKSSNVLLDERLMPKLGDFGLARFSR-------FAGANP 372
Cdd:cd14075  124 HRDLKAENVFYASNNCVKVGDFGFSTHAKrgetlntFCGSPP 165
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
218-420 7.60e-04

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: 41.92  E-value: 7.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVY--RAVMRNTTYAVKRLKEEADLEwtvvkQSFLTEVEQLSRF-RHPNIVDFAGYCAESG------FYCLVY 288
Cdd:cd06636   24 VGNGTYGQVYkgRHVKTGQLAAIKVMDVTEDEE-----EEIKLEINMLKKYsHHRNIATYYGAFIKKSppghddQLWLVM 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 289 GFLPNGSLEDQLHLQTQACSPLSWPQRL--DILLGTAraiqflHQDSPSLIHGDIKSSNVLLDERLMPKLGDFGL-ARFS 365
Cdd:cd06636   99 EFCGAGSVTDLVKNTKGNALKEDWIAYIcrEILRGLA------HLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVsAQLD 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 366 RfaganpsqssTVARTCTVRGTLAYLPEEYIKTGRLAVDT-----DTFSFGVVILETLAG 420
Cdd:cd06636  173 R----------TVGRRNTFIGTPYWMAPEVIACDENPDATydyrsDIWSLGITAIEMAEG 222
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
218-420 7.73e-04

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: 42.09  E-value: 7.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCV---YRAVMRNTTYAVK---RLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFL 291
Cdd:cd14076    9 LGEGEFGKVklgWPLPKANHRSGVQvaiKLIRRDTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGIVLEFV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 PNGSLEDqlHLQTQACSPLSWPQRLDILLgtARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLArfSRFAGAN 371
Cdd:cd14076   89 SGGELFD--YILARRRLKDSVACRLFAQL--ISGVAYLH--KKGVVHRDLKLENLLLDKNRNLVITDFGFA--NTFDHFN 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 189011594 372 PSQSSTvarTCtvrGTLAYLPEEYI--KTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd14076  161 GDLMST---SC---GSPCYAAPELVvsDSMYAGRKADIWSCGVILYAMLAG 205
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
218-363 7.89e-04

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: 42.28  E-value: 7.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEADLEwTVVKQSFlTEVEQLSRFRHPNIVdfagycaesgfyCLVYGFLPNGS 295
Cdd:cd07851   23 VGSGAYGQVCSAFDTKTgrKVAIKKLSRPFQSA-IHAKRTY-RELRLLKHMKHENVI------------GLLDVFTPASS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 296 LED--QLHLQTQ----------ACSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLAR 363
Cdd:cd07851   89 LEDfqDVYLVTHlmgadlnnivKCQKLSDDHIQFLVYQILRGLKYIH--SAGIIHRDLKPSNLAVNEDCELKILDFGLAR 166
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
218-435 8.12e-04

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: 42.33  E-value: 8.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVyRAVMRNTT---YAVKRLKEEADLEWTVV-----KQSFLTEVEQLSRFRHpnivdFAGYCAESGFYcLVYG 289
Cdd:cd05628    9 IGRGAFGEV-RLVQKKDTghvYAMKILRKADMLEKEQVghiraERDILVEADSLWVVKM-----FYSFQDKLNLY-LIME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 290 FLPNGSLEDQLHLQtqacSPLSWPQRLDILLGTARAIQFLHQdsPSLIHGDIKSSNVLLDERLMPKLGDFGL-------- 361
Cdd:cd05628   82 FLPGGDMMTLLMKK----DTLTEEETQFYIAETVLAIDSIHQ--LGFIHRDIKPDNLLLDSKGHVKLSDFGLctglkkah 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 362 -ARFSR-----------FAGANPSQSSTVAR------TCTVRGTLAYL-PEEYIKTGRLAVdTDTFSFGVVILETLAGQR 422
Cdd:cd05628  156 rTEFYRnlnhslpsdftFQNMNSKRKAETWKrnrrqlAFSTVGTPDYIaPEVFMQTGYNKL-CDWWSLGVIMYEMLIGYP 234
                        250
                 ....*....|...
gi 189011594 423 AVRTQGAKTKYLK 435
Cdd:cd05628  235 PFCSETPQETYKK 247
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
330-436 9.74e-04

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: 41.96  E-value: 9.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 330 HQDSPSLIHGDIKSSNVLLDERLMPKLGDFGLArfSRFAGANPSQSStvartctvrGTLAYLPEEYIKTGrLAVDT--DT 407
Cdd:cd14223  118 HMHSRFVVYRDLKPANILLDEFGHVRISDLGLA--CDFSKKKPHASV---------GTHGYMAPEVLQKG-VAYDSsaDW 185
                         90       100
                 ....*....|....*....|....*....
gi 189011594 408 FSFGVVILETLAGQRAVRTQGAKTKYLKD 436
Cdd:cd14223  186 FSLGCMLFKLLRGHSPFRQHKTKDKHEID 214
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
218-364 1.19e-03

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 41.48  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVY-------RAVMRNTTYAVKRLKEEADLEWTVVKQSfLTEVEQLSRFRHPNIVDFAG----YCAESGFYCL 286
Cdd:PHA02882  20 IGCGGFGCVYetqcasdHCINNQAVAKIENLENETIVMETLVYNN-IYDIDKIALWKNIHNIDHLGipkyYGCGSFKRCR 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 287 VY-GFLpngsLEDQLHLQTQACSP--LSWPQRL--DILLGTARAIQFLHQDSPSliHGDIKSSNVLLDERLMPKLGDFGL 361
Cdd:PHA02882  99 MYyRFI----LLEKLVENTKEIFKriKCKNKKLikNIMKDMLTTLEYIHEHGIS--HGDIKPENIMVDGNNRGYIIDYGI 172

                 ...
gi 189011594 362 ARF 364
Cdd:PHA02882 173 ASH 175
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
259-360 1.41e-03

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-C subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270946 [Multi-domain]  Cd Length: 271  Bit Score: 41.02  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 259 EVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLEDQLH--LQTQACSPLSWPQRLDILLGTARAIQFLHQdSPSL 336
Cdd:cd14044   53 ELNKLLQIDYYNLTKFYGTVKLDTMIFGVIEYCERGSLRDVLNdkISYPDGTFMDWEFKISVMYDIAKGMSYLHS-SKTE 131
                         90       100
                 ....*....|....*....|....
gi 189011594 337 IHGDIKSSNVLLDERLMPKLGDFG 360
Cdd:cd14044  132 VHGRLKSTNCVVDSRMVVKITDFG 155
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
218-439 1.80e-03

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) 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. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 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: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 40.78  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMR------NTTYAVKRLKEEADLEwtvVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYcLVYGFL 291
Cdd:cd05109   15 LGSGAFGTVYKGIWIpdgenvKIPVAIKVLRENTSPK---ANKEILDEAYVMAGVGSPYVCRLLGICLTSTVQ-LVTQLM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 292 PNGSLEDQLHLQTQACSP---LSWPQRLdillgtARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFsrfa 368
Cdd:cd05109   91 PYGCLLDYVRENKDRIGSqdlLNWCVQI------AKGMSYL--EEVRLVHRDLAARNVLVKSPNHVKITDFGLARL---- 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189011594 369 gANPSQSSTVARTCTVrgTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLA-GQRAVrtQGAKTKYLKDLIE 439
Cdd:cd05109  159 -LDIDETEYHADGGKV--PIKWMALESILHRRFTHQSDVWSYGVTVWELMTfGAKPY--DGIPAREIPDLLE 225
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
325-421 1.92e-03

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: 41.15  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 325 AIQFLHQdsPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFaganpSQSSTVARTCTVRGTLAYL-PEEYIKTGRLAV 403
Cdd:cd05598  113 AIESVHK--MGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRW-----THDSKYYLAHSLVGTPNYIaPEVLLRTGYTQL 185
                         90
                 ....*....|....*...
gi 189011594 404 dTDTFSFGVVILETLAGQ 421
Cdd:cd05598  186 -CDWWSVGVILYEMLVGQ 202
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
308-419 2.05e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 41.22  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 308 SPLSWPQRlDILLGTARAIQFLHqdSPSLIHGDIKSSNVLLDERLMPKLGDFGLarfsrfagANPSQSSTVARTCTVRGT 387
Cdd:PHA03210 263 RPLLKQTR-AIMKQLLCAVEYIH--DKKLIHRDIKLENIFLNCDGKIVLGDFGT--------AMPFEKEREAFDYGWVGT 331
                         90       100       110
                 ....*....|....*....|....*....|..
gi 189011594 388 LAYLPEEYIKTGRLAVDTDTFSFGVVILETLA 419
Cdd:PHA03210 332 VATNSPEILAGDGYCEITDIWSCGLILLDMLS 363
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
325-430 2.14e-03

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: 41.06  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 325 AIQFLHQdsPSLIHGDIKSSNVLLDERLMPKLGDFGLARfsRFAganpsqSSTVARTCTVRGTLAYLPEEYI--KTGRlA 402
Cdd:cd05614  117 ALEHLHK--LGIVYRDIKLENILLDSEGHVVLTDFGLSK--EFL------TEEKERTYSFCGTIEYMAPEIIrgKSGH-G 185
                         90       100
                 ....*....|....*....|....*...
gi 189011594 403 VDTDTFSFGVVILETLAGQRAVRTQGAK 430
Cdd:cd05614  186 KAVDWWSLGILMFELLTGASPFTLEGEK 213
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
311-363 2.89e-03

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R 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: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 40.60  E-value: 2.89e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 189011594 311 SWPQRLDILLG----TARAIQFLhqDSPSLIHGDIKSSNVLLDERLMPKLGDFGLAR 363
Cdd:cd05106  206 SWPLDLDDLLRfssqVAQGMDFL--ASKNCIHRDVAARNVLLTDGRVAKICDFGLAR 260
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
325-372 3.14e-03

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: 39.81  E-value: 3.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 325 AIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLA-------RFSRFAGANP 372
Cdd:cd14072  111 AVQYCHQKR--IVHRDLKAENLLLDADMNIKIADFGFSneftpgnKLDTFCGSPP 163
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
325-464 3.39e-03

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: 40.25  E-value: 3.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 325 AIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARfsrfagANPSQSSTVARTCtvrGTLAYL-PEEYIKTGRLAV 403
Cdd:cd05586  108 ALEHLHKND--IVYRDLKPENILLDANGHIALCDFGLSK------ADLTDNKTTNTFC---GTTEYLaPEVLLDEKGYTK 176
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189011594 404 DTDTFSFGVVILETLAGQR---AVRTQG-------AKTKYLKDLIEDEAEEVGVTLKSTQPTLWMGVATDA 464
Cdd:cd05586  177 MVDFWSLGVLVFEMCCGWSpfyAEDTQQmyrniafGKVRFPKDVLSDEGRSFVKGLLNRNPKHRLGAHDDA 247
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
218-365 3.45e-03

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: 39.94  E-value: 3.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNT--TYAVKRLKEEADLewtvVKQSfLTEVEQLSRFR------HPNIVDFAGYcaesgFY----- 284
Cdd:cd14133    7 LGKGTFGQVVKCYDLLTgeEVALKIIKNNKDY----LDQS-LDEIRLLELLNkkdkadKYHIVRLKDV-----FYfknhl 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 285 CLVYGFLPNGSLEdqLHLQTQAcSPLSWPQRLDILLGTARAIQFLHqdSPSLIHGDIKSSNVLL--DERLMPKLGDFGLA 362
Cdd:cd14133   77 CIVFELLSQNLYE--FLKQNKF-QYLSLPRIRKIAQQILEALVFLH--SLGLIHCDLKPENILLasYSRCQIKIIDFGSS 151

                 ...
gi 189011594 363 RFS 365
Cdd:cd14133  152 CFL 154
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
218-366 4.50e-03

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


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 39.56  E-value: 4.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRAVMRNTTYAV------KRLKEEADLEWTVVKqsfltEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFL 291
Cdd:cd14079   10 LGVGSFGKVKLAEHELTGHKVavkilnRQKIKSLDMEEKIRR-----EIQILKLFRHPHIIRLYEVIETPTDIFMVMEYV 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189011594 292 PNGSLEDQLHLQtqacSPLSWPQRLDILLGTARAIQFLHQDSpsLIHGDIKSSNVLLDERLMPKLGDFGLARFSR 366
Cdd:cd14079   85 SGGELFDYIVQK----GRLSEDEARRFFQQIISGVEYCHRHM--VVHRDLKPENLLLDSNMNVKIADFGLSNIMR 153
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
213-364 4.80e-03

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 38.44  E-value: 4.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 213 SEELRIGEGGFGCVYRaVMRNTTYAVKRLKeeadlewTVVKQSFLTEVEQLSRFRH------PNIVDFagyCAESGFYCL 286
Cdd:cd05120    1 ISVKLIKEGGDNKVYL-LGDPREYVLKIGP-------PRLKKDLEKEAAMLQLLAGklslpvPKVYGF---GESDGWEYL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 287 VYGFLPNGSLEDQLHLQTQAcsplswpQRLDILLGTARAIQFLHQ-DSPSLIHGDIKSSNVLLDE--RLmpkLG--DFGL 361
Cdd:cd05120   70 LMERIEGETLSEVWPRLSEE-------EKEKIADQLAEILAALHRiDSSVLTHGDLHPGNILVKPdgKL---SGiiDWEF 139

                 ...
gi 189011594 362 ARF 364
Cdd:cd05120  140 AGY 142
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
218-420 5.70e-03

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. Jaks 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 Jak3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271110 [Multi-domain]  Cd Length: 260  Bit Score: 39.12  E-value: 5.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 218 IGEGGFGCVYRA----VMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAeSGFYCLVYGFLPN 293
Cdd:cd14208    7 LGKGSFTKIYRGlrtdEEDDERCETEVLLKVMDPTHGNCQESFLEAASIMSQISHKHLVLLHGVCV-GKDSIMVQEFVCH 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189011594 294 GSLEDQLHLQTQACS-PLSWpqRLDILLGTARAIQFLhqDSPSLIHGDIKSSNVLLDERlmpklGDFGLARFSRFAgaNP 372
Cdd:cd14208   86 GALDLYLKKQQQKGPvAISW--KLQVVKQLAYALNYL--EDKQLVHGNVSAKKVLLSRE-----GDKGSPPFIKLS--DP 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 189011594 373 SQSSTVARTCTVRGTLAYL-PEEYIKTGRLAVDTDTFSFGVVILETLAG 420
Cdd:cd14208  155 GVSIKVLDEELLAERIPWVaPECLSDPQNLALEADKWGFGATLWEIFSG 203
 
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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