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Conserved domains on  [gi|17542550|ref|NP_501993|]
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Tyrosine-protein kinase [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
175-431 2.14e-110

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: 329.12  E-value: 2.14e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550    175 INLDKKLGCGAFGEVFKGQYKAVGStNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGKGD-GKEVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550    255 MELVTGGDLRKYLQTTQN--IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEVT 330
Cdd:smart00221  80 MEYMPGGDLLDYLRKNRPkeLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSrdLYDDDYY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550    331 TKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHdPLYPKSLKDAKAWILTEERPHKMENgDPKELMVLI 410
Cdd:smart00221 160 KVKGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEE-PYPGMSNAEVLEYLKKGYRLPKPPN-CPPELYKLM 237
                          250       260
                   ....*....|....*....|.
gi 17542550    411 DACCERNPNERLNFNTVKRQI 431
Cdd:smart00221 238 LQCWAEDPEDRPTFSELVEIL 258
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
72-153 1.93e-13

Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides via 2 surface pockets. Specificity is provided via interaction with residues that are distinct from the phosphotyrosine. Only a single occurrence of a SH2 domain has been found in S. cerevisiae.


:

Pssm-ID: 214585 [Multi-domain]  Cd Length: 84  Bit Score: 65.71  E-value: 1.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550     72 YHGVLFGSEAEKLLTW--DRAYLVRRAITKPNKFlCISVNWKKKIFHYQLDFNEDGwcckklyeKFPTMPNRRFLHIRQL 149
Cdd:smart00252   4 YHGFISREEAEKLLKNegDGDFLVRDSESSPGDY-VLSVRVKGKVKHYRIRRNEDG--------KFYLEGGRKFPSLVEL 74

                   ....
gi 17542550    150 LEAW 153
Cdd:smart00252  75 VEHY 78
 
Name Accession Description Interval E-value
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
175-431 2.14e-110

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: 329.12  E-value: 2.14e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550    175 INLDKKLGCGAFGEVFKGQYKAVGStNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGKGD-GKEVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550    255 MELVTGGDLRKYLQTTQN--IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEVT 330
Cdd:smart00221  80 MEYMPGGDLLDYLRKNRPkeLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSrdLYDDDYY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550    331 TKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHdPLYPKSLKDAKAWILTEERPHKMENgDPKELMVLI 410
Cdd:smart00221 160 KVKGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEE-PYPGMSNAEVLEYLKKGYRLPKPPN-CPPELYKLM 237
                          250       260
                   ....*....|....*....|.
gi 17542550    411 DACCERNPNERLNFNTVKRQI 431
Cdd:smart00221 238 LQCWAEDPEDRPTFSELVEIL 258
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
175-431 1.49e-99

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: 301.34  E-value: 1.49e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550   175 INLDKKLGCGAFGEVFKGQYKAVGStNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEGE-NTKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550   255 MELVTGGDLRKYLQT-TQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS---LQGTEVT 330
Cdd:pfam07714  80 TEYMPGGDLLDFLRKhKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSrdiYDDDYYR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550   331 TKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEhDPLYPKSLKDAKAWILTEERPHKMENgDPKELMVLI 410
Cdd:pfam07714 160 KRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGE-QPYPGMSNEEVLEFLEDGYRLPQPEN-CPDELYDLM 237
                         250       260
                  ....*....|....*....|.
gi 17542550   411 DACCERNPNERLNFNTVKRQI 431
Cdd:pfam07714 238 KQCWAYDPEDRPTFSELVEDL 258
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
179-432 1.23e-93

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: 286.36  E-value: 1.23e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKavGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd00192   1 KKLGEGAFGEVYKGKLK--GGDGKTVDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQ---------NIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSL---QG 326
Cdd:cd00192  79 EGGDLLDFLRKSRpvfpspepsTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRdiyDD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 327 TEVTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEhDPLYPKSLKDAKAWILTEERPHKMENGDPK-- 404
Cdd:cd00192 159 DYYRKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGA-TPYPGLSNEEVLEYLRKGYRLPKPENCPDEly 237
                       250       260
                ....*....|....*....|....*...
gi 17542550 405 ELMVLidaCCERNPNERLNFNTVKRQIT 432
Cdd:cd00192 238 ELMLS---CWQLDPEDRPTFSELVERLE 262
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
177-421 5.33e-36

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 140.15  E-value: 5.33e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGStnppiEVAVKRILGNAKR--KQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:COG0515  11 ILRLLGRGGMGVVYLARDLRLGR-----PVALKVLRPELAAdpEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEVTTK 332
Cdd:COG0515  86 MEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIAraLGGATLTQT 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 333 NLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARceHDPLYPKSLKDAKAWILTEE--RPHKMENGDPKELMVLI 410
Cdd:COG0515 166 GTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTG--RPPFDGDSPAELLRAHLREPppPPSELRPDLPPALDAIV 243
                       250
                ....*....|.
gi 17542550 411 DACCERNPNER 421
Cdd:COG0515 244 LRALAKDPEER 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
173-381 2.86e-18

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 86.03  E-value: 2.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  173 STINLDKKLGCGAFGEVFKGQYKAVGstnppiEVAVKRILGNA---KRKQIQEFCNEAQIMTVLQHENIVAFY-GFASlE 248
Cdd:PTZ00263  18 SDFEMGETLGTGSFGRVRIAKHKGTG------EYYAIKCLKKReilKMKQVQHVAQEKSILMELSHPFIVNMMcSFQD-E 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  249 EPIMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTE 328
Cdd:PTZ00263  91 NRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPD 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 17542550  329 vTTKNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMArcEHDPLYPKS 381
Cdd:PTZ00263 171 -RTFTLCGTP-EYLAPEVIQSKGHGKAVDWWTMGVLLYEFIA--GYPPFFDDT 219
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
205-369 4.77e-18

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 87.16  E-value: 4.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  205 EVAVKrILgnakRKQIQE-------FCNEAQIMTVLQHENIVAFY--GFaslEEPI-MVVMELVTGGDLRKYLQTTQNIP 274
Cdd:NF033483  34 DVAVK-VL----RPDLARdpefvarFRREAQSAASLSHPNIVSVYdvGE---DGGIpYIVMEYVDGRTLKDYIREHGPLS 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  275 KLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGL--SLQGTEVTTKNlekAPI---RWLAPESLKS 349
Cdd:NF033483 106 PEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIarALSSTTMTQTN---SVLgtvHYLSPEQARG 182
                        170       180
                 ....*....|....*....|
gi 17542550  350 GMFNEKTDVWSYGVFLTELM 369
Cdd:NF033483 183 GTVDARSDIYSLGIVLYEML 202
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
72-153 1.93e-13

Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides via 2 surface pockets. Specificity is provided via interaction with residues that are distinct from the phosphotyrosine. Only a single occurrence of a SH2 domain has been found in S. cerevisiae.


Pssm-ID: 214585 [Multi-domain]  Cd Length: 84  Bit Score: 65.71  E-value: 1.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550     72 YHGVLFGSEAEKLLTW--DRAYLVRRAITKPNKFlCISVNWKKKIFHYQLDFNEDGwcckklyeKFPTMPNRRFLHIRQL 149
Cdd:smart00252   4 YHGFISREEAEKLLKNegDGDFLVRDSESSPGDY-VLSVRVKGKVKHYRIRRNEDG--------KFYLEGGRKFPSLVEL 74

                   ....
gi 17542550    150 LEAW 153
Cdd:smart00252  75 VEHY 78
SH2 cd00173
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ...
72-151 1.76e-09

Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they bind pTyr-containing polypeptide ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. They are present in a wide array of proteins including: adaptor proteins (Nck1, Crk, Grb2), scaffolds (Slp76, Shc, Dapp1), kinases (Src, Syk, Fps, Tec), phosphatases (Shp-1, Shp-2), transcription factors (STAT1), Ras signaling molecules (Ras-Gap), ubiquitination factors (c-Cbl), cytoskeleton regulators (Tensin), signal regulators (SAP), and phospholipid second messengers (PLCgamma), amongst others.


Pssm-ID: 198173 [Multi-domain]  Cd Length: 79  Bit Score: 54.38  E-value: 1.76e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  72 YHGVLFGSEAEKLLT--WDRAYLVRRAITKPNKFlCISVNWK-KKIFHYQLDFNEDGWCCKKLyekfptmPNRRFLHIRQ 148
Cdd:cd00173   3 FHGSISREEAERLLRgkPDGTFLVRESSSEPGDY-VLSVRSGdGKVKHYLIERNEGGYYLLGG-------SGRTFPSLPE 74

                ...
gi 17542550 149 LLE 151
Cdd:cd00173  75 LVE 77
 
Name Accession Description Interval E-value
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
175-431 2.14e-110

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: 329.12  E-value: 2.14e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550    175 INLDKKLGCGAFGEVFKGQYKAVGStNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGKGD-GKEVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550    255 MELVTGGDLRKYLQTTQN--IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEVT 330
Cdd:smart00221  80 MEYMPGGDLLDYLRKNRPkeLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSrdLYDDDYY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550    331 TKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHdPLYPKSLKDAKAWILTEERPHKMENgDPKELMVLI 410
Cdd:smart00221 160 KVKGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEE-PYPGMSNAEVLEYLKKGYRLPKPPN-CPPELYKLM 237
                          250       260
                   ....*....|....*....|.
gi 17542550    411 DACCERNPNERLNFNTVKRQI 431
Cdd:smart00221 238 LQCWAEDPEDRPTFSELVEIL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
175-431 3.49e-110

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 328.72  E-value: 3.49e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550    175 INLDKKLGCGAFGEVFKGQYKAvGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKG-KGGKKKVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550    255 MELVTGGDLRKYLQTTQ-NIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEVTT 331
Cdd:smart00219  80 MEYMEGGDLLSYLRKNRpKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSrdLYDDDYYR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550    332 KNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHdPLYPKSLKDAKAWILTEERPHKMENgDPKELMVLID 411
Cdd:smart00219 160 KRGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQ-PYPGMSNEEVLEYLKNGYRLPQPPN-CPPELYDLML 237
                          250       260
                   ....*....|....*....|
gi 17542550    412 ACCERNPNERLNFNTVKRQI 431
Cdd:smart00219 238 QCWAEDPEDRPTFSELVEIL 257
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
175-431 1.49e-99

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: 301.34  E-value: 1.49e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550   175 INLDKKLGCGAFGEVFKGQYKAVGStNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEGE-NTKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550   255 MELVTGGDLRKYLQT-TQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS---LQGTEVT 330
Cdd:pfam07714  80 TEYMPGGDLLDFLRKhKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSrdiYDDDYYR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550   331 TKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEhDPLYPKSLKDAKAWILTEERPHKMENgDPKELMVLI 410
Cdd:pfam07714 160 KRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGE-QPYPGMSNEEVLEFLEDGYRLPQPEN-CPDELYDLM 237
                         250       260
                  ....*....|....*....|.
gi 17542550   411 DACCERNPNERLNFNTVKRQI 431
Cdd:pfam07714 238 KQCWAYDPEDRPTFSELVEDL 258
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
179-432 1.23e-93

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: 286.36  E-value: 1.23e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKavGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd00192   1 KKLGEGAFGEVYKGKLK--GGDGKTVDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQ---------NIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSL---QG 326
Cdd:cd00192  79 EGGDLLDFLRKSRpvfpspepsTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRdiyDD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 327 TEVTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEhDPLYPKSLKDAKAWILTEERPHKMENGDPK-- 404
Cdd:cd00192 159 DYYRKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGA-TPYPGLSNEEVLEYLRKGYRLPKPENCPDEly 237
                       250       260
                ....*....|....*....|....*...
gi 17542550 405 ELMVLidaCCERNPNERLNFNTVKRQIT 432
Cdd:cd00192 238 ELMLS---CWQLDPEDRPTFSELVERLE 262
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
181-427 3.43e-60

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: 198.92  E-value: 3.43e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAvgstnppIEVAVKRILGNAKR-KQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVT 259
Cdd:cd13999   1 IGSGSFGEVYKGKWRG-------TDVAIKKLKVEDDNdELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 260 GGDLRKYLQTTQ-NIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSlqGTEVTTKNLEKAP 338
Cdd:cd13999  74 GGSLYDLLHKKKiPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLS--RIKNSTTEKMTGV 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 339 I---RWLAPESLKSGMFNEKTDVWSYGVFLTELMARcehDPLYPK--SLKDAKAWILTEERPhKMENGDPKELMVLIDAC 413
Cdd:cd13999 152 VgtpRWMAPEVLRGEPYTEKADVYSFGIVLWELLTG---EVPFKElsPIQIAAAVVQKGLRP-PIPPDCPPELSKLIKRC 227
                       250
                ....*....|....
gi 17542550 414 CERNPNERLNFNTV 427
Cdd:cd13999 228 WNEDPEKRPSFSEI 241
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
175-434 1.24e-58

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: 195.26  E-value: 1.24e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKavGSTnppieVAVKRILGNAKRKQiqEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:cd05039   8 LKLGELIGKGEFGDVMLGDYR--GQK-----VAVKCLKDDSTAAQ--AFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQT--TQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGtevtTK 332
Cdd:cd05039  79 TEYMAKGSLVDYLRSrgRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEA----SS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 333 NLE--KAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMA--RCehdPlYPK-SLKDAKAWIlteERPHKME--NGDPKE 405
Cdd:cd05039 155 NQDggKLPIKWTAPEALREKKFSTKSDVWSFGILLWEIYSfgRV---P-YPRiPLKDVVPHV---EKGYRMEapEGCPPE 227
                       250       260
                ....*....|....*....|....*....
gi 17542550 406 LMVLIDACCERNPNERLNFNTVKRQITDI 434
Cdd:cd05039 228 VYKVMKNCWELDPAKRPTFKQLREKLEHI 256
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
175-424 1.05e-57

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: 193.71  E-value: 1.05e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:cd05032   8 ITLIRELGQGSFGMVYEGLAKGVVKGEPETRVAIKTVNENASMRERIEFLNEASVMKEFNCHHVVRLLGVVSTGQPTLVV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTT---------QNIPKLQ-ILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS- 323
Cdd:cd05032  88 MELMAKGDLKSYLRSRrpeaennpgLGPPTLQkFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDFGMTr 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 324 -LQGTEVTTKNLEKA-PIRWLAPESLKSGMFNEKTDVWSYGVFLTElMARCEHDPLYPKSLKDAKAWILTE---ERPhkm 398
Cdd:cd05032 168 dIYETDYYRKGGKGLlPVRWMAPESLKDGVFTTKSDVWSFGVVLWE-MATLAEQPYQGLSNEEVLKFVIDGghlDLP--- 243
                       250       260
                ....*....|....*....|....*.
gi 17542550 399 eNGDPKELMVLIDACCERNPNERLNF 424
Cdd:cd05032 244 -ENCPDKLLELMRMCWQYNPKMRPTF 268
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
179-432 3.87e-55

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: 186.11  E-value: 3.87e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd05041   1 EKIGRGNFGDVYRGVLKPDNT-----EVAVKTCRETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQN-IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ---GTEVTTKNL 334
Cdd:cd05041  76 PGGSLLTFLRKKGArLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREeedGEYTVSDGL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 335 EKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARceHDPLYPK-SLKDAKAWIlteERPHKM--ENGDPKELMVLID 411
Cdd:cd05041 156 KQIPIKWTAPEALNYGRYTSESDVWSFGILLWEIFSL--GATPYPGmSNQQTREQI---ESGYRMpaPELCPEAVYRLML 230
                       250       260
                ....*....|....*....|.
gi 17542550 412 ACCERNPNERLNFNTVKRQIT 432
Cdd:cd05041 231 QCWAYDPENRPSFSEIYNELQ 251
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
179-435 5.04e-55

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: 186.02  E-value: 5.04e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGstNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFaSLEEPIMVVMELV 258
Cdd:cd05060   1 KELGHGNFGSVRKGVYLMKS--GKEVEVAVKTLKQEHEKAGKKEFLREASVMAQLDHPCIVRLIGV-CKGEPLMLVMELA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS----LQGTEVTTKNL 334
Cdd:cd05060  78 PLGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSralgAGSDYYRATTA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 335 EKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHdPLYPKSLKDAKAWIlteERPHKME--NGDPKELMVLIDA 412
Cdd:cd05060 158 GRWPLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSYGAK-PYGEMKGPEVIAML---ESGERLPrpEECPQEIYSIMLS 233
                       250       260
                ....*....|....*....|...
gi 17542550 413 CCERNPNERLNFNTVKRQITDIY 435
Cdd:cd05060 234 CWKYRPEDRPTFSELESTFRRDP 256
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
179-428 2.95e-53

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: 180.94  E-value: 2.95e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKavGSTnppiEVAVKRIlgnakrKQ----IQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:cd05034   1 KKLGAGQFGEVWMGVWN--GTT----KVAVKTL------KPgtmsPEAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIV 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQT----TQNIPKLqiLWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTE 328
Cdd:cd05034  69 TELMSKGSLLDYLRTgegrALRLPQL--IDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLArlIEDDE 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 329 VTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELM--ARCehdPlYP-KSLKDAKAWILTEERPHKMENGdPKE 405
Cdd:cd05034 147 YTAREGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLYEIVtyGRV---P-YPgMTNREVLEQVERGYRMPKPPGC-PDE 221
                       250       260
                ....*....|....*....|...
gi 17542550 406 LMVLIDACCERNPNERLNFNTVK 428
Cdd:cd05034 222 LYDIMLQCWKKEPEERPTFEYLQ 244
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
179-432 2.28e-51

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: 177.19  E-value: 2.28e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFA-SLEEPIM-VVME 256
Cdd:cd05038  10 KQLGEGHFGSVELCRYDPLGD-NTGEQVAVKSLQPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCeSPGRRSLrLIME 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQ-NIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTE----VTT 331
Cdd:cd05038  89 YLPSGSLRDYLQRHRdQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVLPEdkeyYYV 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 332 KNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHD----PLYPKSLKDAKAWILTEERPHKMENGD----- 402
Cdd:cd05038 169 KEPGESPIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGDPSqsppALFLRMIGIAQGQMIVTRLLELLKSGErlprp 248
                       250       260       270
                ....*....|....*....|....*....|...
gi 17542550 403 ---PKELMVLIDACCERNPNERLNFNTVKRQIT 432
Cdd:cd05038 249 pscPDEVYDLMKECWEYEPQDRPSFSDLILIID 281
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
177-429 1.61e-50

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 173.87  E-value: 1.61e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550    177 LDKKLGCGAFGEVFKGQYKAVGStnppiEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVME 256
Cdd:smart00220   3 ILEKLGEGSFGKVYLARDKKTGK-----LVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550    257 LVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLEK 336
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTTFV 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550    337 APIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCehdPLYPKSLKDAKAW-ILTEERPHKMENGD--PKELMVLIDAC 413
Cdd:smart00220 158 GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGK---PPFPGDDQLLELFkKIGKPKPPFPPPEWdiSPEAKDLIRKL 234
                          250
                   ....*....|....*.
gi 17542550    414 CERNPNERLNFNTVKR 429
Cdd:smart00220 235 LVKDPEKRLTAEEALQ 250
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
179-433 2.76e-50

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: 173.76  E-value: 2.76e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAV-GSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMEL 257
Cdd:cd05044   1 KFLGSGAFGEVFEGTAKDIlGDGSGETKVAVKTLRKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQ----TTQNIPKL---QILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQ----DLKAKISDFGLS--L 324
Cdd:cd05044  81 MEGGDLLSYLRaarpTAFTPPLLtlkDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSkdyrERVVKIGDFGLArdI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 325 QGTEVTTKNLE-KAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARcEHDPlYP-KSLKDAKAWILTEERPHKMENGd 402
Cdd:cd05044 161 YKNDYYRKEGEgLLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEILTL-GQQP-YPaRNNLEVLHFVRAGGRLDQPDNC- 237
                       250       260       270
                ....*....|....*....|....*....|.
gi 17542550 403 PKELMVLIDACCERNPNERLNFNTVKRQITD 433
Cdd:cd05044 238 PDDLYELMLRCWSTDPEERPSFARILEQLQN 268
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
173-431 1.41e-49

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: 171.59  E-value: 1.41e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 173 STINLDKKLGCGAFGEVFKGQYKAVgstnppiEVAVKRILGNAKrkqIQEFCNEAQIMTVLQHENIVAFYGFAsLEEPIM 252
Cdd:cd05083   6 QKLTLGEIIGEGEFGAVLQGEYMGQ-------KVAVKNIKCDVT---AQAFLEETAVMTKLQHKNLVRLLGVI-LHNGLY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYLQTTQN--IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSlqGTEVT 330
Cdd:cd05083  75 IVMELMSKGNLVNFLRSRGRalVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLA--KVGSM 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 331 TKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHDplYPK-SLKDAKAWIlteERPHKME--NGDPKELM 407
Cdd:cd05083 153 GVDNSRLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGRAP--YPKmSVKEVKEAV---EKGYRMEppEGCPPDVY 227
                       250       260
                ....*....|....*....|....
gi 17542550 408 VLIDACCERNPNERLNFNTVKRQI 431
Cdd:cd05083 228 SIMTSCWEAEPGKRPSFKKLREKL 251
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
173-431 1.73e-49

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: 171.40  E-value: 1.73e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 173 STINLDKKLGCGAFGEVFKGQYKAVGstNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIM 252
Cdd:cd05033   4 SYVTIEKVIGGGEFGEVCSGSLKLPG--KKEIDVAIKTLKSGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRPVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYL-QTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEV 329
Cdd:cd05033  82 IVTEYMENGSLDKFLrENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSrrLEDSEA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 T-TKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHdPLYPKSLKDAKAWILTEER-PHKMENgdPKELM 407
Cdd:cd05033 162 TyTTKGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSYGER-PYWDMSNQDVIKAVEDGYRlPPPMDC--PSALY 238
                       250       260
                ....*....|....*....|....
gi 17542550 408 VLIDACCERNPNERLNFNTVKRQI 431
Cdd:cd05033 239 QLMLDCWQKDRNERPTFSQIVSTL 262
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
174-427 5.09e-49

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: 170.72  E-value: 5.09e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 174 TINLDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMV 253
Cdd:cd05049   6 TIVLKRELGEGAFGKVFLGECYNLEPEQDKMLVAVKTLKDASSPDARKDFEREAELLTNLQHENIVKFYGVCTEGDPLLM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYL--------------QTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISD 319
Cdd:cd05049  86 VFEYMEHGDLNKFLrshgpdaaflasedSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKIGD 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 320 FGLSlqgTEVTTKNLEKA------PIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHdPLYPKSLKDAKAWIlTEE 393
Cdd:cd05049 166 FGMS---RDIYSTDYYRVgghtmlPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQ-PWFQLSNTEVIECI-TQG 240
                       250       260       270
                ....*....|....*....|....*....|....
gi 17542550 394 RPHKMENGDPKELMVLIDACCERNPNERLNFNTV 427
Cdd:cd05049 241 RLLQRPRTCPSEVYAVMLGCWKREPQQRLNIKDI 274
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
179-431 6.63e-49

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: 169.73  E-value: 6.63e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAvgsTNPPieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd05084   2 ERIGRGNFGEVFSGRLRA---DNTP--VAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTT-QNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ---GTEVTTKNL 334
Cdd:cd05084  77 QGGDFLTFLRTEgPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREeedGVYAATGGM 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 335 EKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEhDPLYPKSLKDAKAWIlteERPHKMENGD--PKELMVLIDA 412
Cdd:cd05084 157 KQIPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGA-VPYANLSNQQTREAV---EQGVRLPCPEncPDEVYRLMEQ 232
                       250
                ....*....|....*....
gi 17542550 413 CCERNPNERLNFNTVKRQI 431
Cdd:cd05084 233 CWEYDPRKRPSFSTVHQDL 251
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
173-435 6.73e-49

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: 169.89  E-value: 6.73e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 173 STINLDKKLGCGAFGEVFKGQYkavgstNPPIEVAVKRIlgNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIM 252
Cdd:cd05068   8 KSLKLLRKLGSGQFGEVWEGLW------NNTTPVAVKTL--KPGTMDPEDFLREAQIMKKLRHPKLIQLYAVCTLEEPIY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYLQTTQNIPKL-QILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEV 329
Cdd:cd05068  80 IITELMKHGSLLEYLQGKGRSLQLpQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLArvIKVEDE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 -TTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHdPlYPKSlkdAKAWILTE-ERPHKMEN--GDPKE 405
Cdd:cd05068 160 yEAREGAKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTYGRI-P-YPGM---TNAEVLQQvERGYRMPCppNCPPQ 234
                       250       260       270
                ....*....|....*....|....*....|
gi 17542550 406 LMVLIDACCERNPNERLNFNTVKRQITDIY 435
Cdd:cd05068 235 LYDIMLECWKADPMERPTFETLQWKLEDFF 264
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
172-434 3.40e-48

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: 168.00  E-value: 3.40e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 172 HSTINLDKKLGCGAFGEVFKGQYKAVgstnppIEVAVKRILGNAKRKQiQEFCNEAQIMTVLQHENIVAFYGFASLEEPI 251
Cdd:cd05148   5 REEFTLERKLGSGYFGEVWEGLWKNR------VRVAIKILKSDDLLKQ-QDFQKEVQALKRLRHKHLISLFAVCSVGEPV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 MVVMELVTGGDLRKYLQTT--QNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS-LQGTE 328
Cdd:cd05148  78 YIITELMEKGSLLAFLRSPegQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLArLIKED 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 329 VTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHDplYPKSLKDAKAWILTE----ERPHKMengdPK 404
Cdd:cd05148 158 VYLSSDKKIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQVP--YPGMNNHEVYDQITAgyrmPCPAKC----PQ 231
                       250       260       270
                ....*....|....*....|....*....|
gi 17542550 405 ELMVLIDACCERNPNERLNFNTVKRQITDI 434
Cdd:cd05148 232 EIYKIMLECWAAEPEDRPSFKALREELDNI 261
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
181-431 4.07e-48

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: 166.29  E-value: 4.07e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGstnppIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd00180   1 LGKGSFGKVYKARDKETG-----KKVAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQT-TQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ---GTEVTTKNLEK 336
Cdd:cd00180  76 GSLKDLLKEnKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDldsDDSLLKTTGGT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 337 APIRWLAPESLKSGMFNEKTDVWSYGVFLTELmarcehdplypKSLKDakawilteerphkmengdpkelmvLIDACCER 416
Cdd:cd00180 156 TPPYYAPPELLGGRYYGPKVDIWSLGVILYEL-----------EELKD------------------------LIRRMLQY 200
                       250
                ....*....|....*
gi 17542550 417 NPNERLNFNTVKRQI 431
Cdd:cd00180 201 DPKKRPSAKELLEHL 215
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
179-433 4.99e-48

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: 167.52  E-value: 4.99e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTNppIEVAVKrILGNAKRKQ---IQEFCNEAQIMTVLQHENIVAFYGFAsLEEPIMVVM 255
Cdd:cd05040   1 EKLGDGSFGVVRRGEWTTPSGKV--IQVAVK-CLKSDVLSQpnaMDDFLKEVNAMHSLDHPNLIRLYGVV-LSSPLMMVT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRKYLQTTQNIPKLQILW-FAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTE---V 329
Cdd:cd05040  77 ELAPLGSLLDRLRKDQGHFLISTLCdYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMraLPQNEdhyV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 TTKNLeKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEhDPLypKSLKDAKawILTE-----ERPHKMENGdPK 404
Cdd:cd05040 157 MQEHR-KVPFAWCAPESLKTRKFSHASDVWMFGVTLWEMFTYGE-EPW--LGLNGSQ--ILEKidkegERLERPDDC-PQ 229
                       250       260
                ....*....|....*....|....*....
gi 17542550 405 ELMVLIDACCERNPNERLNFNTVKRQITD 433
Cdd:cd05040 230 DIYNVMLQCWAHKPADRPTFVALRDFLPE 258
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
181-432 9.41e-48

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: 166.33  E-value: 9.41e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGStnppieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd05085   4 LGKGNFGEVYKGTLKDKTP------VAVKTCKEDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQTTQNIPKL-QILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ--GTEVTTKNLEKA 337
Cdd:cd05085  78 GDFLSFLRKKKDELKTkQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQedDGVYSSSGLKQI 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 338 PIRWLAPESLKSGMFNEKTDVWSYGVFLTEL--MARCEhdplYP-KSLKDAKAWIlteERPHKMENGD--PKELMVLIDA 412
Cdd:cd05085 158 PIKWTAPEALNYGRYSSESDVWSFGILLWETfsLGVCP----YPgMTNQQAREQV---EKGYRMSAPQrcPEDIYKIMQR 230
                       250       260
                ....*....|....*....|
gi 17542550 413 CCERNPNERLNFNTVKRQIT 432
Cdd:cd05085 231 CWDYNPENRPKFSELQKELA 250
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
174-435 1.83e-46

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: 163.67  E-value: 1.83e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 174 TINLDKKLGCGAFGEVFKGQYkavgstNPPIEVAVKRIlgNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMV 253
Cdd:cd05072   8 SIKLVKKLGAGQFGEVWMGYY------NNSTKVAVKTL--KPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQN----IPKLqiLWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGT 327
Cdd:cd05072  80 ITEYMAKGSLLDFLKSDEGgkvlLPKL--IDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLArvIEDN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 328 EVTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHDplYP-KSLKDAKAWILTEERPHKMENGdPKEL 406
Cdd:cd05072 158 EYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTYGKIP--YPgMSNSDVMSALQRGYRMPRMENC-PDEL 234
                       250       260
                ....*....|....*....|....*....
gi 17542550 407 MVLIDACCERNPNERLNFNTVKRQITDIY 435
Cdd:cd05072 235 YDIMKTCWKEKAEERPTFDYLQSVLDDFY 263
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
173-427 2.76e-46

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: 163.74  E-value: 2.76e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 173 STINLDKKLGCGAFGEVFKGQYKAV-GSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVL-QHENIVAFYGFASLEEP 250
Cdd:cd05053  12 DRLTLGKPLGEGAFGQVVKAEAVGLdNKPNEVVTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDGP 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMELVTGGDLRKYLQ----------------TTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLK 314
Cdd:cd05053  92 LYVVVEYASKGNLREFLRarrppgeeaspddprvPEEQLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVLVTEDNV 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 315 AKISDFGLSLQGTEV-----TTKNleKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMArCEHDPlYP--------KS 381
Cdd:cd05053 172 MKIADFGLARDIHHIdyyrkTTNG--RLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFT-LGGSP-YPgipveelfKL 247
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 17542550 382 LKDAKAWilteERPHKMengdPKELMVLIDACCERNPNERLNFNTV 427
Cdd:cd05053 248 LKEGHRM----EKPQNC----TQELYMLMRDCWHEVPSQRPTFKQL 285
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
175-445 7.22e-46

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: 162.45  E-value: 7.22e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:cd05061   8 ITLLRELGQGSFGMVYEGNARDIIKGEAETRVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPTLVV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQT----TQN-----IPKLQ-ILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSL 324
Cdd:cd05061  88 MELMAHGDLKSYLRSlrpeAENnpgrpPPTLQeMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMTR 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 325 QGTEvtTKNLEKA-----PIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHdPLYPKSLKDAKAWILTEERPHKME 399
Cdd:cd05061 168 DIYE--TDYYRKGgkgllPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQ-PYQGLSNEQVLKFVMDGGYLDQPD 244
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 17542550 400 NGdPKELMVLIDACCERNPNERLNFntvkRQITDIYMEALNKGPQD 445
Cdd:cd05061 245 NC-PERVTDLMRMCWQFNPKMRPTF----LEIVNLLKDDLHPSFPE 285
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
175-432 8.31e-46

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: 162.17  E-value: 8.31e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:cd05036   8 LTLIRALGQGAFGEVYEGTVSGMPGDPSPLQVAVKTLPELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQRLPRFIL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTTQNIPK-------LQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQ---DLKAKISDFGLSl 324
Cdd:cd05036  88 LELMAGGDLKSFLRENRPRPEqpssltmLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCkgpGRVAKIGDFGMA- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 325 qgtevttKNLEKA-----------PIRWLAPESLKSGMFNEKTDVWSYGVFLTELMArCEHDPlYP-KSLKDAKAWILTE 392
Cdd:cd05036 167 -------RDIYRAdyyrkggkamlPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFS-LGYMP-YPgKSNQEVMEFVTSG 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 17542550 393 ERphkME--NGDPKELMVLIDACCERNPNERLNFNTVKRQIT 432
Cdd:cd05036 238 GR---MDppKNCPGPVYRIMTQCWQHIPEDRPNFSTILERLN 276
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
179-369 1.62e-45

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: 161.43  E-value: 1.62e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTNPpIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFaSLEEPIMVVMELV 258
Cdd:cd05057  13 KVLGSGAFGTVYKGVWIPEGEKVK-IPVAIKVLREETGPKANEEILDEAYVMASVDHPHLVRLLGI-CLSSQVQLITQLM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYL-QTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS-LQGTEVTTKNLE- 335
Cdd:cd05057  91 PLGCLLDYVrNHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAkLLDVDEKEYHAEg 170
                       170       180       190
                ....*....|....*....|....*....|....*
gi 17542550 336 -KAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd05057 171 gKVPIKWMALESIQYRIYTHKSDVWSYGVTVWELM 205
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
173-368 2.57e-45

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: 161.00  E-value: 2.57e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 173 STINLDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIM 252
Cdd:cd05048   5 SAVRFLEELGEGAFGKVYKGELLGPSSEESAISVAIKTLKENASPKTQQDFRREAELMSDLQHPNIVCLLGVCTKEQPQC 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYLqtTQNIPK------------LQILW------FAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLK 314
Cdd:cd05048  85 MLFEYMAHGDLHEFL--VRHSPHsdvgvssdddgtASSLDqsdflhIAIQIAAGMEYLSSHHYVHRDLAARNCLVGDGLT 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17542550 315 AKISDFGLSLQG-----TEVTTKNLekAPIRWLAPESLKSGMFNEKTDVWSYGVFLTEL 368
Cdd:cd05048 163 VKISDFGLSRDIyssdyYRVQSKSL--LPVRWMPPEAILYGKFTTESDVWSFGVVLWEI 219
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
179-432 2.67e-45

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: 159.92  E-value: 2.67e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVgstnppIEVAVKRILGNAKRKQiqEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd05059  10 KELGSGQFGVVHLGKWRGK------IDVAIKMIKEGSMSED--DFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQNIPKLQILW-FAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEVTTKNLE 335
Cdd:cd05059  82 ANGCLLNYLRERRGKFQTEQLLeMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLAryVLDDEYTSSVGT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 336 KAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMArCEHDPLYPKSLKDAKAWILTE---ERPHKMengdPKELMVLIDA 412
Cdd:cd05059 162 KFPVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFS-EGKMPYERFSNSEVVEHISQGyrlYRPHLA----PTEVYTIMYS 236
                       250       260
                ....*....|....*....|
gi 17542550 413 CCERNPNERLNFNTVKRQIT 432
Cdd:cd05059 237 CWHEKPEERPTFKILLSQLT 256
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
173-424 8.64e-45

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: 158.74  E-value: 8.64e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 173 STINLDKKLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKrkQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIM 252
Cdd:cd05052   6 TDITMKHKLGGGQYGEVYEGVWKKYNLT-----VAVKTLKEDTM--EVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYLQTT--QNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTE 328
Cdd:cd05052  79 IITEFMPYGNLLDYLRECnrEELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSrlMTGDT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 329 VTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELmARCEHDPlYPK-SLKDAKAWIlteERPHKME--NGDPKE 405
Cdd:cd05052 159 YTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEI-ATYGMSP-YPGiDLSQVYELL---EKGYRMErpEGCPPK 233
                       250
                ....*....|....*....
gi 17542550 406 LMVLIDACCERNPNERLNF 424
Cdd:cd05052 234 VYELMRACWQWNPSDRPSF 252
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
175-427 1.68e-44

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: 158.59  E-value: 1.68e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKrILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:cd05092   7 IVLKWELGEGAFGKVFLAECHNLLPEQDKMLVAVK-ALKEATESARQDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTTQNIPKL---------------QILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISD 319
Cdd:cd05092  86 FEYMRHGDLNRFLRSHGPDAKIldggegqapgqltlgQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGD 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 320 FGLS--LQGTE---VTTKNLekAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHdPLYPKSLKDAKAWIlTEER 394
Cdd:cd05092 166 FGMSrdIYSTDyyrVGGRTM--LPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTYGKQ-PWYQLSNTEAIECI-TQGR 241
                       250       260       270
                ....*....|....*....|....*....|...
gi 17542550 395 PHKMENGDPKELMVLIDACCERNPNERLNFNTV 427
Cdd:cd05092 242 ELERPRTCPPEVYAIMQGCWQREPQQRHSIKDI 274
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
175-437 2.17e-44

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: 157.97  E-value: 2.17e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKAvgSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASlEEPIMVV 254
Cdd:cd05056   8 ITLGRCIGEGQFGDVYQGVYMS--PENEKIAVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVIT-ENPVWIV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTTQN-IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEVTT 331
Cdd:cd05056  85 MELAPLGELRSYLQVNKYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSryMEDESYYK 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 332 KNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCehdplypkslKDAKAWILTEERPHKMENGD--------P 403
Cdd:cd05056 165 ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMLG----------VKPFQGVKNNDVIGRIENGErlpmppncP 234
                       250       260       270
                ....*....|....*....|....*....|....
gi 17542550 404 KELMVLIDACCERNPNERLNFNTVKRQITDIYME 437
Cdd:cd05056 235 PTLYSLMTKCWAYDPSKRPRFTELKAQLSDILQE 268
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
181-424 4.09e-43

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: 154.93  E-value: 4.09e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd05046  13 LGRGEFGEVFLAKAKGIEEEGGETLVLVKALQKTKDENLQSEFRRELDMFRKLSHKNVVRLLGLCREAEPHYMILEYTDL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQTT---------QNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEV 329
Cdd:cd05046  93 GDLKQFLRATkskdeklkpPPLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLSkdVYNSEY 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 TTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHdPLYPKS----LKDAKAWILTEERPhkmeNGDPKE 405
Cdd:cd05046 173 YKLRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTQGEL-PFYGLSdeevLNRLQAGKLELPVP----EGCPSR 247
                       250
                ....*....|....*....
gi 17542550 406 LMVLIDACCERNPNERLNF 424
Cdd:cd05046 248 LYKLMTRCWAVNPKDRPSF 266
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
174-435 2.04e-42

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: 152.73  E-value: 2.04e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 174 TINLDKKLGCGAFGEVFKGQYKavGSTnppiEVAVKRIlgNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASlEEPIMV 253
Cdd:cd05067   8 TLKLVERLGAGQFGEVWMGYYN--GHT----KVAIKSL--KQGSMSPDAFLAEANLMKQLQHQRLVRLYAVVT-QEPIYI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQNIpKLQI---LWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTE 328
Cdd:cd05067  79 ITEYMENGSLVDFLKTPSGI-KLTInklLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLArlIEDNE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 329 VTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELM--ARCEhdplYPkSLKDAKAwILTEERPHKMENGD--PK 404
Cdd:cd05067 158 YTAREGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVthGRIP----YP-GMTNPEV-IQNLERGYRMPRPDncPE 231
                       250       260       270
                ....*....|....*....|....*....|.
gi 17542550 405 ELMVLIDACCERNPNERLNFNTVKRQITDIY 435
Cdd:cd05067 232 ELYQLMRLCWKERPEDRPTFEYLRSVLEDFF 262
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
171-373 2.82e-42

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: 152.44  E-value: 2.82e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 171 IH-STINLDKKLGCGAFGEVFKGQYKAVGSTNPPieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEE 249
Cdd:cd05063   2 IHpSHITKQKVIGAGEFGEVFRGILKMPGRKEVA--VAIKTLKPGYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 250 PIMVVMELVTGGDLRKYLQTTQ-NIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSL---- 324
Cdd:cd05063  80 PAMIITEYMENGALDKYLRDHDgEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRvled 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17542550 325 --QGTEVTTKNleKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCE 373
Cdd:cd05063 160 dpEGTYTTSGG--KIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSFGE 208
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
173-427 3.67e-42

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: 151.94  E-value: 3.67e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 173 STINLDKKLGCGAFGEVFKGQYKAVGSTNPPieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIM 252
Cdd:cd05066   4 SCIKIEKVIGAGEFGEVCSGRLKLPGKREIP--VAIKTLKAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYLQTTQ-NIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSL----QGT 327
Cdd:cd05066  82 IVTEYMENGSLDAFLRKHDgQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRvledDPE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 328 EVTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHdPLYPKSLKDAKAWILTEER-PHKMenGDPKEL 406
Cdd:cd05066 162 AAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGER-PYWEMSNQDVIKAIEEGYRlPAPM--DCPAAL 238
                       250       260
                ....*....|....*....|.
gi 17542550 407 MVLIDACCERNPNERLNFNTV 427
Cdd:cd05066 239 HQLMLDCWQKDRNERPKFEQI 259
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
177-424 9.16e-42

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: 151.87  E-value: 9.16e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVL-QHENIVAFYGFASLEEPIMVVM 255
Cdd:cd05055  39 FGKTLGAGAFGKVVEATAYGLSKSDAVMKVAVKMLKPTAHSSEREALMSELKIMSHLgNHENIVNLLGACTIGGPILVIT 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRKYLQTTQN--IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS---LQGTEVT 330
Cdd:cd05055 119 EYCCYGDLLNFLRRKREsfLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLArdiMNDSNYV 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 331 TKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMArCEHDPlYPKSLKDAKAWILTeERPHKMENGD--PKELMV 408
Cdd:cd05055 199 VKGNARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFS-LGSNP-YPGMPVDSKFYKLI-KEGYRMAQPEhaPAEIYD 275
                       250
                ....*....|....*.
gi 17542550 409 LIDACCERNPNERLNF 424
Cdd:cd05055 276 IMKTCWDADPLKRPTF 291
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
179-424 3.34e-41

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: 150.18  E-value: 3.34e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFkgQYKAVGST-------------NPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFA 245
Cdd:cd05051  11 EKLGEGQFGEVH--LCEANGLSdltsddfigndnkDEPVLVAVKMLRPDASKNAREDFLKEVKIMSQLKDPNIVRLLGVC 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 246 SLEEPIMVVMELVTGGDLRKYLQ-------TTQNIPKLQI-----LWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDL 313
Cdd:cd05051  89 TRDEPLCMIVEYMENGDLNQFLQkheaetqGASATNSKTLsygtlLYMATQIASGMKYLESLNFVHRDLATRNCLVGPNY 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 314 KAKISDFGLS----------LQGTEVTtknlekaPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHDP---LYPK 380
Cdd:cd05051 169 TIKIADFGMSrnlysgdyyrIEGRAVL-------PIRWMAWESILLGKFTTKSDVWAFGVTLWEILTLCKEQPyehLTDE 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 17542550 381 SL--------KDAKAWILTeERPHkmenGDPKELMVLIDACCERNPNERLNF 424
Cdd:cd05051 242 QVienageffRDDGMEVYL-SRPP----NCPKEIYELMLECWRRDEEDRPTF 288
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
175-434 3.66e-41

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: 148.98  E-value: 3.66e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKAVgstnppiEVAVKRILGNAKrkqIQEFCNEAQIMTVLQHENIVAFYGFASLEE-PIMV 253
Cdd:cd05082   8 LKLLQTIGKGEFGDVMLGDYRGN-------KVAVKCIKNDAT---AQAFLAEASVMTQLRHSNLVQLLGVIVEEKgGLYI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQN--IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTevTT 331
Cdd:cd05082  78 VTEYMAKGSLVDYLRSRGRsvLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEAS--ST 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 332 KNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTEL--MARCEhdplYPK-SLKDAKAWIlteERPHKME--NGDPKEL 406
Cdd:cd05082 156 QDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIysFGRVP----YPRiPLKDVVPRV---EKGYKMDapDGCPPAV 228
                       250       260
                ....*....|....*....|....*...
gi 17542550 407 MVLIDACCERNPNERLNFNTVKRQITDI 434
Cdd:cd05082 229 YDVMKNCWHLDAAMRPSFLQLREQLEHI 256
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
173-427 7.59e-41

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: 148.48  E-value: 7.59e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 173 STINLDKKLGCGAFGEVFKGQYKAVGSTNppIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIM 252
Cdd:cd05065   4 SCVKIEEVIGAGEFGEVCRGRLKLPGKRE--IFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYL-QTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTT 331
Cdd:cd05065  82 IITEFMENGALDSFLrQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDTS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 332 KNLE------KAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHdPLYPKSLKDAKAWILTEER-PHKMENgdPK 404
Cdd:cd05065 162 DPTYtsslggKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGER-PYWDMSNQDVINAIEQDYRlPPPMDC--PT 238
                       250       260
                ....*....|....*....|...
gi 17542550 405 ELMVLIDACCERNPNERLNFNTV 427
Cdd:cd05065 239 ALHQLMLDCWQKDRNLRPKFGQI 261
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
179-433 1.42e-40

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: 146.99  E-value: 1.42e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKavGSTNppieVAVKRIlgNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASlEEPIMVVMELV 258
Cdd:cd14203   1 VKLGQGCFGEVWMGTWN--GTTK----VAIKTL--KPGTMSPEAFLEEAQIMKKLRHDKLVQLYAVVS-EEPIYIVTEFM 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTT--QNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEVTTKNL 334
Cdd:cd14203  72 SKGSLLDFLKDGegKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLArlIEDNEYTARQG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 335 EKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHDplYPKSLKDAkawILTE-ERPHKME--NGDPKELMVLID 411
Cdd:cd14203 152 AKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVP--YPGMNNRE---VLEQvERGYRMPcpPGCPESLHELMC 226
                       250       260
                ....*....|....*....|..
gi 17542550 412 ACCERNPNERLNFNTVKRQITD 433
Cdd:cd14203 227 QCWRKDPEERPTFEYLQSFLED 248
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
175-433 1.85e-40

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: 147.87  E-value: 1.85e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:cd05062   8 ITMSRELGQGSFGMVYEGIAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVI 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQT---------TQNIPKL-QILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSL 324
Cdd:cd05062  88 MELMTRGDLKSYLRSlrpemennpVQAPPSLkKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTR 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 325 QGTEvtTKNLEKA-----PIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHdPLYPKSLKDAKAWILTEERPHKME 399
Cdd:cd05062 168 DIYE--TDYYRKGgkgllPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQ-PYQGMSNEQVLRFVMEGGLLDKPD 244
                       250       260       270
                ....*....|....*....|....*....|....
gi 17542550 400 NGdPKELMVLIDACCERNPNERLNFNTVKRQITD 433
Cdd:cd05062 245 NC-PDMLFELMRMCWQYNPKMRPSFLEIISSIKE 277
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
177-434 8.19e-40

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: 145.76  E-value: 8.19e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGSTNppIEVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFA----SLEEPI 251
Cdd:cd05035   3 LGKILGEGEFGSVMEAQLKQDDGSQ--LKVAVKTMkVDIHTYSEIEEFLSEAACMKDFDHPNVMRLIGVCftasDLNKPP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 --MVVMELVTGGDLRKYLQTTQ------NIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS 323
Cdd:cd05035  81 spMVILPFMKHGDLHSYLLYSRlgglpeKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 324 ---LQGTEVTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEhDPlYPkSLKDAKAW--ILTEERPHKM 398
Cdd:cd05035 161 rkiYSGDYYRQGRISKMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATRGQ-TP-YP-GVENHEIYdyLRNGNRLKQP 237
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 17542550 399 ENGdPKELMVLIDACCERNPNERLNFNTVKRQITDI 434
Cdd:cd05035 238 EDC-LDEVYFLMYFCWTVDPKDRPTFTKLREVLENI 272
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
175-368 1.78e-39

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: 144.25  E-value: 1.78e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEV----FKGQYkavgstnppiEVAVKRILGNAKRKQiqEFCNEAQIMTVLQHENIVAFYGFASLEEP 250
Cdd:cd05113   6 LTFLKELGTGQFGVVkygkWRGQY----------DVAIKMIKEGSMSED--EFIEEAKVMMNLSHEKLVQLYGVCTKQRP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMELVTGGDLRKYLQTTQNIPKL-QILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGT 327
Cdd:cd05113  74 IFIITEYMANGCLLNYLREMRKRFQTqQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSryVLDD 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 17542550 328 EVTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTEL 368
Cdd:cd05113 154 EYTSSVGSKFPVRWSPPEVLMYSKFSSKSDVWAFGVLMWEV 194
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
173-433 4.98e-39

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: 143.24  E-value: 4.98e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 173 STINLDKKLGCGAFGEVFKGQYkavgstNPPIEVAVKRIlgNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASlEEPIM 252
Cdd:cd05073  11 ESLKLEKKLGAGQFGEVWMATY------NKHTKVAVKTM--KPGSMSVEAFLAEANVMKTLQHDKLVKLHAVVT-KEPIY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYLQT----TQNIPKLqiLWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQG 326
Cdd:cd05073  82 IITEFMAKGSLLDFLKSdegsKQPLPKL--IDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLArvIED 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 327 TEVTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHDplYPkSLKDAKAwILTEERPHKMENGD--PK 404
Cdd:cd05073 160 NEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIP--YP-GMSNPEV-IRALERGYRMPRPEncPE 235
                       250       260
                ....*....|....*....|....*....
gi 17542550 405 ELMVLIDACCERNPNERLNFNTVKRQITD 433
Cdd:cd05073 236 ELYNIMMRCWKNRPEERPTFEYIQSVLDD 264
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
177-421 1.12e-38

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: 142.34  E-value: 1.12e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQykavgSTNPPIEVAVKRILGN--AKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:cd14014   4 LVRLLGRGGMGEVYRAR-----DTLLGRPVAIKVLRPElaEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEVTTK 332
Cdd:cd14014  79 MEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIAraLGDSGLTQT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 333 NLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELmarCEHDPLYPKSLKDAKAWILTEERPHKMEN---GDPKELMVL 409
Cdd:cd14014 159 GSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYEL---LTGRPPFDGDSPAAVLAKHLQEAPPPPSPlnpDVPPALDAI 235
                       250
                ....*....|..
gi 17542550 410 IDACCERNPNER 421
Cdd:cd14014 236 ILRALAKDPEER 247
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
179-421 1.12e-38

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: 142.27  E-value: 1.12e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMEL 257
Cdd:cd06606   6 ELLGKGSFGSVYLALNLDTGE-----LMAVKEVeLSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLEKA 337
Cdd:cd06606  81 VPGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIATGEGTKS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 338 PI---RWLAPESLKSGMFNEKTDVWSYGVFLTElMARCEHdPLYpkSLKDAKAWIL----TEERPHKMENGDPkELMVLI 410
Cdd:cd06606 161 LRgtpYWMAPEVIRGEGYGRAADIWSLGCTVIE-MATGKP-PWS--ELGNPVAALFkigsSGEPPPIPEHLSE-EAKDFL 235
                       250
                ....*....|.
gi 17542550 411 DACCERNPNER 421
Cdd:cd06606 236 RKCLQRDPKKR 246
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
175-427 4.25e-38

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: 141.72  E-value: 4.25e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKrILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:cd05093   7 IVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVK-TLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYL-------------QTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFG 321
Cdd:cd05093  86 FEYMKHGDLNKFLrahgpdavlmaegNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 322 LSlqgTEVTTKNLEKA------PIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHdPLYPKSLKDAKAWIlTEERP 395
Cdd:cd05093 166 MS---RDVYSTDYYRVgghtmlPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQ-PWYQLSNNEVIECI-TQGRV 240
                       250       260       270
                ....*....|....*....|....*....|..
gi 17542550 396 HKMENGDPKELMVLIDACCERNPNERLNFNTV 427
Cdd:cd05093 241 LQRPRTCPKEVYDLMLGCWQREPHMRLNIKEI 272
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
177-424 9.69e-38

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: 141.26  E-value: 9.69e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGSTNP--PIEVAVKRILGNAKRKQIQEFCNEAQIMTVL-QHENIVAFYGFASLEEPIMV 253
Cdd:cd05099  16 LGKPLGEGCFGQVVRAEAYGIDKSRPdqTVTVAVKMLKDNATDKDLADLISEMELMKLIgKHKNIINLLGVCTQEGPLYV 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQT--------TQNIPKL--QILWF------AMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKI 317
Cdd:cd05099  96 IVEYAAKGNLREFLRArrppgpdyTFDITKVpeEQLSFkdlvscAYQVARGMEYLESRRCIHRDLAARNVLVTEDNVMKI 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 318 SDFGLSLQGTEV----TTKNlEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMArCEHDPlYPKSLKDAKAWILTEE 393
Cdd:cd05099 176 ADFGLARGVHDIdyykKTSN-GRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFT-LGGSP-YPGIPVEELFKLLREG 252
                       250       260       270
                ....*....|....*....|....*....|...
gi 17542550 394 rpHKMENGD--PKELMVLIDACCERNPNERLNF 424
Cdd:cd05099 253 --HRMDKPSncTHELYMLMRECWHAVPTQRPTF 283
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
169-434 1.29e-37

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: 140.07  E-value: 1.29e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 169 VLIHSTINLDKKLGCGAFGEVFKGQYKAVGSTnpPIEVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFA-- 245
Cdd:cd14204   3 MIDRNLLSLGKVLGEGEFGSVMEGELQQPDGT--NHKVAVKTMkLDNFSQREIEEFLSEAACMKDFNHPNVIRLLGVCle 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 246 ----SLEEPiMVVMELVTGGDLRKYL------QTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKA 315
Cdd:cd14204  81 vgsqRIPKP-MVILPFMKYGDLHSFLlrsrlgSGPQHVPLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 316 KISDFGLS---LQGTEVTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARcEHDPlYPKSLKDAKAWILTE 392
Cdd:cd14204 160 CVADFGLSkkiYSGDYYRQGRIAKMPVKWIAVESLADRVYTVKSDVWAFGVTMWEIATR-GMTP-YPGVQNHEIYDYLLH 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 17542550 393 ERPHKMENGDPKELMVLIDACCERNPNERLNFNTVKRQITDI 434
Cdd:cd14204 238 GHRLKQPEDCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKL 279
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
179-421 1.40e-37

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: 138.88  E-value: 1.40e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRILGNAKRKQiQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd05122   6 EKIGKGGFGVVYKARHKKTGQ-----IVAIKKINLESKEKK-ESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFC 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTT-QNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGT-EVTTKNLEK 336
Cdd:cd05122  80 SGGSLKDLLKNTnKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSdGKTRNTFVG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 337 APIrWLAPESLKSGMFNEKTDVWSYGVFLTElMARCE---HDPLYPKSLKdakaWILTE-----ERPHKMEngdpKELMV 408
Cdd:cd05122 160 TPY-WMAPEVIQGKPYGFKADIWSLGITAIE-MAEGKppySELPPMKALF----LIATNgppglRNPKKWS----KEFKD 229
                       250
                ....*....|...
gi 17542550 409 LIDACCERNPNER 421
Cdd:cd05122 230 FLKKCLQKDPEKR 242
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
181-437 2.64e-37

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: 138.76  E-value: 2.64e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYkaVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPI-MVVMELVT 259
Cdd:cd05058   3 IGKGHFGCVYHGTL--IDSDGQKIHCAVKSLNRITDIEEVEQFLKEGIIMKDFSHPNVLSLLGICLPSEGSpLVVLPYMK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 260 GGDLRKYLQTTQNIPKLQ-ILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTE-----VTTKN 333
Cdd:cd05058  81 HGDLRNFIRSETHNPTVKdLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIYDkeyysVHNHT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 334 LEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEhdPLYPK-SLKDAKAWILTEERPHKMENGdPKELMVLIDA 412
Cdd:cd05058 161 GAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGA--PPYPDvDSFDITVYLLQGRRLLQPEYC-PDPLYEVMLS 237
                       250       260
                ....*....|....*....|....*
gi 17542550 413 CCERNPNERLNFNTVKRQITDIYME 437
Cdd:cd05058 238 CWHPKPEMRPTFSELVSRISQIFST 262
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
175-429 2.92e-37

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: 139.38  E-value: 2.92e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKrILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:cd05094   7 IVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVK-TLKDPTLAARKDFQREAELLTNLQHDHIVKFYGVCGDGDPLIMV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYL----------------QTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKIS 318
Cdd:cd05094  86 FEYMKHGDLNKFLrahgpdamilvdgqprQAKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 319 DFGLSlqgTEVTTKNLEKA------PIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHD--PLYPKSLKDAKAWIL 390
Cdd:cd05094 166 DFGMS---RDVYSTDYYRVgghtmlPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPwfQLSNTEVIECITQGR 242
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 17542550 391 TEERPHKMengdPKELMVLIDACCERNPNERLNFNTVKR 429
Cdd:cd05094 243 VLERPRVC----PKEVYDIMLGCWQREPQQRLNIKEIYK 277
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
174-435 3.12e-37

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: 139.05  E-value: 3.12e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 174 TINLDKKLGCGAFGEVFKGQYkavgstNPPIEVAVKRIlgNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASlEEPIMV 253
Cdd:cd05069  13 SLRLDVKLGQGCFGEVWMGTW------NGTTKVAIKTL--KPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVS-EEPIYI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTT--QNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEV 329
Cdd:cd05069  84 VTEFMGKGSLLDFLKEGdgKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLArlIEDNEY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 TTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHDplYPKSLKdaKAWILTEERPHKM--ENGDPKELM 407
Cdd:cd05069 164 TARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVP--YPGMVN--REVLEQVERGYRMpcPQGCPESLH 239
                       250       260
                ....*....|....*....|....*...
gi 17542550 408 VLIDACCERNPNERLNFNTVKRQITDIY 435
Cdd:cd05069 240 ELMKLCWKKDPDERPTFEYIQSFLEDYF 267
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
179-434 3.66e-37

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: 139.00  E-value: 3.66e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTNPPIeVAVKRiLGNAKRKQIQEFCNEAQIMTVLQHENIVAFYG--FASLEEPIMVVME 256
Cdd:cd14205  10 QQLGKGNFGSVEMCRYDPLQDNTGEV-VAVKK-LQHSTEEHLRDFEREIEILKSLQHDNIVKYKGvcYSAGRRNLRLIME 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQN-IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSL---QGTE-VTT 331
Cdd:cd14205  88 YLPYGSLRDYLQKHKErIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKvlpQDKEyYKV 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 332 KNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHDPLYPKSL-----KDAKAWILTEERPHKMEN------ 400
Cdd:cd14205 168 KEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIEKSKSPPAEFmrmigNDKQGQMIVFHLIELLKNngrlpr 247
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 17542550 401 --GDPKELMVLIDACCERNPNERLNFNTVKRQITDI 434
Cdd:cd14205 248 pdGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQI 283
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
173-432 4.81e-37

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: 137.77  E-value: 4.81e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 173 STINLDKKLGCGAFGEVFKGQYKavgstnPPIEVAVKRILGNAKRKQiqEFCNEAQIMTVLQHENIVAFYGFASLEEPIM 252
Cdd:cd05112   4 SELTFVQEIGSGQFGLVHLGYWL------NKDKVAIKTIREGAMSEE--DFIEEAEVMMKLSHPKLVQLYGVCLEQAPIC 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYLQTTQN-IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEV 329
Cdd:cd05112  76 LVFEFMEHGCLSDYLRTQRGlFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTrfVLDDQY 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 TTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHdPLYPKSLKDAKAWILTEERPHKMENGdPKELMVL 409
Cdd:cd05112 156 TSSTGTKFPVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKI-PYENRSNSEVVEDINAGFRLYKPRLA-STHVYEI 233
                       250       260
                ....*....|....*....|...
gi 17542550 410 IDACCERNPNERLNFNTVKRQIT 432
Cdd:cd05112 234 MNHCWKERPEDRPSFSLLLRQLA 256
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
179-435 1.11e-36

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: 136.63  E-value: 1.11e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTNPpieVAVKRILGNAKRKQIQ-EFCNEAQIMTVLQHENIVAFYGFASlEEPIMVVMEL 257
Cdd:cd05116   1 GELGSGNFGTVKKGYYQMKKVVKT---VAVKILKNEANDPALKdELLREANVMQQLDNPYIVRMIGICE-AESWMLVMEM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTE--VTTKN 333
Cdd:cd05116  77 AELGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSkaLRADEnyYKAQT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 334 LEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEhdplypKSLKDAKAWILTE--ERPHKME--NGDPKELMVL 409
Cdd:cd05116 157 HGKWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSYGQ------KPYKGMKGNEVTQmiEKGERMEcpAGCPPEMYDL 230
                       250       260
                ....*....|....*....|....*.
gi 17542550 410 IDACCERNPNERLNFNTVKRQITDIY 435
Cdd:cd05116 231 MKLCWTYDVDERPGFAAVELRLRNYY 256
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
177-376 1.33e-36

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: 137.80  E-value: 1.33e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVF----KGQYKAVGSTNP-----PIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASL 247
Cdd:cd05097   9 LKEKLGEGQFGEVHlceaEGLAEFLGEGAPefdgqPVLVAVKMLRADVTKTARNDFLKEIKIMSRLKNPNIIRLLGVCVS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 248 EEPIMVVMELVTGGDLRKYLQTTQ---------NIPKLQI---LWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKA 315
Cdd:cd05097  89 DDPLCMITEYMENGDLNQFLSQREiestfthanNIPSVSIanlLYMAVQIASGMKYLASLNFVHRDLATRNCLVGNHYTI 168
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17542550 316 KISDFGLS----------LQGTEVTtknlekaPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHDP 376
Cdd:cd05097 169 KIADFGMSrnlysgdyyrIQGRAVL-------PIRWMAWESILLGKFTTASDVWAFGVTLWEMFTLCKEQP 232
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
178-435 1.34e-36

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: 137.00  E-value: 1.34e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 178 DKKLGCGAFGEVFKGQYKAvgsTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASlEEPIMVVMEL 257
Cdd:cd05115   9 EVELGSGNFGCVKKGVYKM---RKKQIDVAIKVLKQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVCE-AEALMLVMEM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTQN-IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS----LQGTEVTTK 332
Cdd:cd05115  85 ASGGPLNKFLSGKKDeITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSkalgADDSYYKAR 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 333 NLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEhDPLypKSLKDAKAwILTEERPHKME--NGDPKELMVLI 410
Cdd:cd05115 165 SAGKWPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSYGQ-KPY--KKMKGPEV-MSFIEQGKRMDcpAECPPEMYALM 240
                       250       260
                ....*....|....*....|....*
gi 17542550 411 DACCERNPNERLNFNTVKRQITDIY 435
Cdd:cd05115 241 SDCWIYKWEDRPNFLTVEQRMRTYY 265
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
175-429 1.34e-36

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: 137.27  E-value: 1.34e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:cd05050   7 IEYVRDIGQGAFGRVFQARAPGLLPYEPFTMVAVKMLKEEASADMQADFQREAALMAEFDHPNIVKLLGVCAVGKPMCLL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQ-----------------TTQNIPKLQI-----LWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQD 312
Cdd:cd05050  87 FEYMAYGDLNEFLRhrspraqcslshstssaRKCGLNPLPLscteqLCIAKQVAAGMAYLSERKFVHRDLATRNCLVGEN 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 313 LKAKISDFGLSlqgTEVTTKNLEKA------PIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHdPLYPKSLKDAK 386
Cdd:cd05050 167 MVVKIADFGLS---RNIYSADYYKAsendaiPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGMQ-PYYGMAHEEVI 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 17542550 387 AWIlTEERPHKMENGDPKELMVLIDACCERNPNERLNFNTVKR 429
Cdd:cd05050 243 YYV-RDGNVLSCPDNCPLELYNLMRLCWSKLPSDRPSFASINR 284
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
177-421 5.33e-36

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 140.15  E-value: 5.33e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGStnppiEVAVKRILGNAKR--KQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:COG0515  11 ILRLLGRGGMGVVYLARDLRLGR-----PVALKVLRPELAAdpEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEVTTK 332
Cdd:COG0515  86 MEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIAraLGGATLTQT 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 333 NLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARceHDPLYPKSLKDAKAWILTEE--RPHKMENGDPKELMVLI 410
Cdd:COG0515 166 GTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTG--RPPFDGDSPAELLRAHLREPppPPSELRPDLPPALDAIV 243
                       250
                ....*....|.
gi 17542550 411 DACCERNPNER 421
Cdd:COG0515 244 LRALAKDPEER 254
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
174-435 2.41e-35

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: 133.66  E-value: 2.41e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 174 TINLDKKLGCGAFGEVFKGQYkavgstNPPIEVAVKRIlgNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASlEEPIMV 253
Cdd:cd05071  10 SLRLEVKLGQGCFGEVWMGTW------NGTTRVAIKTL--KPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVS-EEPIYI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYL--QTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEV 329
Cdd:cd05071  81 VTEYMSKGSLLDFLkgEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLArlIEDNEY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 TTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELM--ARCEHDPLYPKSLKDAKawilteERPHKMENGD--PKE 405
Cdd:cd05071 161 TARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTtkGRVPYPGMVNREVLDQV------ERGYRMPCPPecPES 234
                       250       260       270
                ....*....|....*....|....*....|
gi 17542550 406 LMVLIDACCERNPNERLNFNTVKRQITDIY 435
Cdd:cd05071 235 LHDLMCQCWRKEPEERPTFEYLQAFLEDYF 264
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
181-424 4.11e-35

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: 132.23  E-value: 4.11e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGstnppiEVAVKRILGNAKRKQiqEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd14065   1 LGKGFFGEVYKVTHRETG------KVMVMKELKRFDEQR--SFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQT-TQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAK---ISDFGLS-LQGTEVTTKNLE 335
Cdd:cd14065  73 GTLEELLKSmDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRnavVADFGLArEMPDEKTKKPDR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 336 KAPIR------WLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHDPLYpksLKDAKAWILTEERPHKMENGD-PKELMV 408
Cdd:cd14065 153 KKRLTvvgspyWMAPEMLRGESYDEKVDVFSFGIVLCEIIGRVPADPDY---LPRTMDFGLDVRAFRTLYVPDcPPSFLP 229
                       250
                ....*....|....*.
gi 17542550 409 LIDACCERNPNERLNF 424
Cdd:cd14065 230 LAIRCCQLDPEKRPSF 245
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
175-434 4.51e-35

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: 132.82  E-value: 4.51e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKAVGSTnppIEVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFA-------S 246
Cdd:cd05075   2 LALGKTLGEGEFGSVMEGQLNQDDSV---LKVAVKTMkIAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVClqnteseG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 247 LEEPImVVMELVTGGDLRKYL------QTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDF 320
Cdd:cd05075  79 YPSPV-VILPFMKHGDLHSFLlysrlgDCPVYLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 321 GLS---LQGTEVTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHDplYPkSLKDAKAWILTEERPHK 397
Cdd:cd05075 158 GLSkkiYNGDYYRQGRISKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATRGQTP--YP-GVENSEIYDYLRQGNRL 234
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 17542550 398 MENGDPKE-LMVLIDACCERNPNERLNFNTVKRQITDI 434
Cdd:cd05075 235 KQPPDCLDgLYELMSSCWLLNPKDRPSFETLRCELEKI 272
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
181-436 1.15e-34

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: 131.48  E-value: 1.15e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGstnppiEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd14154   1 LGKGFFGQAIKVTHRETG------EVMVMKELIRFDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQT-TQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS----------LQGTEV 329
Cdd:cd14154  75 GTLKDVLKDmARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLArliveerlpsGNMSPS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 TTKNLEKAPIR-----------WLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHDPLYPKSLKDAKawILTEERPHKM 398
Cdd:cd14154 155 ETLRHLKSPDRkkrytvvgnpyWMAPEMLNGRSYDEKVDIFSFGIVLCEIIGRVEADPDYLPRTKDFG--LNVDSFREKF 232
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 17542550 399 ENGDPKELMVLIDACCERNPNERLNFNTVKRQITDIYM 436
Cdd:cd14154 233 CAGCPPPFFKLAFLCCDLDPEKRPPFETLEEWLEALYL 270
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
175-429 1.18e-34

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: 132.42  E-value: 1.18e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEV----------FKGQYKAV-GSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYG 243
Cdd:cd05095   7 LTFKEKLGEGQFGEVhlceaegmekFMDKDFALeVSENQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIRLLA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 244 FASLEEPIMVVMELVTGGDLRKYL--QTTQNIPKL----------QILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQ 311
Cdd:cd05095  87 VCITDDPLCMITEYMENGDLNQFLsrQQPEGQLALpsnaltvsysDLRFMAAQIASGMKYLSSLNFVHRDLATRNCLVGK 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 312 DLKAKISDFGLS----------LQGTEVTtknlekaPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHDPLypKS 381
Cdd:cd05095 167 NYTIKIADFGMSrnlysgdyyrIQGRAVL-------PIRWMSWESILLGKFTTASDVWAFGVTLWETLTFCREQPY--SQ 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17542550 382 LKDAKAWILTEE--RPHKME------NGDPKELMVLIDACCERNPNERLNFNTVKR 429
Cdd:cd05095 238 LSDEQVIENTGEffRDQGRQtylpqpALCPDSVYKLMLSCWRRDTKDRPSFQEIHT 293
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
177-431 1.56e-34

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: 131.62  E-value: 1.56e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVME 256
Cdd:cd05045   4 LGKTLGEGEFGKVVKATAFRLKGRAGYTTVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLIVE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQNI------------------PKLQ------ILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQD 312
Cdd:cd05045  84 YAKYGSLRSFLRESRKVgpsylgsdgnrnssyldnPDERaltmgdLISFAWQISRGMQYLAEMKLVHRDLAARNVLVAEG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 313 LKAKISDFGLSLQGTE---VTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMArCEHDPlYPkSLKDAKAWI 389
Cdd:cd05045 164 RKMKISDFGLSRDVYEedsYVKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVT-LGGNP-YP-GIAPERLFN 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 17542550 390 LTEErPHKMENGD--PKELMVLIDACCERNPNERLNFNTVKRQI 431
Cdd:cd05045 241 LLKT-GYRMERPEncSEEMYNLMLTCWKQEPDKRPTFADISKEL 283
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
179-427 5.36e-34

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: 130.05  E-value: 5.36e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLE--EPIMVVME 256
Cdd:cd05079  10 RDLGEGHFGKVELCRYDPEGD-NTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIME 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQNIPKL-QILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGL--SLQGTE--VTT 331
Cdd:cd05079  89 FLPSGSLKEYLPRNKNKINLkQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLtkAIETDKeyYTV 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 332 KNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHD------------PLYPKSLKDAKAWILTEERPHKME 399
Cdd:cd05079 169 KDDLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTYCDSEsspmtlflkmigPTHGQMTVTRLVRVLEEGKRLPRP 248
                       250       260
                ....*....|....*....|....*...
gi 17542550 400 NGDPKELMVLIDACCERNPNERLNFNTV 427
Cdd:cd05079 249 PNCPEEVYQLMRKCWEFQPSKRTTFQNL 276
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
177-425 5.49e-34

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: 130.52  E-value: 5.49e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGSTNPP--IEVAVKRILGNAKRKQIQEFCNEAQIMTVL-QHENIVAFYGFASLEEPIMV 253
Cdd:cd05098  17 LGKPLGEGCFGQVVLAEAIGLDKDKPNrvTKVAVKMLKSDATEKDLSDLISEMEMMKMIgKHKNIINLLGACTQDGPLYV 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQT----------------TQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKI 317
Cdd:cd05098  97 IVEYASKGNLREYLQArrppgmeycynpshnpEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKI 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 318 SDFGLS-----LQGTEVTTKNleKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMArCEHDPlYPKSLKDAKAWILTE 392
Cdd:cd05098 177 ADFGLArdihhIDYYKKTTNG--RLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFT-LGGSP-YPGVPVEELFKLLKE 252
                       250       260       270
                ....*....|....*....|....*....|....*
gi 17542550 393 erPHKMENGD--PKELMVLIDACCERNPNERLNFN 425
Cdd:cd05098 253 --GHRMDKPSncTNELYMMMRDCWHAVPSQRPTFK 285
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
181-434 8.35e-34

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: 128.75  E-value: 8.35e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGstnppiEVAVKRIlgNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd14155   1 IGSGFFSEVYKVRHRTSG------QVMALKM--NTLSSNRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYING 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQD---LKAKISDFGLSLQGTEVTTKNlEKA 337
Cdd:cd14155  73 GNLEQLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDengYTAVVGDFGLAEKIPDYSDGK-EKL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 338 PI----RWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHDPLY-PKSLKDAKAWILTEErphkMENGDPKELMVLIDA 412
Cdd:cd14155 152 AVvgspYWMAPEVLRGEPYNEKADVFSYGIILCEIIARIQADPDYlPRTEDFGLDYDAFQH----MVGDCPPDFLQLAFN 227
                       250       260
                ....*....|....*....|..
gi 17542550 413 CCERNPNERLNFNTVKRQITDI 434
Cdd:cd14155 228 CCNMDPKSRPSFHDIVKTLEEI 249
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
181-431 1.21e-33

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: 129.24  E-value: 1.21e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTNPPIeVAVKRiLGNAKRKQIQEFCNEAQIMTVLQHENIVAFYG--FASLEEPIMVVMELV 258
Cdd:cd05081  12 LGKGNFGSVELCRYDPLGDNTGAL-VAVKQ-LQHSGPDQQRDFQREIQILKALHSDFIVKYRGvsYGPGRRSLRLVMEYL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQN-IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS----LQGTEVTTKN 333
Cdd:cd05081  90 PSGCLRDFLQRHRArLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAkllpLDKDYYVVRE 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 334 LEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHDPLYPKSL-------KDAKAW-----ILTEERPHKMENG 401
Cdd:cd05081 170 PGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTYCDKSCSPSAEFlrmmgceRDVPALcrlleLLEEGQRLPAPPA 249
                       250       260       270
                ....*....|....*....|....*....|
gi 17542550 402 DPKELMVLIDACCERNPNERLNFNTVKRQI 431
Cdd:cd05081 250 CPAEVHELMKLCWAPSPQDRPSFSALGPQL 279
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
174-435 1.21e-33

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: 129.03  E-value: 1.21e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 174 TINLDKKLGCGAFGEVFKGQYkavgstNPPIEVAVKRIlgNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASlEEPIMV 253
Cdd:cd05070  10 SLQLIKRLGNGQFGEVWMGTW------NGNTKVAIKTL--KPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVS-EEPIYI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQ----NIPKLQILwfAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGT 327
Cdd:cd05070  81 VTEYMSKGSLLDFLKDGEgralKLPNLVDM--AAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLArlIEDN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 328 EVTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEhdplYPKSLKDAKAWILTEERPHKM--ENGDPKE 405
Cdd:cd05070 159 EYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGR----VPYPGMNNREVLEQVERGYRMpcPQDCPIS 234
                       250       260       270
                ....*....|....*....|....*....|
gi 17542550 406 LMVLIDACCERNPNERLNFNTVKRQITDIY 435
Cdd:cd05070 235 LHELMIHCWKKDPEERPTFEYLQGFLEDYF 264
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
181-432 1.44e-33

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: 128.62  E-value: 1.44e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTnppIEVAVKRILGNAKRKQIQEFCNEAQIMTVL-QHENIVAFYGFASLEEPIMVVMELVT 259
Cdd:cd05047   3 IGEGNFGQVLKARIKKDGLR---MDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 260 GGDLRKYLQ----------------TTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS 323
Cdd:cd05047  80 HGNLLDFLRksrvletdpafaiansTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 324 lQGTEV-TTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMArCEHDPLYPKSLKDakawiLTEERPHKMENGD 402
Cdd:cd05047 160 -RGQEVyVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVS-LGGTPYCGMTCAE-----LYEKLPQGYRLEK 232
                       250       260       270
                ....*....|....*....|....*....|....
gi 17542550 403 PK----ELMVLIDACCERNPNERLNFNTVKRQIT 432
Cdd:cd05047 233 PLncddEVYDLMRQCWREKPYERPSFAQILVSLN 266
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
177-429 2.20e-33

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: 127.59  E-value: 2.20e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKavgSTNppIEVAVKRIlgnaKRKQIQEFCNEAQ------IMTVLQHENIVAFYGFASLEEP 250
Cdd:cd14007   4 IGKPLGKGKFGNVYLAREK---KSG--FIVALKVI----SKSQLQKSGLEHQlrreieIQSHLRHPNILRLYGYFEDKKR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS------- 323
Cdd:cd14007  75 IYLILEYAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSvhapsnr 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 324 ---LQGTevttknlekapIRWLAPESLKSGMFNEKTDVWSYGVFLTELMarCEHDPLYPKSLKDAKAWILTEErpHKMEN 400
Cdd:cd14007 155 rktFCGT-----------LDYLPPEMVEGKEYDYKVDIWSLGVLCYELL--VGKPPFESKSHQETYKRIQNVD--IKFPS 219
                       250       260
                ....*....|....*....|....*....
gi 17542550 401 GDPKELMVLIDACCERNPNERLNFNTVKR 429
Cdd:cd14007 220 SVSPEAKDLISKLLQKDPSKRLSLEQVLN 248
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
170-368 3.10e-33

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: 129.37  E-value: 3.10e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 170 LIHSTINLDKKLGCGAFGEVFKGQykAVG----STNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVL-QHENIVAFYGF 244
Cdd:cd05100   9 LSRTRLTLGKPLGEGCFGQVVMAE--AIGidkdKPNKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 245 ASLEEPIMVVMELVTGGDLRKYLQT-----------TQNIPKLQILW-----FAMNVASGMRHLSSKGIIHRDLAARNCL 308
Cdd:cd05100  87 CTQDGPLYVLVEYASKGNLREYLRArrppgmdysfdTCKLPEEQLTFkdlvsCAYQVARGMEYLASQKCIHRDLAARNVL 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17542550 309 VTQDLKAKISDFGLS-----LQGTEVTTKNleKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTEL 368
Cdd:cd05100 167 VTEDNVMKIADFGLArdvhnIDYYKKTTNG--RLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEI 229
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
173-370 3.87e-33

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: 127.82  E-value: 3.87e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 173 STINLDKKLGCGAFGEVFKGQYKAVGSTNPPIeVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIM 252
Cdd:cd05090   5 SAVRFMEELGECAFGKIYKGHLYLPGMDHAQL-VAIKTLKDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQPVC 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYL-----------------QTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKA 315
Cdd:cd05090  84 MLFEFMNQGDLHEFLimrsphsdvgcssdedgTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHV 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 316 KISDFGLSLQGTE-----VTTKNLekAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd05090 164 KISDLGLSREIYSsdyyrVQNKSL--LPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFS 221
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
179-421 3.96e-33

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: 126.94  E-value: 3.96e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGstnppIEVAVKRILGNAKRKQIqeFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd06614   6 EKIGEGASGEVYKATDRATG-----KEVAIKKMRLRKQNKEL--IINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLqtTQNIPKL---QILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTevttknlE 335
Cdd:cd06614  79 DGGSLTDII--TQNPVRMnesQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLT-------K 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 336 KAPIR--------WLAPESLKSGMFNEKTDVWSYGVFLTELMarcEHDPLYpKSLKDAKA-WILTEERPHKMENGDP--K 404
Cdd:cd06614 150 EKSKRnsvvgtpyWMAPEVIKRKDYGPKVDIWSLGIMCIEMA---EGEPPY-LEEPPLRAlFLITTKGIPPLKNPEKwsP 225
                       250
                ....*....|....*..
gi 17542550 405 ELMVLIDACCERNPNER 421
Cdd:cd06614 226 EFKDFLNKCLVKDPEKR 242
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
181-435 4.10e-33

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: 126.78  E-value: 4.10e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAvgstnppIEVAVKRILGNAKRKQIQEfcnEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd14058   1 VGRGSFGVVCKARWRN-------QIVAVKIIESESEKKAFEV---EVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEG 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQTTQNIPKL---QILWFAMNVASGMRHLSS---KGIIHRDLAARNCLVT-QDLKAKISDFGLSLQGTEVTTKN 333
Cdd:cd14058  71 GSLYNVLHGKEPKPIYtaaHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTnGGTVLKICDFGTACDISTHMTNN 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 334 leKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCE-HDPLYPKSLKDAKaWILTEERPhKMENGDPKELMVLIDA 412
Cdd:cd14058 151 --KGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKpFDHIGGPAFRIMW-AVHNGERP-PLIKNCPKPIESLMTR 226
                       250       260
                ....*....|....*....|...
gi 17542550 413 CCERNPNERLNFNTVKRQITDIY 435
Cdd:cd14058 227 CWSKDPEKRPSMKEIVKIMSHLM 249
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
168-435 5.70e-33

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: 127.34  E-value: 5.70e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 168 NVLI-HSTINLDKKLGCGAFGEVFKGQYKAvgSTNPPIEVAVKRILGNA-KRKQIQEFCNEAQIMTVLQHENIVAFYGfA 245
Cdd:cd05074   3 DVLIqEQQFTLGRMLGKGEFGSVREAQLKS--EDGSFQKVAVKMLKADIfSSSDIEEFLREAACMKEFDHPNVIKLIG-V 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 246 SLEE------PI-MVVMELVTGGDLRKYLQTTQ------NIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQD 312
Cdd:cd05074  80 SLRSrakgrlPIpMVILPFMKHGDLHTFLLMSRigeepfTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNEN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 313 LKAKISDFGLSLQ---GTEVTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEhDPLYPKSLKDAKAWI 389
Cdd:cd05074 160 MTVCVADFGLSKKiysGDYYRQGCASKLPVKWLALESLADNVYTTHSDVWAFGVTMWEIMTRGQ-TPYAGVENSEIYNYL 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 17542550 390 LTEERpHKMENGDPKELMVLIDACCERNPNERLNFNTVKRQITDIY 435
Cdd:cd05074 239 IKGNR-LKQPPDCLEDVYELMCQCWSPEPKCRPSFQHLRDQLELIW 283
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
179-395 1.27e-32

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: 125.65  E-value: 1.27e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGfaSLEEP--IMVVM 255
Cdd:cd08215   6 RVIGKGSFGSAYLVRRKSDGKL-----YVLKEIdLSNMSEKEREEALNEVKLLSKLKHPNIVKYYE--SFEENgkLCIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDL----RKYLQTTQNIPKLQIL-WFAmNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTE 328
Cdd:cd08215  79 EYADGGDLaqkiKKQKKKGQPFPEEQILdWFV-QICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISkvLESTT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 329 VTTKNLEKAPIrWLAPESLKSGMFNEKTDVWSYGVFLTELMA------------------RCEHDPL---YPKSLKDAKA 387
Cdd:cd08215 158 DLAKTVVGTPY-YLSPELCENKPYNYKSDIWALGCVLYELCTlkhpfeannlpalvykivKGQYPPIpsqYSSELRDLVN 236
                       250
                ....*....|.
gi 17542550 388 WILT---EERP 395
Cdd:cd08215 237 SMLQkdpEKRP 247
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
173-434 1.64e-32

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: 125.36  E-value: 1.64e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 173 STINLDKKLGCGAFGEVFKGQYKAvgstnpPIEVAVKRILGNAKRKQiqEFCNEAQIMTVLQHENIVAFYGFASLEEPIM 252
Cdd:cd05114   4 SELTFMKELGSGLFGVVRLGKWRA------QYKVAIKAIREGAMSEE--DFIEEAKVMMKLTHPKLVQLYGVCTQQKPIY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYLQTTQ-NIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEV 329
Cdd:cd05114  76 IVTEFMENGCLLNYLRQRRgKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTryVLDDQY 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 TTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHdPLYPKSLKDAKAWILTEER---PHKMengdPKEL 406
Cdd:cd05114 156 TSSSGAKFPVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEGKM-PFESKSNYEVVEMVSRGHRlyrPKLA----SKSV 230
                       250       260
                ....*....|....*....|....*...
gi 17542550 407 MVLIDACCERNPNERLNFNTVKRQITDI 434
Cdd:cd05114 231 YEVMYSCWHEKPEGRPTFADLLRTITEI 258
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
181-425 2.66e-32

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: 125.12  E-value: 2.66e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKavgsTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd14202  10 IGHGAFAVVFKGRHK----EKHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVT---------QDLKAKISDFGLS--LQGTEV 329
Cdd:cd14202  86 GDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrksnpNNIRIKIADFGFAryLQNNMM 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 TTkNLEKAPIrWLAPESLKSGMFNEKTDVWSYGVFLTE-LMARCEHDPLYPKSLKdakawiLTEERPHKMENGDPKE--- 405
Cdd:cd14202 166 AA-TLCGSPM-YMAPEVIMSQHYDAKADLWSIGTIIYQcLTGKAPFQASSPQDLR------LFYEKNKSLSPNIPREtss 237
                       250       260
                ....*....|....*....|.
gi 17542550 406 -LMVLIDACCERNPNERLNFN 425
Cdd:cd14202 238 hLRQLLLGLLQRNQKDRMDFD 258
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
184-369 6.37e-32

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: 124.10  E-value: 6.37e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 184 GAFGEVFKGQYKAVGSTNPpiEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFAS-LEEPIMVVMELVTGGD 262
Cdd:cd05043  17 GTFGRIFHGILRDEKGKEE--EVLVKTVKDHASEIQVTMLLQESSLLYGLSHQNLLPILHVCIeDGEKPMVLYPYMNWGN 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 263 LRKYLQ--------TTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSlqgtevttKNL 334
Cdd:cd05043  95 LKLFLQqcrlseanNPQALSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALS--------RDL 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17542550 335 -----------EKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd05043 167 fpmdyhclgdnENRPIKWMSLESLVNKEYSSASDVWSFGVLLWELM 212
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
181-434 7.19e-32

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: 123.92  E-value: 7.19e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVfkgqYKAVGSTNPPieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd14066   1 IGSGGFGTV----YKGVLENGTV--VAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQTTQNIPKL---QILWFAMNVASGMRHLSSKG---IIHRDLAARNCLVTQDLKAKISDFGLSLQGTE---VTT 331
Cdd:cd14066  75 GSLEDRLHCHKGSPPLpwpQRLKIAKGIARGLEYLHEECpppIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPsesVSK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 332 KNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMAR-------CEHDPL-----YPKSLKDAKAWILTEERPHKME 399
Cdd:cd14066 155 TSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGkpavdenRENASRkdlveWVESKGKEELEDILDKRLVDDD 234
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 17542550 400 NGDPKELMVLIDA---CCERNPNERLNFNTVKRQITDI 434
Cdd:cd14066 235 GVEEEEVEALLRLallCTRSDPSLRPSMKEVVQMLEKL 272
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
181-424 8.36e-32

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: 123.25  E-value: 8.36e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAvgstNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd14120   1 IGHGAFAVVFKGRHRK----KPDLPVAIKCITKKNLSKSQNLLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQ---------DLKAKISDFGLS--LQGtEV 329
Cdd:cd14120  77 GDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHnsgrkpspnDIRLKIADFGFArfLQD-GM 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 TTKNLEKAPIrWLAPESLKSGMFNEKTDVWSYGVFLTE-LMARCehdPLYPKSLKDAKAWIlteERPH----KMENGDPK 404
Cdd:cd14120 156 MAATLCGSPM-YMAPEVIMSLQYDAKADLWSIGTIVYQcLTGKA---PFQAQTPQELKAFY---EKNAnlrpNIPSGTSP 228
                       250       260
                ....*....|....*....|
gi 17542550 405 ELMVLIDACCERNPNERLNF 424
Cdd:cd14120 229 ALKDLLLGLLKRNPKDRIDF 248
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
170-434 8.42e-32

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: 123.50  E-value: 8.42e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 170 LIHSTINLDKKLGCGAFGEVFKGQYKAVGSTNPPieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEE 249
Cdd:cd05064   2 LDNKSIKIERILGTGRFGELCRGCLKLPSKRELP--VAIHTLRAGCSDKQRRGFLAEALTLGQFDHSNIVRLEGVITRGN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 250 PIMVVMELVTGGDLRKYLQTTQ-NIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFG-LSLQGT 327
Cdd:cd05064  80 TMMIVTEYMSNGALDSFLRKHEgQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCKISGFRrLQEDKS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 328 EVTTKNLE-KAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHdPLYPKSLKDAKAWILTEERPHKMENGdPKEL 406
Cdd:cd05064 160 EAIYTTMSgKSPVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSYGER-PYWDMSGQDVIKAVEDGFRLPAPRNC-PNLL 237
                       250       260
                ....*....|....*....|....*...
gi 17542550 407 MVLIDACCERNPNERLNFNtvkrQITDI 434
Cdd:cd05064 238 HQLMLDCWQKERGERPRFS----QIHSI 261
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
179-427 9.13e-32

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: 123.86  E-value: 9.13e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTNPPIeVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASL--EEPIMVVME 256
Cdd:cd05080  10 RDLGEGHFGKVSLYCYDPTNDGTGEM-VAVKALKADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEqgGKSLQLIME 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLqTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSL---QGTE-VTTK 332
Cdd:cd05080  89 YVPLGSLRDYL-PKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKavpEGHEyYRVR 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 333 NLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHDPLYPKSLKD----AKAWI----LTE--ERPHKMENGD 402
Cdd:cd05080 168 EDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSSQSPPTKFLEmigiAQGQMtvvrLIEllERGERLPCPD 247
                       250       260
                ....*....|....*....|....*..
gi 17542550 403 --PKELMVLIDACCERNPNERLNFNTV 427
Cdd:cd05080 248 kcPQEVYHLMKNCWETEASFRPTFENL 274
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
175-432 1.74e-31

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: 123.57  E-value: 1.74e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKAVGSTnppIEVAVKRILGNAKRKQIQEFCNEAQIMTVL-QHENIVAFYGFASLEEPIMV 253
Cdd:cd05089   4 IKFEDVIGEGNFGQVIKAMIKKDGLK---MNAAIKMLKEFASENDHRDFAGELEVLCKLgHHPNIINLLGACENRGYLYI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQ----------------TTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKI 317
Cdd:cd05089  81 AIEYAPYGNLLDFLRksrvletdpafakehgTASTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 318 SDFGLSlQGTEV-TTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMArCEHDPLYPKSLKDakawiLTEERPH 396
Cdd:cd05089 161 ADFGLS-RGEEVyVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVS-LGGTPYCGMTCAE-----LYEKLPQ 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 17542550 397 KMENGDPK----ELMVLIDACCERNPNERLNFNTVKRQIT 432
Cdd:cd05089 234 GYRMEKPRncddEVYELMRQCWRDRPYERPPFSQISVQLS 273
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
181-369 2.89e-31

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: 121.06  E-value: 2.89e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVgstnppiEVAVKRIlgnakRKQiqefcNEAQI--MTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd14059   1 LGSGAQGAVFLGKFRGE-------EVAVKKV-----RDE-----KETDIkhLRKLNHPNIIKFKGVCTQAPCYCILMEYC 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLEKAP 338
Cdd:cd14059  64 PYGQLYEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKSTKMSFAGT 143
                       170       180       190
                ....*....|....*....|....*....|.
gi 17542550 339 IRWLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd14059 144 VAWMAPEVIRNEPCSEKVDIWSFGVVLWELL 174
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
173-370 3.62e-31

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: 122.43  E-value: 3.62e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 173 STINLDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIM 252
Cdd:cd05091   6 SAVRFMEELGEDRFGKVYKGHLFGTAPGEQTQAVAIKTLKDKAEGPLREEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYL---------------QTTQN-IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAK 316
Cdd:cd05091  86 MIFSYCSHGDLHEFLvmrsphsdvgstdddKTVKStLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLNVK 165
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 317 ISDFGLSlqgTEVTTKNLEKA------PIRWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd05091 166 ISDLGLF---REVYAADYYKLmgnsllPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFS 222
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
179-433 6.34e-31

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: 121.97  E-value: 6.34e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKavgstNP----------------PIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFY 242
Cdd:cd05096  11 EKLGEGQFGEVHLCEVV-----NPqdlptlqfpfnvrkgrPLLVAVKILRPDANKNARNDFLKEVKILSRLKDPNIIRLL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 243 GFASLEEPIMVVMELVTGGDLRKYLQTTQNIPKLQ-------------------ILWFAMNVASGMRHLSSKGIIHRDLA 303
Cdd:cd05096  86 GVCVDEDPLCMITEYMENGDLNQFLSSHHLDDKEEngndavppahclpaisyssLLHVALQIASGMKYLSSLNFVHRDLA 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 304 ARNCLVTQDLKAKISDFGLS----------LQGTEVTtknlekaPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCE 373
Cdd:cd05096 166 TRNCLVGENLTIKIADFGMSrnlyagdyyrIQGRAVL-------PIRWMAWECILMGKFTTASDVWAFGVTLWEILMLCK 238
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 374 HDP---LYPKSLKDAKAWILTEE-------RPHKMengdPKELMVLIDACCERNPNERLNFNTVKRQITD 433
Cdd:cd05096 239 EQPygeLTDEQVIENAGEFFRDQgrqvylfRPPPC----PQGLYELMLQCWSRDCRERPSFSDIHAFLTE 304
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
179-431 9.57e-31

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: 120.86  E-value: 9.57e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGstnppIEVAVKRI-LGNAKRKQIQEFcNEAQIMTVLQHENIVAFYGFASLEEPIMVVMEL 257
Cdd:cd13996  12 ELLGSGGFGSVYKVRNKVDG-----VTYAIKKIrLTEKSSASEKVL-REVKALAKLNHPNIVRYYTAWVEEPPLYIQMEL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTQNIPKLQ---ILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLK-AKISDFGL--SLQGTEVTT 331
Cdd:cd13996  86 CEGGTLRDWIDRRNSSSKNDrklALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLqVKIGDFGLatSIGNQKREL 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 332 KNLEKAP-------------IRWLAPESLKSGMFNEKTDVWSYGVFLTELmarcehdpLYPKSLKDAKAWILTEER---- 394
Cdd:cd13996 166 NNLNNNNngntsnnsvgigtPLYASPEQLDGENYNEKADIYSLGIILFEM--------LHPFKTAMERSTILTDLRngil 237
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 17542550 395 PHKMENGDPKELMvLIDACCERNPNERLNFNTVKRQI 431
Cdd:cd13996 238 PESFKAKHPKEAD-LIQSLLSKNPEERPSAEQLLRSL 273
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
181-434 1.06e-30

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: 120.09  E-value: 1.06e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVgstnppiEVAVKrilgnAKRKQIQE--------FCNEAQIMTVLQHENIVAFYGfASLEEP-I 251
Cdd:cd14148   2 IGVGGFGKVYKGLWRGE-------EVAVK-----AARQDPDEdiavtaenVRQEARLFWMLQHPNIIALRG-VCLNPPhL 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 MVVMELVTGGDLRKYLQTTQNIPKLQILWfAMNVASGMRHLSSKG---IIHRDLAARNCLVTQ-----DLKA---KISDF 320
Cdd:cd14148  69 CLVMEYARGGALNRALAGKKVPPHVLVNW-AVQIARGMNYLHNEAivpIIHRDLKSSNILILEpiendDLSGktlKITDF 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 321 GLSLQGTEvTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMA----RCEHDPL---YPKSLKDakawiLTEE 393
Cdd:cd14148 148 GLAREWHK-TTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTgevpYREIDALavaYGVAMNK-----LTLP 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 17542550 394 RPHKMengdPKELMVLIDACCERNPNERLNFNTVKRQITDI 434
Cdd:cd14148 222 IPSTC----PEPFARLLEECWDPDPHGRPDFGSILKRLEDI 258
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
182-427 1.10e-30

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: 119.68  E-value: 1.10e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 182 GCGAFGEVFKGQYKAVGStnppiEVAVKRILgnakrkQIQEfcnEAQIMTVLQHENIVAFYGfASLEEP-IMVVMELVTG 260
Cdd:cd14060   2 GGGSFGSVYRAIWVSQDK-----EVAVKKLL------KIEK---EAEILSVLSHRNIIQFYG-AILEAPnYGIVTEYASY 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQT--TQNIPKLQILWFAMNVASGMRHLSSKG---IIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLe 335
Cdd:cd14060  67 GSLFDYLNSneSEEMDMDQIMTWATDIAKGMHYLHMEApvkVIHRDLKSRNVVIAADGVLKICDFGASRFHSHTTHMSL- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 336 KAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARceHDPLypKSLKDAK-AWILTE--ERPhKMENGDPKELMVLIDA 412
Cdd:cd14060 146 VGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTR--EVPF--KGLEGLQvAWLVVEknERP-TIPSSCPRSFAELMRR 220
                       250
                ....*....|....*
gi 17542550 413 CCERNPNERLNFNTV 427
Cdd:cd14060 221 CWEADVKERPSFKQI 235
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
181-434 1.44e-30

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: 119.81  E-value: 1.44e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVgstnppiEVAVKRILGNAKR---KQIQEFCNEAQIMTVLQHENIVAFYGfASLEEP-IMVVME 256
Cdd:cd14061   2 IGVGGFGKVYRGIWRGE-------EVAVKAARQDPDEdisVTLENVRQEARLFWMLRHPNIIALRG-VCLQPPnLCLVME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLqTTQNIPKLQILWFAMNVASGMRHLSSKG---IIHRDLAARNCLVTQDLKA--------KISDFGLSLQ 325
Cdd:cd14061  74 YARGGALNRVL-AGRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEAIENedlenktlKITDFGLARE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 326 GTEvTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELmarcehdplypkslkdakawiLTEERPHK-------- 397
Cdd:cd14061 153 WHK-TTRMSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWEL---------------------LTGEVPYKgidglava 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 17542550 398 -----------MENGDPKELMVLIDACCERNPNERLNFNTVKRQITDI 434
Cdd:cd14061 211 ygvavnkltlpIPSTCPEPFAQLMKDCWQPDPHDRPSFADILKQLENI 258
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
169-369 1.90e-30

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: 120.90  E-value: 1.90e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 169 VLIHSTINLDKKLGCGAFGEVFKGQYKAVGStNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFAsLE 248
Cdd:cd05108   3 ILKETEFKKIKVLGSGAFGTVYKGLWIPEGE-KVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGIC-LT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 249 EPIMVVMELVTGGDLRKYLQTTQ-NIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS-LQG 326
Cdd:cd05108  81 STVQLITQLMPFGCLLDYVREHKdNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAkLLG 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17542550 327 TEVTTKNLE--KAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd05108 161 AEEKEYHAEggKVPIKWMALESILHRIYTHQSDVWSYGVTVWELM 205
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
175-368 2.57e-30

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: 120.51  E-value: 2.57e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKAVGSTNP--PIEVAVKRILGNAKRKQIQEFCNEAQIMTVL-QHENIVAFYGFASLEEPI 251
Cdd:cd05101  26 LTLGKPLGEGCFGQVVMAEAVGIDKDKPkeAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPL 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 MVVMELVTGGDLRKYLQTTQ-----------NIPKLQILWFAM-----NVASGMRHLSSKGIIHRDLAARNCLVTQDLKA 315
Cdd:cd05101 106 YVIVEYASKGNLREYLRARRppgmeysydinRVPEEQMTFKDLvsctyQLARGMEYLASQKCIHRDLAARNVLVTENNVM 185
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17542550 316 KISDFGLSLQGTEV----TTKNlEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTEL 368
Cdd:cd05101 186 KIADFGLARDINNIdyykKTTN-GRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEI 241
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
176-365 2.85e-30

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: 119.12  E-value: 2.85e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 176 NLDKKLGCGAFGEVFKGQYKAVGStnppiEVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:cd05117   3 ELGKVLGRGSFGVVRLAVHKKTGE-----EYAVKIIdKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVT---QDLKAKISDFGLSlqgTEVTT 331
Cdd:cd05117  78 MELCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLAskdPDSPIKIIDFGLA---KIFEE 154
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 17542550 332 KNLEKAP---IRWLAPESLKSGMFNEKTDVWSYGVFL 365
Cdd:cd05117 155 GEKLKTVcgtPYYVAPEVLKGKGYGKKCDIWSLGVIL 191
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
181-424 3.13e-30

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: 119.28  E-value: 3.13e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGstnppiEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd14222   1 LGKGFFGQAIKVTHKATG------KVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS-LQGTEVTTKNLEKAPI 339
Cdd:cd14222  75 GTLKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSrLIVEEKKKPPPDKPTT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 340 R--------------------WLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHDP-LYPKSLK---DAKAWIlteerp 395
Cdd:cd14222 155 KkrtlrkndrkkrytvvgnpyWMAPEMLNGKSYDEKVDIFSFGIVLCEIIGQVYADPdCLPRTLDfglNVRLFW------ 228
                       250       260       270
                ....*....|....*....|....*....|
gi 17542550 396 HKMENGD-PKELMVLIDACCERNPNERLNF 424
Cdd:cd14222 229 EKFVPKDcPPAFFPLAAICCRLEPDSRPAF 258
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
181-436 3.47e-30

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: 118.91  E-value: 3.47e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGstnppiEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd14221   1 LGKGCFGQAIKVTHRETG------EVMVMKELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQTT-QNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTK-----NL 334
Cdd:cd14221  75 GTLRGIIKSMdSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDEKTQpeglrSL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 335 EKAPIR----------WLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHDPLY-PKSLK---DAKAWiLTEERPHKMen 400
Cdd:cd14221 155 KKPDRKkrytvvgnpyWMAPEMINGRSYDEKVDVFSFGIVLCEIIGRVNADPDYlPRTMDfglNVRGF-LDRYCPPNC-- 231
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 17542550 401 gdPKELMVLIDACCERNPNERLNFNTVKRQITDIYM 436
Cdd:cd14221 232 --PPSFFPIAVLCCDLDPEKRPSFSKLEHWLETLRM 265
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
177-368 6.88e-30

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: 117.71  E-value: 6.88e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQ-IQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVM 255
Cdd:cd06627   4 LGDLIGRGAFGSVYKGLNLNTGEF-----VAIKQISLEKIPKSdLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIIL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLE 335
Cdd:cd06627  79 EYVENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVEKDENS 158
                       170       180       190
                ....*....|....*....|....*....|....*
gi 17542550 336 KA--PiRWLAPESLKSGMFNEKTDVWSYGVFLTEL 368
Cdd:cd06627 159 VVgtP-YWMAPEVIEMSGVTTASDIWSVGCTVIEL 192
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
177-421 8.30e-30

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: 117.75  E-value: 8.30e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAkrkQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVME 256
Cdd:cd06612   7 ILEKLGEGSYGSVYKAIHKETGQV-----VAIKVVPVEE---DLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQ-NIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEVTTKN 333
Cdd:cd06612  79 YCGAGSVSDIMKITNkTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSgqLTDTMAKRNT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 334 LEKAPIrWLAPESLKSGMFNEKTDVWSYGVFLTElMArcEHDPLY----------------PKSLKDAKAWilteerphk 397
Cdd:cd06612 159 VIGTPF-WMAPEVIQEIGYNNKADIWSLGITAIE-MA--EGKPPYsdihpmraifmipnkpPPTLSDPEKW--------- 225
                       250       260
                ....*....|....*....|....
gi 17542550 398 mengdPKELMVLIDACCERNPNER 421
Cdd:cd06612 226 -----SPEFNDFVKKCLVKDPEER 244
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
175-434 2.25e-29

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: 117.59  E-value: 2.25e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVL-QHENIVAFYGFASLEE-PIM 252
Cdd:cd05054   9 LKLGKPLGRGAFGKVIQASAFGIDKSATCRTVAVKMLKEGATASEHKALMTELKILIHIgHHLNVVNLLGACTKPGgPLM 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYLQTTQNIPKLQ--------------------------ILWFAMNVASGMRHLSSKGIIHRDLAARN 306
Cdd:cd05054  89 VIVEFCKFGNLSNYLRSKREEFVPYrdkgardveeeedddelykepltledLICYSFQVARGMEFLASRKCIHRDLAARN 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 307 CLVTQDLKAKISDFGLS---LQGTEVTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMArCEHDPlYPKSLK 383
Cdd:cd05054 169 ILLSENNVVKICDFGLArdiYKDPDYVRKGDARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFS-LGASP-YPGVQM 246
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17542550 384 DakawiltEERPHKMENG--------DPKELMVLIDACCERNPNERLNFNTVKRQITDI 434
Cdd:cd05054 247 D-------EEFCRRLKEGtrmrapeyTTPEIYQIMLDCWHGEPKERPTFSELVEKLGDL 298
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
175-431 2.62e-29

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: 119.18  E-value: 2.62e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVL-QHENIVAFYGFASLEEPIMV 253
Cdd:cd05106  40 LQFGKTLGAGAFGKVVEATAFGLGKEDNVLRVAVKMLKASAHTDEREALMSELKILSHLgQHKNIVNLLGACTHGGPVLV 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQ--------NIPKL------------------------------------------------- 276
Cdd:cd05106 120 ITEYCCYGDLLNFLRKKAetflnfvmALPEIsetssdyknitlekkyirsdsgfssqgsdtyvemrpvsssssqssdskd 199
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 277 -------------QILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS---LQGTEVTTKNLEKAPIR 340
Cdd:cd05106 200 eedtedswpldldDLLRFSSQVAQGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFGLArdiMNDSNYVVKGNARLPVK 279
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 341 WLAPESLKSGMFNEKTDVWSYGVFLTELMArCEHDPlYPKSLKDAKAWILTeERPHKMENGD--PKELMVLIDACCERNP 418
Cdd:cd05106 280 WMAPESIFDCVYTVQSDVWSYGILLWEIFS-LGKSP-YPGILVNSKFYKMV-KRGYQMSRPDfaPPEIYSIMKMCWNLEP 356
                       330
                ....*....|...
gi 17542550 419 NERLNFNTVKRQI 431
Cdd:cd05106 357 TERPTFSQISQLI 369
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
181-426 3.61e-29

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: 116.26  E-value: 3.61e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKavgsTNPPIEVAVKRI-LGNAKRKQIQeFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVT 259
Cdd:cd14201  14 VGHGAFAVVFKGRHR----KKTDWEVAIKSInKKNLSKSQIL-LGKEIKILKELQHENIVALYDVQEMPNSVFLVMEYCN 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 260 GGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVT---------QDLKAKISDFGLS--LQgTE 328
Cdd:cd14201  89 GGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyasrkkssvSGIRIKIADFGFAryLQ-SN 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 329 VTTKNLEKAPIrWLAPESLKSGMFNEKTDVWSYGVFLTELMArcEHDPLYPKSLKDAKawiLTEERPHKMENGDPKE--- 405
Cdd:cd14201 168 MMAATLCGSPM-YMAPEVIMSQHYDAKADLWSIGTVIYQCLV--GKPPFQANSPQDLR---MFYEKNKNLQPSIPREtsp 241
                       250       260
                ....*....|....*....|..
gi 17542550 406 -LMVLIDACCERNPNERLNFNT 426
Cdd:cd14201 242 yLADLLLGLLQRNQKDRMDFEA 263
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
169-370 4.11e-29

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: 117.02  E-value: 4.11e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 169 VLIHSTINLDKKLGCGAFGEVFKGQYKAVGSTnppIEVAVKRILGNAKRKQIQEFCNEAQIMTVL-QHENIVAFYGFASL 247
Cdd:cd05088   3 VLEWNDIKFQDVIGEGNFGQVLKARIKKDGLR---MDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 248 EEPIMVVMELVTGGDLRKYLQ----------------TTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQ 311
Cdd:cd05088  80 RGYLYLAIEYAPHGNLLDFLRksrvletdpafaiansTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGE 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 312 DLKAKISDFGLSlQGTEV-TTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd05088 160 NYVAKIADFGLS-RGQEVyVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVS 218
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
179-430 5.35e-29

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: 115.20  E-value: 5.35e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMEL 257
Cdd:cd08529   6 NKLGKGSFGVVYKVVRKVDGRV-----YALKQIdISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYL--QTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGL--SLQGTEVTTKN 333
Cdd:cd08529  81 AENGDLHSLIksQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVakILSDTTNFAQT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 334 LEKAPIrWLAPESLKSGMFNEKTDVWSYGVFLTELmarCEHDplYPKSLKDAKAWILTEER----PhkMENGDPKELMVL 409
Cdd:cd08529 161 IVGTPY-YLSPELCEDKPYNEKSDVWALGCVLYEL---CTGK--HPFEAQNQGALILKIVRgkypP--ISASYSQDLSQL 232
                       250       260
                ....*....|....*....|.
gi 17542550 410 IDACCERNPNERLNFNTVKRQ 430
Cdd:cd08529 233 IDSCLTKDYRQRPDTTELLRN 253
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
181-431 5.75e-29

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: 115.18  E-value: 5.75e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVgstnppieVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASlEEPIMVVMELVT 259
Cdd:cd14062   1 IGSGSFGTVYKGRWHGD--------VAVKKLnVTDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYMT-KPQLAIVTQWCE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 260 GGDLRKYLQTTQN-IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLEKAP 338
Cdd:cd14062  72 GSSLYKHLHVLETkFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATVKTRWSGSQQFEQP 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 339 ---IRWLAPESLKsgM-----FNEKTDVWSYGVFLTELMARCehdplYPKSLKDAKAWILTEE-----RPH--KMENGDP 403
Cdd:cd14062 152 tgsILWMAPEVIR--MqdenpYSFQSDVYAFGIVLYELLTGQ-----LPYSHINNRDQILFMVgrgylRPDlsKVRSDTP 224
                       250       260
                ....*....|....*....|....*...
gi 17542550 404 KELMVLIDACCERNPNERLNFntvkRQI 431
Cdd:cd14062 225 KALRRLMEDCIKFQRDERPLF----PQI 248
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
181-370 6.05e-29

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: 115.01  E-value: 6.05e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGStnppiEVAVKRILGNAKRKQIQEFCN-EAQIMTVLQHENIVAFYGFASLEEPIMVVMELVT 259
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGE-----VVAIKEISRKKLNKKLQENLEsEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 260 GGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKA---KISDFGL--SLQ-GTEVTTkn 333
Cdd:cd14009  76 GGDLSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDpvlKIADFGFarSLQpASMAET-- 153
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 17542550 334 LEKAPIrWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd14009 154 LCGSPL-YMAPEILQFQKYDAKADLWSVGAILFEMLV 189
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
181-369 7.48e-29

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: 114.93  E-value: 7.48e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVgstnppiEVAVKRILGNA--KRKQIQEFCNEAQIMTVLQHENIVAFYGfASLEEP--IMVVME 256
Cdd:cd14064   1 IGSGSFGKVYKGRCRNK-------IVAIKRYRANTycSKSDVDMFCREVSILCRLNHPCVIQFVG-ACLDDPsqFAIVTQ 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQNIPKLQI-LWFAMNVASGMRHL--SSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKN 333
Cdd:cd14064  73 YVSGGSLFSLLHEQKRVIDLQSkLIIAVDVAKGMEYLhnLTQPIIHRDLNSHNILLYEDGHAVVADFGESRFLQSLDEDN 152
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 17542550 334 LEKAP--IRWLAPESL-KSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd14064 153 MTKQPgnLRWMAPEVFtQCTRYSIKADVFSYALCLWELL 191
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
181-434 8.94e-29

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: 115.13  E-value: 8.94e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVgstnppiEVAVKrilgnAKRKQIQE--------FCNEAQIMTVLQHENIVAFYGfASLEEP-I 251
Cdd:cd14146   2 IGVGGFGKVYRATWKGQ-------EVAVK-----AARQDPDEdikataesVRQEAKLFSMLRHPNIIKLEG-VCLEEPnL 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 MVVMELVTGGDLRKYL---------QTTQNIPKLQILWFAMNVASGMRHLSSKG---IIHRDLAARNCLVTQDLK----- 314
Cdd:cd14146  69 CLVMEFARGGTLNRALaaanaapgpRRARRIPPHILVNWAVQIARGMLYLHEEAvvpILHRDLKSSNILLLEKIEhddic 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 315 ---AKISDFGLSLQGTEvTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELmarcehdplypkslkdakawiLT 391
Cdd:cd14146 149 nktLKITDFGLAREWHR-TTKMSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWEL---------------------LT 206
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17542550 392 EERPHKMENG-------------------DPKELMVLIDACCERNPNERLNFNTVKRQITDI 434
Cdd:cd14146 207 GEVPYRGIDGlavaygvavnkltlpipstCPEPFAKLMKECWEQDPHIRPSFALILEQLTAI 268
Pkinase pfam00069
Protein kinase domain;
176-424 2.91e-28

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 111.95  E-value: 2.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550   176 NLDKKLGCGAFGEVFKGQYKAVGstnppIEVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:pfam00069   2 EVLRKLGSGSFGTVYKAKHRDTG-----KIVAIKKIkKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550   255 MELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKgiihrdlaarnclvtqdlkakisdfgLSLQGTevttknl 334
Cdd:pfam00069  77 LEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLESGSSL--------------------------TTFVGT------- 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550   335 ekapIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCehdPLYPKSLKDAKAWILTEERPHKMENGD--PKELMVLIDA 412
Cdd:pfam00069 124 ----PWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGK---PPFPGINGNEIYELIIDQPYAFPELPSnlSEEAKDLLKK 196
                         250
                  ....*....|..
gi 17542550   413 CCERNPNERLNF 424
Cdd:pfam00069 197 LLKKDPSKRLTA 208
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
179-423 2.98e-28

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: 113.26  E-value: 2.98e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMEL 257
Cdd:cd08530   6 KKLGKGSYGSVYKVKRLSDNQV-----YALKEVnLGSLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTQNIPKL---QILW-FAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSlqgtEVTTKN 333
Cdd:cd08530  81 APFGDLSKLISKRKKKRRLfpeDDIWrIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGIS----KVLKKN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 334 LEKAPI---RWLAPESLKSGMFNEKTDVWSYGVFLTELMARceHDPLYPKSLKDAKAWILTEERPhKMENGDPKELMVLI 410
Cdd:cd08530 157 LAKTQIgtpLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATF--RPPFEARTMQELRYKVCRGKFP-PIPPVYSQDLQQII 233
                       250
                ....*....|...
gi 17542550 411 DACCERNPNERLN 423
Cdd:cd08530 234 RSLLQVNPKKRPS 246
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
175-434 3.66e-28

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: 115.10  E-value: 3.66e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFkgQYKAVGSTNPPI--EVAVKRILGNAKRKQIQEFCNEAQIMT-VLQHENIVAFYGFASLEE-P 250
Cdd:cd14207   9 LKLGKSLGRGAFGKVV--QASAFGIKKSPTcrVVAVKMLKEGATASEYKALMTELKILIhIGHHLNVVNLLGACTKSGgP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMELVTGGDLRKYLQTTQNI------PKLQ----------------------------------------------- 277
Cdd:cd14207  87 LMVIVEYCKYGNLSNYLKSKRDFfvtnkdTSLQeelikekkeaeptggkkkrlesvtssesfassgfqedkslsdveeee 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 278 ---------------ILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS---LQGTEVTTKNLEKAPI 339
Cdd:cd14207 167 edsgdfykrpltmedLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLArdiYKNPDYVRKGDARLPL 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 340 RWLAPESLKSGMFNEKTDVWSYGVFLTELMArCEHDPlYPKSLKDAKAWILTEE--RPHKMENGDPKELMVLIDaCCERN 417
Cdd:cd14207 247 KWMAPESIFDKIYSTKSDVWSYGVLLWEIFS-LGASP-YPGVQIDEDFCSKLKEgiRMRAPEFATSEIYQIMLD-CWQGD 323
                       330
                ....*....|....*..
gi 17542550 418 PNERLNFNTVKRQITDI 434
Cdd:cd14207 324 PNERPRFSELVERLGDL 340
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
173-369 5.50e-28

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: 112.83  E-value: 5.50e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 173 STINLDKKLGCGAFGEVfkgqYKAVGSTNppiEVAVKRILGNAKR---KQIQEFCNEAQIMTVLQHENIVAFYGFASLEE 249
Cdd:cd14145   6 SELVLEEIIGIGGFGKV----YRAIWIGD---EVAVKAARHDPDEdisQTIENVRQEAKLFAMLKHPNIIALRGVCLKEP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 250 PIMVVMELVTGGDLRKYLQTTQNIPKLQILWfAMNVASGMRHLSSKGI---IHRDLAARNCLVTQ-----DLKAK---IS 318
Cdd:cd14145  79 NLCLVMEFARGGPLNRVLSGKRIPPDILVNW-AVQIARGMNYLHCEAIvpvIHRDLKSSNILILEkvengDLSNKilkIT 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17542550 319 DFGLSLQGTEvTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd14145 158 DFGLAREWHR-TTKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELL 207
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
181-424 6.32e-28

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: 112.55  E-value: 6.32e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGstnppIEVAVKRILG----NAKRKQIQEfcnEAQIMTVLQHENIVAFYGFASLEEPIMVVME 256
Cdd:cd13978   1 LGSGGFGTVSKARHVSWF-----GMVAIKCLHSspncIEERKALLK---EAEKMERARHSYVLPLLGVCVERRSLGLVME 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQ-TTQNIP---KLQILwfaMNVASGMR--HLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS------- 323
Cdd:cd13978  73 YMENGSLKSLLErEIQDVPwslRFRII---HEIALGMNflHNMDPPLLHHDLKPENILLDNHFHVKISDFGLSklgmksi 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 324 LQGTEVTTKNLEKAPIrWLAPESL--KSGMFNEKTDVWSYGVFLTELMARCEhdplyPKSLKDAKAWILTE----ERPHK 397
Cdd:cd13978 150 SANRRRGTENLGGTPI-YMAPEAFddFNKKPTSKSDVYSFAIVIWAVLTRKE-----PFENAINPLLIMQIvskgDRPSL 223
                       250       260       270
                ....*....|....*....|....*....|...
gi 17542550 398 MENGDPK------ELMVLIDACCERNPNERLNF 424
Cdd:cd13978 224 DDIGRLKqienvqELISLMIRCWDGNPDARPTF 256
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
175-432 1.68e-27

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: 111.66  E-value: 1.68e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKA------VGSTNPPIEVAVKrilgnakrkqIQEFCNEAQIMTVLQHENIVAFYGfASLE 248
Cdd:cd14147   5 LRLEEVIGIGGFGKVYRGSWRGelvavkAARQDPDEDISVT----------AESVRQEARLFAMLAHPNIIALKA-VCLE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 249 EP-IMVVMELVTGGDLRKYLQTTQNIPKLQILWfAMNVASGMRHLSSKGI---IHRDLAARNCLVTQ--------DLKAK 316
Cdd:cd14147  74 EPnLCLVMEYAAGGPLSRALAGRRVPPHVLVNW-AVQIARGMHYLHCEALvpvIHRDLKSNNILLLQpienddmeHKTLK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 317 ISDFGLSLQGTEvTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELmarcehdplypkslkdakawiLTEERPH 396
Cdd:cd14147 153 ITDFGLAREWHK-TTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWEL---------------------LTGEVPY 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17542550 397 KMENG-------------------DPKELMVLIDACCERNPNERLNFNTVKRQIT 432
Cdd:cd14147 211 RGIDClavaygvavnkltlpipstCPEPFAQLMADCWAQDPHRRPDFASILQQLE 265
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
169-369 2.26e-27

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: 112.08  E-value: 2.26e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 169 VLIHSTINLDKKLGCGAFGEVFKGQYKAVGSTnPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGfASLE 248
Cdd:cd05110   3 ILKETELKRVKVLGSGAFGTVYKGIWVPEGET-VKIPVAIKILNETTGPKANVEFMDEALIMASMDHPHLVRLLG-VCLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 249 EPIMVVMELVTGGDLRKYLQTTQ-NIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQ 325
Cdd:cd05110  81 PTIQLVTQLMPHGCLLDYVHEHKdNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLArlLE 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17542550 326 GTEVT-TKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd05110 161 GDEKEyNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELM 205
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
179-369 3.32e-27

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: 110.88  E-value: 3.32e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFAsLEEPIMVVMELV 258
Cdd:cd05109  13 KVLGSGAFGTVYKGIWIPDGE-NVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVCRLLGIC-LTSTVQLVTQLM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQN-IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS-LQGTEVTTKNLE- 335
Cdd:cd05109  91 PYGCLLDYVRENKDrIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLArLLDIDETEYHADg 170
                       170       180       190
                ....*....|....*....|....*....|....*
gi 17542550 336 -KAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd05109 171 gKVPIKWMALESILHRRFTHQSDVWSYGVTVWELM 205
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
179-368 4.14e-27

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: 110.43  E-value: 4.14e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQykaVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd14206   3 QEIGNGWFGKVILGE---IFSDYTPAQVVVKELRVSAGPLEQRKFISEAQPYRSLQHPNILQCLGLCTETIPFLLIMEFC 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQT------------TQNIPKLQILwfAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQG 326
Cdd:cd14206  80 QLGDLKRYLRAqrkadgmtpdlpTRDLRTLQRM--AYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLSHNN 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17542550 327 TE----VTTKNLEkAPIRWLAPESLKS--GMF-----NEKTDVWSYGVFLTEL 368
Cdd:cd14206 158 YKedyyLTPDRLW-IPLRWVAPELLDElhGNLivvdqSKESNVWSLGVTIWEL 209
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
179-368 5.16e-27

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: 110.08  E-value: 5.16e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTNppiEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd05087   3 KEIGHGWFGKVFLGEVNSGLSST---QVVVKELKASASVQDQMQFLEEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEFC 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQNIPK-----LQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS---LQGTEVT 330
Cdd:cd05087  80 PLGDLKGYLRSCRAAESmapdpLTLQRMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLShckYKEDYFV 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17542550 331 TKNLEKAPIRWLAPESLKSGMFN-------EKTDVWSYGVFLTEL 368
Cdd:cd05087 160 TADQLWVPLRWIAPELVDEVHGNllvvdqtKQSNVWSLGVTIWEL 204
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
179-368 5.33e-27

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: 109.98  E-value: 5.33e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQykaVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd05042   1 QEIGNGWFGKVLLGE---IYSGTSVAQVVVKELKASANPKEQDTFLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQ----NIPKLQILW-FAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTE---VT 330
Cdd:cd05042  78 DLGDLKAYLRSEReherGDSDTRTLQrMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAHSRYKedyIE 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17542550 331 TKNLEKAPIRWLAPESLKS--GMF-----NEKTDVWSYGVFLTEL 368
Cdd:cd05042 158 TDDKLWFPLRWTAPELVTEfhDRLlvvdqTKYSNIWSLGVTLWEL 202
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
181-369 5.35e-27

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: 109.93  E-value: 5.35e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNA--------KRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIM 252
Cdd:cd06628   8 IGSGSFGSVYLGMNASSGEL-----MAVKQVELPSvsaenkdrKKSMLDALQREIALLRELQHENIVQYLGSSSDANHLN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEVT 330
Cdd:cd06628  83 IFLEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISkkLEANSLS 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 17542550 331 TKNLEKAP-----IRWLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd06628 163 TKNNGARPslqgsVFWMAPEVVKQTSYTRKADIWSLGCLVVEML 206
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
177-434 6.10e-27

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha 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: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 112.81  E-value: 6.10e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVL-QHENIVAFYGFASLEEPIMVVM 255
Cdd:cd05105  41 LGRILGSGAFGKVVEGTAYGLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLgPHLNIVNLLGACTKSGPIYIIT 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRKYLQ---------------------------------------------------TTQNIPKLQI------ 278
Cdd:cd05105 121 EYCFYGDLVNYLHknrdnflsrhpekpkkdldifginpadestrsyvilsfenkgdymdmkqadTTQYVPMLEIkeasky 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 279 ---------------------------------------LWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISD 319
Cdd:cd05105 201 sdiqrsnydrpasykgsndsevknllsddgseglttldlLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICD 280
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 320 FGLS---LQGTEVTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARceHDPLYPKSLKDAKAW--ILTEER 394
Cdd:cd05105 281 FGLArdiMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSL--GGTPYPGMIVDSTFYnkIKSGYR 358
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 17542550 395 PHKMENGdPKELMVLIDACCERNPNERLNFntvkRQITDI 434
Cdd:cd05105 359 MAKPDHA-TQEVYDIMVKCWNSEPEKRPSF----LHLSDI 393
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
175-370 7.04e-27

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: 109.72  E-value: 7.04e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKAvgstnppiEVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEpIMV 253
Cdd:cd14150   2 VSMLKRIGTGSFGTVFRGKWHG--------DVAVKILkVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTRPN-FAI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQN-IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTK 332
Cdd:cd14150  73 ITQWCEGSSLYRHLHVTETrFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSGS 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 17542550 333 NLEKAP---IRWLAPESLK---SGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd14150 153 QQVEQPsgsILWMAPEVIRmqdTNPYSFQSDVYAYGVVLYELMS 196
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
181-432 7.75e-27

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: 109.49  E-value: 7.75e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMvVMELVTG 260
Cdd:cd05037   7 LGQGTFTNIYDGILREVGDGRVQEVEVLLKVLDSDHRDISESFFETASLMSQISHKHLVKLYGVCVADENIM-VQEYVRY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQTTQNIP----KLQILWfamNVASGMRHLSSKGIIHRDLAARNCLVTQD------LKAKISDFGLSlqgTEVT 330
Cdd:cd05037  86 GPLDKYLRRMGNNVplswKLQVAK---QLASALHYLEDKKLIHGNVRGRNILLAREgldgypPFIKLSDPGVP---ITVL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 331 TKNLEKAPIRWLAPESLKSGM--FNEKTDVWSYGVFLTELMARCEhDPLYPKSLKDAKawiLTEERPHKMENGDPKELMV 408
Cdd:cd05037 160 SREERVDRIPWIAPECLRNLQanLTIAADKWSFGTTLWEICSGGE-EPLSALSSQEKL---QFYEDQHQLPAPDCAELAE 235
                       250       260
                ....*....|....*....|....
gi 17542550 409 LIDACCERNPNERLNFNTVKRQIT 432
Cdd:cd05037 236 LIMQCWTYEPTKRPSFRAILRDLN 259
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
177-429 1.12e-26

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: 108.76  E-value: 1.12e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGStnppiEVAVKRILGNAKRKQIQEFCN-EAQIMTVLQHENIVAFYGFasLEEP--IMV 253
Cdd:cd14003   4 LGKTLGEGSFGKVKLARHKLTGE-----KVAIKIIDKSKLKEEIEEKIKrEIEIMKLLNHPNIIKLYEV--IETEnkIYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQ--------TTQNIPKlQILwfamnvaSGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSlq 325
Cdd:cd14003  77 VMEYASGGELFDYIVnngrlsedEARRFFQ-QLI-------SAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLS-- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 326 gTEVTTKNLEKAP---IRWLAPESLKSGMFN-EKTDVWSYGVFLTELMARC------EHDPLYPKSLKDakawilTEERP 395
Cdd:cd14003 147 -NEFRGGSLLKTFcgtPAYAAPEVLLGRKYDgPKADVWSLGVILYAMLTGYlpfdddNDSKLFRKILKG------KYPIP 219
                       250       260       270
                ....*....|....*....|....*....|....
gi 17542550 396 HKMengdPKELMVLIDACCERNPNERLNFNTVKR 429
Cdd:cd14003 220 SHL----SPDARDLIRRMLVVDPSKRITIEEILN 249
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
181-422 1.36e-26

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: 108.37  E-value: 1.36e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTnppieVAVK-----RILgnaKRKQIQEFCNEAQIMTVLQHENIVA-FYGFASlEEPIMVV 254
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKL-----YAMKvlrkkEII---KRKEVEHTLNERNILERVNHPFIVKlHYAFQT-EEKLYLV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKN- 333
Cdd:cd05123  72 LDYVPGGELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTy 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 334 -----LEkapirWLAPESLKSGMFNEKTDVWSYGVFLTELMarCEHDPLYPKSLKDAKAWILTEerPHKMENGDPKELMV 408
Cdd:cd05123 152 tfcgtPE-----YLAPEVLLGKGYGKAVDWWSLGVLLYEML--TGKPPFYAENRKEIYEKILKS--PLKFPEYVSPEAKS 222
                       250
                ....*....|....
gi 17542550 409 LIDACCERNPNERL 422
Cdd:cd05123 223 LISGLLQKDPTKRL 236
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
179-370 1.86e-26

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: 108.89  E-value: 1.86e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGF---ASLEepimVVM 255
Cdd:cd05111  13 KVLGSGVFGTVHKGIWIPEGDS-IKIPVAIKVIQDRSGRQSFQAVTDHMLAIGSLDHAYIVRLLGIcpgASLQ----LVT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRKYL-QTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS---LQGTEVTT 331
Cdd:cd05111  88 QLLPLGSLLDHVrQHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVAdllYPDDKKYF 167
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 17542550 332 KNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd05111 168 YSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMT 206
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
181-434 3.33e-26

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: 107.60  E-value: 3.33e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGstnppiEVAVKRILGNA--KRKQIQEFcneaQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd14156   1 IGSGFFSKVYKVTHGATG------KVMVVKIYKNDvdQHKIVREI----SLLQKLSHPNIVRYLGICVKDEKLHPILEYV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQnipkLQILW-----FAMNVASGMRHLSSKGIIHRDLAARNCLVTQD---LKAKISDFGLSLQGTEVT 330
Cdd:cd14156  71 SGGCLEELLAREE----LPLSWrekveLACDISRGMVYLHSKNIYHRDLNSKNCLIRVTprgREAVVTDFGLAREVGEMP 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 331 TKNLEK-----APIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHDplyPKSLKDAKAWILTEERPHKMENGDPKE 405
Cdd:cd14156 147 ANDPERklslvGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEILARIPAD---PEVLPRTGDFGLDVQAFKEMVPGCPEP 223
                       250       260
                ....*....|....*....|....*....
gi 17542550 406 LMVLIDACCERNPNERLNFNTVKRQITDI 434
Cdd:cd14156 224 FLDLAASCCRMDAFKRPSFAELLDELEDI 252
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
180-434 4.78e-26

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: 107.97  E-value: 4.78e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQykaVGSTNppieVAVKRIL---GNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVME 256
Cdd:cd14158  22 KLGEGGFGVVFKGY---INDKN----VAVKKLAamvDISTEDLTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYT 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQNIPKL---QILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSlQGTEVTTKN 333
Cdd:cd14158  95 YMPNGSLLDRLACLNDTPPLswhMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLA-RASEKFSQT 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 334 LEKAPI----RWLAPESLKsGMFNEKTDVWSYGVFLTELMA--------RCEHDPLYPKSLKDAKAWILTEERPHKMENG 401
Cdd:cd14158 174 IMTERIvgttAYMAPEALR-GEITPKSDIFSFGVVLLEIITglppvdenRDPQLLLDIKEEIEDEEKTIEDYVDKKMGDW 252
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 17542550 402 DPKELMVLIDA---CCERNPNERLNFNTVKRQITDI 434
Cdd:cd14158 253 DSTSIEAMYSVasqCLNDKKNRRPDIAKVQQLLQEL 288
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
179-421 8.00e-26

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: 106.52  E-value: 8.00e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGstnppIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYG-FASlEEPIMVVMEL 257
Cdd:cd06623   7 KVLGQGSSGVVYKVRHKPTG-----KIYALKKIHVDGDEEFRKQLLRELKTLRSCESPYVVKCYGaFYK-EGEISIVLEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHL-SSKGIIHRDLAARNCLVTQDLKAKISDFGLSlqgtEVTTKNLEK 336
Cdd:cd06623  81 MDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLhTKRHIIHRDIKPSNLLINSKGEVKIADFGIS----KVLENTLDQ 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 337 AP-----IRWLAPESLKSGMFNEKTDVWSYGVFLTEL-MARCEHDPLYPKSLKDAKAWILTEERPHKMENGDPKELMVLI 410
Cdd:cd06623 157 CNtfvgtVTYMSPERIQGESYSYAADIWSLGLTLLECaLGKFPFLPPGQPSFFELMQAICDGPPPSLPAEEFSPEFRDFI 236
                       250
                ....*....|.
gi 17542550 411 DACCERNPNER 421
Cdd:cd06623 237 SACLQKDPKKR 247
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
181-370 2.45e-25

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: 105.18  E-value: 2.45e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTnppieVAVKRIL----GNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVME 256
Cdd:cd06632   8 LGSGSFGSVYEGFNGDTGDF-----FAVKEVSlvddDKKSRESVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEV-TTKNLE 335
Cdd:cd06632  83 YVPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFsFAKSFK 162
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 17542550 336 KAPIrWLAPESL--KSGMFNEKTDVWSYGVFLTElMA 370
Cdd:cd06632 163 GSPY-WMAPEVImqKNSGYGLAVDIWSLGCTVLE-MA 197
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
179-370 3.81e-25

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: 104.72  E-value: 3.81e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKgqykAVgSTNPPIEVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMEL 257
Cdd:cd14069   7 QTLGEGAFGEVFL----AV-NRNTEEAVAVKFVdMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ----GTE-VTTK 332
Cdd:cd14069  82 ASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVfrykGKErLLNK 161
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 17542550 333 NLEKAPirWLAPESLKSGMFN-EKTDVWSYGVFLTELMA 370
Cdd:cd14069 162 MCGTLP--YVAPELLAKKKYRaEPVDVWSCGIVLFAMLA 198
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
179-421 5.38e-25

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: 104.35  E-value: 5.38e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGstnppIEVAVKRILGN---AKRKQIqefcneAQIMTVLQHEN---IVAFYGFASLEEPIM 252
Cdd:cd06605   7 GELGEGNGGVVSKVRHRPSG-----QIMAVKVIRLEideALQKQI------LRELDVLHKCNspyIVGFYGAFYSEGDIS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSK-GIIHRDLAARNCLVTQDLKAKISDFGLSLQ------ 325
Cdd:cd06605  76 ICMEYMDGGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQVKLCDFGVSGQlvdsla 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 326 GTEVTTKNlekapirWLAPESLKSGMFNEKTDVWSYGVFLTEL-MARcehdplYPKSLKDAKAWILTEERPHKMENGDP- 403
Cdd:cd06605 156 KTFVGTRS-------YMAPERISGGKYTVKSDIWSLGLSLVELaTGR------FPYPPPNAKPSMMIFELLSYIVDEPPp 222
                       250       260
                ....*....|....*....|....*.
gi 17542550 404 --------KELMVLIDACCERNPNER 421
Cdd:cd06605 223 llpsgkfsPDFQDFVSQCLQKDPTER 248
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
179-368 6.46e-25

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: 103.92  E-value: 6.46e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKrKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd06613   6 QRIGSGTYGDVYKARNIATGEL-----AAVKVIKLEPG-DDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYC 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKnlEKAP 338
Cdd:cd06613  80 GGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATIAK--RKSF 157
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17542550 339 I---RWLAPESL---KSGMFNEKTDVWSYGVFLTEL 368
Cdd:cd06613 158 IgtpYWMAPEVAaveRKGGYDGKCDIWALGITAIEL 193
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
182-434 9.58e-25

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: 104.06  E-value: 9.58e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 182 GCGAFGEVFKGQYKAVgstnppiEVAVKrILGNAKRkqiQEFCNEAQIMTV--LQHENIVAFygFAS------LEEPIMV 253
Cdd:cd13998   4 GKGRFGEVWKASLKNE-------PVAVK-IFSSRDK---QSWFREKEIYRTpmLKHENILQF--IAAderdtaLRTELWL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTtqNIPKLQILW-FAMNVASGMRHLSSK---------GIIHRDLAARNCLVTQDLKAKISDFGLS 323
Cdd:cd13998  71 VTAFHPNGSL*DYLSL--HTIDWVSLCrLALSVARGLAHLHSEipgctqgkpAIAHRDLKSKNILVKNDGTCCIADFGLA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 324 LQGTEVTTKnLEKAP------IRWLAPESLKSGMFNE------KTDVWSYGVFLTELMARC-----EHD----------P 376
Cdd:cd13998 149 VRLSPSTGE-EDNANngqvgtKRYMAPEVLEGAINLRdfesfkRVDIYAMGLVLWEMASRCtdlfgIVEeykppfysevP 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17542550 377 LYPkSLKDAKAWILTEE-RP----HKMENGDPKELMVLIDACCERNPNERLNFNTVKRQITDI 434
Cdd:cd13998 228 NHP-SFEDMQEVVVRDKqRPnipnRWLSHPGLQSLAETIEECWDHDAEARLTAQCIEERLSEF 289
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
180-427 2.39e-24

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: 102.37  E-value: 2.39e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKavGSTNppiEVAVKRIlGNAKRKQIQefcNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVT 259
Cdd:cd14010   7 EIGRGKHSVVYKGRRK--GTIE---FVAIKCV-DKSKRPEVL---NEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 260 GGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS---------LQGTEVT 330
Cdd:cd14010  78 GGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLArregeilkeLFGQFSD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 331 TKNLEKAPIR--------WLAPESLKSGMFNEKTDVWSYGVFLTELMArcEHDPLYPKSLKDAKAWILTEERP---HKME 399
Cdd:cd14010 158 EGNVNKVSKKqakrgtpyYMAPELFQGGVHSFASDLWALGCVLYEMFT--GKPPFVAESFTELVEKILNEDPPpppPKVS 235
                       250       260
                ....*....|....*....|....*...
gi 17542550 400 NGDPKELMVLIDACCERNPNERLNFNTV 427
Cdd:cd14010 236 SKPSPDFKSLLKGLLEKDPAKRLSWDEL 263
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
179-431 3.09e-24

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. 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. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit 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 Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit 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: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 104.60  E-value: 3.09e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVL-QHENIVAFYGFASLEEPIMVVMEL 257
Cdd:cd05104  41 KTLGAGAFGKVVEATAYGLAKADSAMTVAVKMLKPSAHSTEREALMSELKVLSYLgNHINIVNLLGACTVGGPTLVITEY 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTQN---IPKLQ--------------------------------------------------------- 277
Cdd:cd05104 121 CCYGDLLNFLRRKRDsfiCPKFEdlaeaalyrnllhqremacdslneymdmkpsvsyvvptkadkrrgvrsgsyvdqdvt 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 278 ---------------ILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSL---QGTEVTTKNLEKAPI 339
Cdd:cd05104 201 seileedelaldtedLLSFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFGLARdirNDSNYVVKGNARLPV 280
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 340 RWLAPESLKSGMFNEKTDVWSYGVFLTELMArCEHDPlYPKSLKDAKAWILTEErPHKMENGD--PKELMVLIDACCERN 417
Cdd:cd05104 281 KWMAPESIFECVYTFESDVWSYGILLWEIFS-LGSSP-YPGMPVDSKFYKMIKE-GYRMDSPEfaPSEMYDIMRSCWDAD 357
                       330
                ....*....|....
gi 17542550 418 PNERLNFNTVKRQI 431
Cdd:cd05104 358 PLKRPTFKQIVQLI 371
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
180-424 4.27e-24

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: 101.21  E-value: 4.27e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVfkgqYKAVGSTNPPIEVAVKRILGNA-KRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd14121   2 KLGSGTYATV----YKAYRKSGAREVVAVKCVSKSSlNKASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKA--KISDFGLSlqgtEVTTKNLEK 336
Cdd:cd14121  78 SGGDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPvlKLADFGFA----QHLKPNDEA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 337 APIR----WLAPESLKSGMFNEKTDVWSYGVFLTE-LMARCehdPLYPKSLKDakawiLTEerphKMENGDPKELM--VL 409
Cdd:cd14121 154 HSLRgsplYMAPEMILKKKYDARVDLWSVGVILYEcLFGRA---PFASRSFEE-----LEE----KIRSSKPIEIPtrPE 221
                       250       260
                ....*....|....*....|...
gi 17542550 410 IDACC--------ERNPNERLNF 424
Cdd:cd14121 222 LSADCrdlllrllQRDPDRRISF 244
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
181-421 4.71e-24

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: 102.13  E-value: 4.71e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKavgstNPPIEVAVKRILGNAKrKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd06611  13 LGDGAFGKVYKAQHK-----ETGLFAAAKIIQIESE-EELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFCDG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRK-YLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGtevtTKNLEK--- 336
Cdd:cd06611  87 GALDSiMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKN----KSTLQKrdt 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 337 ---APiRWLAP-----ESLKSGMFNEKTDVWSYGVFLTElMARCE--HDPLYPKS--LKDAKAWILTEERPHKMENgdpk 404
Cdd:cd06611 163 figTP-YWMAPevvacETFKDNPYDYKADIWSLGITLIE-LAQMEppHHELNPMRvlLKILKSEPPTLDQPSKWSS---- 236
                       250
                ....*....|....*..
gi 17542550 405 ELMVLIDACCERNPNER 421
Cdd:cd06611 237 SFNDFLKSCLVKDPDDR 253
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
181-434 4.91e-24

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: 101.80  E-value: 4.91e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGqykavgSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd14664   1 IGRGGAGTVYKG------VMPNGTLVAVKRLKGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQT-TQNIPKLQilW-----FAMNVASG---MRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEV 329
Cdd:cd14664  75 GSLGELLHSrPESQPPLD--WetrqrIALGSARGlayLHHDCSPLIIHRDVKSNNILLDEEFEAHVADFGLAklMDDKDS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 TTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMA-RCEHDPLYPKSLKDAKAWI--LTEER-------PHKME 399
Cdd:cd14664 153 HVMSSVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITgKRPFDEAFLDDGVDIVDWVrgLLEEKkvealvdPDLQG 232
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 17542550 400 NGDPKELMVLIDA---CCERNPNERLNFNTVKRQITDI 434
Cdd:cd14664 233 VYKLEEVEQVFQVallCTQSSPMERPTMREVVRMLEGD 270
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
179-368 6.22e-24

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: 101.48  E-value: 6.22e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQ-YKAVGSTnppiEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMEL 257
Cdd:cd05086   3 QEIGNGWFGKVLLGEiYTGTSVA----RVVVKELKASANPKEQDDFLQQGEPYYILQHPNILQCVGQCVEAIPYLLVFEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTQ-----NIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTE---V 329
Cdd:cd05086  79 CDLGDLKTYLANQQeklrgDSQIMLLQRMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYGIGFSRYKedyI 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17542550 330 TTKNLEKAPIRWLAPE---SLKSGMF----NEKTDVWSYGVFLTEL 368
Cdd:cd05086 159 ETDDKKYAPLRWTAPElvtSFQDGLLaaeqTKYSNIWSLGVTLWEL 204
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
181-431 1.00e-23

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: 100.41  E-value: 1.00e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTNP--PIEVAVKrILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd05078   7 LGQGTFTKIFKGIRREVGDYGQlhETEVLLK-VLDKAHRNYSESFFEAASMMSQLSHKHLVLNYGVCVCGDENILVQEYV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQNIpkLQILW---FAMNVASGMRHLSSKGIIHRDLAARNCLVT--QDLKA------KISDFGLSLQgt 327
Cdd:cd05078  86 KFGSLDTYLKKNKNC--INILWkleVAKQLAWAMHFLEEKTLVHGNVCAKNILLIreEDRKTgnppfiKLSDPGISIT-- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 328 eVTTKNLEKAPIRWLAPESLK-SGMFNEKTDVWSYGVFLTELMARCEHdPLypKSLKDAKAWILTEERpHKMENGDPKEL 406
Cdd:cd05078 162 -VLPKDILLERIPWVPPECIEnPKNLSLATDKWSFGTTLWEICSGGDK-PL--SALDSQRKLQFYEDR-HQLPAPKWTEL 236
                       250       260
                ....*....|....*....|....*
gi 17542550 407 MVLIDACCERNPNERLNFNTVKRQI 431
Cdd:cd05078 237 ANLINNCMDYEPDHRPSFRAIIRDL 261
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
182-370 1.21e-23

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: 100.02  E-value: 1.21e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 182 GCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAK-RKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd14002  10 GEGSFGKVYKGRRKYTGQV-----VALKFIPKRGKsEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEYAQG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 gDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGL------------SLQGTe 328
Cdd:cd14002  85 -ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFaramscntlvltSIKGT- 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 17542550 329 vttknlekaPIrWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd14002 163 ---------PL-YMAPELVQEQPYDHTADLWSLGCILYELFV 194
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
176-421 1.23e-23

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: 100.51  E-value: 1.23e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 176 NLDKKLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVM 255
Cdd:cd06610   4 ELIEVIGSGATAVVYAAYCLPKKEK-----VAIKRIDLEKCQTSMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGG---DLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS---LQGTEV 329
Cdd:cd06610  79 PLLSGGsllDIMKSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSaslATGGDR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 TTKNLEK---APIrWLAPESLKSGM-FNEKTDVWSYGVFLTELmARcEHDPLYpkSLKDAKAWILT-EERPHKMENGDP- 403
Cdd:cd06610 159 TRKVRKTfvgTPC-WMAPEVMEQVRgYDFKADIWSFGITAIEL-AT-GAAPYS--KYPPMKVLMLTlQNDPPSLETGADy 233
                       250       260
                ....*....|....*....|..
gi 17542550 404 ----KELMVLIDACCERNPNER 421
Cdd:cd06610 234 kkysKSFRKMISLCLQKDPSKR 255
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
179-323 1.45e-23

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: 99.77  E-value: 1.45e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVK-----RILGNAKRKQIQEfcnEAQIMTVLQHENIVAFYGFASLEEPIMV 253
Cdd:cd14073   7 ETLGKGTYGKVKLAIERATGR-----EVAIKsikkdKIEDEQDMVRIRR---EIEIMSSLNHPHIIRIYEVFENKDKIVI 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS 323
Cdd:cd14073  79 VMEYASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLS 148
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
170-369 1.45e-23

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: 100.49  E-value: 1.45e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 170 LIHSTINLDKKLGCGAFGEVFKGQYKAvgstnppiEVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASlE 248
Cdd:cd14149   9 IEASEVMLSTRIGSGSFGTVYKGKWHG--------DVAVKILkVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMT-K 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 249 EPIMVVMELVTGGDLRKYLQTTQ-NIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGT 327
Cdd:cd14149  80 DNLAIVTQWCEGSSLYKHLHVQEtKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKS 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17542550 328 EVTTKNLEKAP---IRWLAPESLK---SGMFNEKTDVWSYGVFLTELM 369
Cdd:cd14149 160 RWSGSQQVEQPtgsILWMAPEVIRmqdNNPFSFQSDVYSYGIVLYELM 207
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
179-430 2.75e-23

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: 99.26  E-value: 2.75e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFygFASLEEP--IMVVM 255
Cdd:cd08225   6 KKIGEGSFGKIYLAKAKSDSE-----HCVIKEIdLTKMPVKEKEASKKEVILLAKMKHPNIVTF--FASFQENgrLFIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRKYLQTTQNI--PKLQIL-WFaMNVASGMRHLSSKGIIHRDLAARNCLVTQDLK-AKISDFGLS--LQGTEV 329
Cdd:cd08225  79 EYCDGGDLMKRINRQRGVlfSEDQILsWF-VQISLGLKHIHDRKILHRDIKSQNIFLSKNGMvAKLGDFGIArqLNDSME 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 TTKNLEKAPIrWLAPESLKSGMFNEKTDVWSYGVFLTELMA---RCEHDPLYPKSLKDAKAWIlteerpHKMENGDPKEL 406
Cdd:cd08225 158 LAYTCVGTPY-YLSPEICQNRPYNNKTDIWSLGCVLYELCTlkhPFEGNNLHQLVLKICQGYF------APISPNFSRDL 230
                       250       260
                ....*....|....*....|....
gi 17542550 407 MVLIDACCERNPNERLNFNTVKRQ 430
Cdd:cd08225 231 RSLISQLFKVSPRDRPSITSILKR 254
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
180-421 2.82e-23

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: 100.11  E-value: 2.82e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGStnppieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVT 259
Cdd:cd06644  19 ELGDGAFGKVYKAKNKETGA------LAAAKVIETKSEEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCP 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 260 GGDLRK-YLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQgtevTTKNLEK-- 336
Cdd:cd06644  93 GGAVDAiMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAK----NVKTLQRrd 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 337 ----APIrWLAP-----ESLKSGMFNEKTDVWSYGVFLTElMARCE--HDPLYPKS--LKDAKAWILTEERPHKMEngdp 403
Cdd:cd06644 169 sfigTPY-WMAPevvmcETMKDTPYDYKADIWSLGITLIE-MAQIEppHHELNPMRvlLKIAKSEPPTLSQPSKWS---- 242
                       250
                ....*....|....*...
gi 17542550 404 KELMVLIDACCERNPNER 421
Cdd:cd06644 243 MEFRDFLKTALDKHPETR 260
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
179-421 3.02e-23

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: 99.82  E-value: 3.02e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGfASLEEP--IMVVME 256
Cdd:cd06620  11 KDLGAGNGGSVSKVLHIPTGTI-----MAKKVIHIDAKSSVRKQILRELQILHECHSPYIVSFYG-AFLNENnnIIICME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSK-GIIHRDLAARNCLVTQDLKAKISDFGLS------LQGTEV 329
Cdd:cd06620  85 YMDCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKGQIKLCDFGVSgelinsIADTFV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 TTKNlekapirWLAPESLKSGMFNEKTDVWSYGVFLTELMAR---------CEHDPLYPKSLKDAKAWILTEERPhKMEN 400
Cdd:cd06620 165 GTST-------YMSPERIQGGKYSVKSDVWSLGLSIIELALGefpfagsndDDDGYNGPMGILDLLQRIVNEPPP-RLPK 236
                       250       260
                ....*....|....*....|...
gi 17542550 401 GD--PKELMVLIDACCERNPNER 421
Cdd:cd06620 237 DRifPKDLRDFVDRCLLKDPRER 259
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
181-421 4.13e-23

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: 98.70  E-value: 4.13e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVfkgqYKAVGSTNPP---IEVAVKR-ILGNakRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVME 256
Cdd:cd14098   8 LGSGTFAEV----KKAVEVETGKmraIKQIVKRkVAGN--DKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQD--LKAKISDFGLS-LQGTEVTTKN 333
Cdd:cd14098  82 YVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDdpVIVKISDFGLAkVIHTGTFLVT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 334 LEKAPiRWLAPESLKS------GMFNEKTDVWSYGVFLTELM------ARCEHDPLYpKSLKDAkawilTEERPHKMENG 401
Cdd:cd14098 162 FCGTM-AYLAPEILMSkeqnlqGGYSNLVDMWSVGCLVYVMLtgalpfDGSSQLPVE-KRIRKG-----RYTQPPLVDFN 234
                       250       260
                ....*....|....*....|
gi 17542550 402 DPKELMVLIDACCERNPNER 421
Cdd:cd14098 235 ISEEAIDFILRLLDVDPEKR 254
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
181-433 4.55e-23

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: 98.84  E-value: 4.55e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYK----AVGSTNP---------PIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASl 247
Cdd:cd14000   2 LGDGGFGSVYRASYKgepvAVKIFNKhtssnfanvPADTMLRHLRATDAMKNFRLLRQELTVLSHLHHPSIVYLLGIGI- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 248 eEPIMVVMELVTGGDLRKYLQ------------TTQNIpklqilwfAMNVASGMRHLSSKGIIHRDLAARNCLV-----T 310
Cdd:cd14000  81 -HPLMLVLELAPLGSLDHLLQqdsrsfaslgrtLQQRI--------ALQVADGLRYLHSAMIIYRDLKSHNVLVwtlypN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 311 QDLKAKISDFGLSLQGTEVTTKNLEKAPiRWLAPESLKSG-MFNEKTDVWSYGVFLTELMA----RCEHDplypkSLKDA 385
Cdd:cd14000 152 SAIIIKIADYGISRQCCRMGAKGSEGTP-GFRAPEIARGNvIYNEKVDVFSFGMLLYEILSggapMVGHL-----KFPNE 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 17542550 386 KAwILTEERP--HKMENGDPKELMVLIDACCERNPNERLNFNTVKRQITD 433
Cdd:cd14000 226 FD-IHGGLRPplKQYECAPWPEVEVLMKKCWKENPQQRPTAVTVVSILNS 274
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
181-371 7.68e-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: 98.22  E-value: 7.68e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVgstnppiEVAVKRILGNAK-RKQIQEFCNEAQImTVLQHENIV------AFYGFASLEepiMV 253
Cdd:cd13979  11 LGSGGFGSVYKATYKGE-------TVAVKIVRRRRKnRASRQSFWAELNA-ARLRHENIVrvlaaeTGTDFASLG---LI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQNI-PKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTK 332
Cdd:cd13979  80 IMEYCGNGTLQQLIYEGSEPlPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLGEGNEV 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 17542550 333 NLEKAPI----RWLAPESLKSGMFNEKTDVWSYGVFLTELMAR 371
Cdd:cd13979 160 GTPRSHIggtyTYRAPELLKGERVTPKADIYSFGITLWQMLTR 202
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
182-422 9.28e-23

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


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 97.71  E-value: 9.28e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 182 GCGAFGEVFKGQYKAVGSTnppieVAVKRILGNA--KRKQIQEFCNEAQIMTVLQHENIVAF-YGFASlEEPIMVVMELV 258
Cdd:cd05578   9 GKGSFGKVCIVQKKDTKKM-----FAMKYMNKQKciEKDSVRNVLNELEILQELEHPFLVNLwYSFQD-EEDMYMVVDLL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ---GTEVTTKNLE 335
Cdd:cd05578  83 LGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKltdGTLATSTSGT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 336 KApirWLAPESLKSGMFNEKTDVWSYGVFLTELMARceHDPlYPKSLKDAKAWILTEERPHKME--NGDPKELMVLIDAC 413
Cdd:cd05578 163 KP---YMAPEVFMRAGYSFAVDWWSLGVTAYEMLRG--KRP-YEIHSRTSIEEIRAKFETASVLypAGWSEEAIDLINKL 236

                ....*....
gi 17542550 414 CERNPNERL 422
Cdd:cd05578 237 LERDPQKRL 245
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
175-437 9.85e-23

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: 99.28  E-value: 9.85e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMT-VLQHENIVAFYGFASLEE-PIM 252
Cdd:cd05102   9 LRLGKVLGHGAFGKVVEASAFGIDKSSSCETVAVKMLKEGATASEHKALMSELKILIhIGNHLNVVNLLGACTKPNgPLM 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYL-------------------------------------------------QTTQNIPKLQILW--- 280
Cdd:cd05102  89 VIVEFCKYGNLSNFLrakregfspyrersprtrsqvrsmveavradrrsrqgsdrvasftestsSTNQPRQEVDDLWqsp 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 281 --------FAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS---LQGTEVTTKNLEKAPIRWLAPESLKS 349
Cdd:cd05102 169 ltmedlicYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLArdiYKDPDYVRKGSARLPLKWMAPESIFD 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 350 GMFNEKTDVWSYGVFLTELMAR-------CEHDPLYPKSLKDAKawilteeRPHKMENGDPkELMVLIDACCERNPNERL 422
Cdd:cd05102 249 KVYTTQSDVWSFGVLLWEIFSLgaspypgVQINEEFCQRLKDGT-------RMRAPEYATP-EIYRIMLSCWHGDPKERP 320
                       330
                ....*....|....*
gi 17542550 423 NFNTVKRQITDIYME 437
Cdd:cd05102 321 TFSDLVEILGDLLQE 335
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
176-379 1.07e-22

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


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 99.14  E-value: 1.07e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 176 NLDKKLGCGAFGEVFKGQYKAVGstnppIEVAVKRI------LGNAKRkqiqeFCNEAQIMTVLQHENIVA----FYGFA 245
Cdd:cd07834   3 ELLKPIGSGAYGVVCSAYDKRTG-----RKVAIKKIsnvfddLIDAKR-----ILREIKILRHLKHENIIGlldiLRPPS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 246 SLE-EPIMVVMELVtGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSL 324
Cdd:cd07834  73 PEEfNDVYIVTELM-ETDLHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLAR 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17542550 325 QGTE----------VTTknlekapiRWL-APESLKSGM-FNEKTDVWSYGVFLTELMARCehdPLYP 379
Cdd:cd07834 152 GVDPdedkgflteyVVT--------RWYrAPELLLSSKkYTKAIDIWSVGCIFAELLTRK---PLFP 207
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
179-422 1.10e-22

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: 98.06  E-value: 1.10e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVK-----RILgnaKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMV 253
Cdd:cd05581   7 KPLGEGSYSTVVLAKEKETGK-----EYAIKvldkrHII---KEKKVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFG---------LSL 324
Cdd:cd05581  79 VLEYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGtakvlgpdsSPE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 325 QGTEVTTKNLEKAPIR---------WLAPESLKSGMFNEKTDVWSYGVFLTELMA-----RCEHDPLYPKSLKDAKAwil 390
Cdd:cd05581 159 STKGDADSQIAYNQARaasfvgtaeYVSPELLNEKPAGKSSDLWALGCIIYQMLTgkppfRGSNEYLTFQKIVKLEY--- 235
                       250       260       270
                ....*....|....*....|....*....|..
gi 17542550 391 teerphKMENGDPKELMVLIDACCERNPNERL 422
Cdd:cd05581 236 ------EFPENFPPDAKDLIQKLLVLDPSKRL 261
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
181-370 1.69e-22

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: 97.52  E-value: 1.69e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTnppieVAVK--RILGNAKRKQIQEFCNEAQIMTVLQHENIVAfygFASLEEPIMVV---- 254
Cdd:cd13989   1 LGSGGFGYVTLWKHQDTGEY-----VAIKkcRQELSPSDKNRERWCLEVQIMKKLNHPNVVS---ARDVPPELEKLspnd 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 -----MELVTGGDLRKYLQTTQN---IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQ---DLKAKISDFGLS 323
Cdd:cd13989  73 lpllaMEYCSGGDLRKVLNQPENccgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQgggRVIYKLIDLGYA 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17542550 324 lqgtevttKNLEKAP--------IRWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd13989 153 --------KELDQGSlctsfvgtLQYLAPELFESKKYTCTVDYWSFGTLAFECIT 199
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
179-421 2.00e-22

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: 96.74  E-value: 2.00e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRIlgNAKRKQIQEFC-NEAQIMTVLQHENIVAFYGFASLEEPIMVVMEL 257
Cdd:cd06648  13 VKIGEGSTGIVCIATDKSTGR-----QVAVKKM--DLRKQQRRELLfNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLqTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTT--KNLE 335
Cdd:cd06648  86 LEGGALTDIV-THTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKEVPrrKSLV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 336 KAPIrWLAPESLKSGMFNEKTDVWSYGVFLTElMARCEhDPLYPKSLKDAKAWILTEERPH-KMENGDPKELMVLIDACC 414
Cdd:cd06648 165 GTPY-WMAPEVISRLPYGTEVDIWSLGIMVIE-MVDGE-PPYFNEPPLQAMKRIRDNEPPKlKNLHKVSPRLRSFLDRML 241

                ....*..
gi 17542550 415 ERNPNER 421
Cdd:cd06648 242 VRDPAQR 248
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
177-365 2.33e-22

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: 96.48  E-value: 2.33e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGStnpPIEVAVKRIlgnAKRKQIQEFCN-----EAQIMTVLQHENIVAFYGFASLEEPI 251
Cdd:cd14080   4 LGKTIGEGSYSKVKLAEYTKSGL---KEKVACKII---DKKKAPKDFLEkflprELEILRKLRHPNIIQVYSIFERGSKV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 MVVMELVTGGDLRKYLQTTQNIPKLQI-LWFAmNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSlqgtevt 330
Cdd:cd14080  78 FIFMEYAEHGDLLEYIQKRGALSESQArIWFR-QLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFA------- 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 17542550 331 tKNLEKAPIRWL-----------APESLKSGMFNEKT-DVWSYGVFL 365
Cdd:cd14080 150 -RLCPDDDGDVLsktfcgsaayaAPEILQGIPYDPKKyDIWSLGVIL 195
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
177-427 3.31e-22

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: 96.19  E-value: 3.31e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGSTnppieVAVKR--ILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYgfASLEE--PIM 252
Cdd:cd08224   4 IEKKIGKGQFSVVYRARCLLDGRL-----VALKKvqIFEMMDAKARQDCLKEIDLLQQLNHPNIIKYL--ASFIEnnELN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYLQTTQN----IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTE 328
Cdd:cd08224  77 IVLELADAGDLSRLIKHFKKqkrlIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRFFSS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 329 VTT--KNLEKAPIrWLAPESLKSGMFNEKTDVWSYGVFLTELMA--------------------RCEHDPL----YPKSL 382
Cdd:cd08224 157 KTTaaHSLVGTPY-YMSPERIREQGYDFKSDIWSLGCLLYEMAAlqspfygekmnlyslckkieKCEYPPLpadlYSQEL 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 17542550 383 KDakawilteerphkmengdpkelmvLIDACCERNPNERLNFNTV 427
Cdd:cd08224 236 RD------------------------LVAACIQPDPEKRPDISYV 256
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
179-421 5.18e-22

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: 95.91  E-value: 5.18e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKG-QYKAVGStnppieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMEL 257
Cdd:cd06641  10 EKIGKGSFGEVFKGiDNRTQKV------VAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTQnIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTK-NLEK 336
Cdd:cd06641  84 LGGGSALDLLEPGP-LDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKrN*FV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 337 APIRWLAPESLKSGMFNEKTDVWSYGVFLTELmARCE--HDPLYPKSLkdakAWILTEERPHKMENGDPKELMVLIDACC 414
Cdd:cd06641 163 GTPFWMAPEVIKQSAYDSKADIWSLGITAIEL-ARGEppHSELHPMKV----LFLIPKNNPPTLEGNYSKPLKEFVEACL 237

                ....*..
gi 17542550 415 ERNPNER 421
Cdd:cd06641 238 NKEPSFR 244
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
175-429 5.83e-22

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: 95.49  E-value: 5.83e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKAvgstnppiEVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMV 253
Cdd:cd14063   2 LEIKEVIGKGRFGRVHRGRWHG--------DVAIKLLnIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYL-QTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDlKAKISDFGL-SLQGTEVTT 331
Cdd:cd14063  74 VTSLCKGRTLYSLIhERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENG-RVVITDFGLfSLSGLLQPG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 332 KNLE--KAPIRW---LAPESLKSGM----------FNEKTDVWSYGVFLTELMARceHDPlYPKSLKDAKAW-ILTEERP 395
Cdd:cd14063 153 RREDtlVIPNGWlcyLAPEIIRALSpdldfeeslpFTKASDVYAFGTVWYELLAG--RWP-FKEQPAESIIWqVGCGKKQ 229
                       250       260       270
                ....*....|....*....|....*....|....
gi 17542550 396 HKMENGDPKELMVLIDACCERNPNERLNFNTVKR 429
Cdd:cd14063 230 SLSQLDIGREVKDILMQCWAYDPEKRPTFSDLLR 263
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
181-368 7.37e-22

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: 95.18  E-value: 7.37e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTnppieVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVT 259
Cdd:cd08220   8 VGRGAYGTVYLCRRKDDNKL-----VIIKQIpVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYAP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 260 GGDLRKYLQTTQN--IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLK-AKISDFGLSlqgTEVTTKNLEK 336
Cdd:cd08220  83 GGTLFEYIQQRKGslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTvVKIGDFGIS---KILSSKSKAY 159
                       170       180       190
                ....*....|....*....|....*....|....*
gi 17542550 337 APIR---WLAPESLKSGMFNEKTDVWSYGVFLTEL 368
Cdd:cd08220 160 TVVGtpcYISPELCEGKPYNQKSDIWALGCVLYEL 194
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
177-368 7.38e-22

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta 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: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 97.77  E-value: 7.38e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVL-QHENIVAFYGFASLEEPIMVVM 255
Cdd:cd05107  41 LGRTLGSGAFGRVVEATAHGLSHSQSTMKVAVKMLKSTARSSEKQALMSELKIMSHLgPHLNIVNLLGACTKGGPIYIIT 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRKYLQTTQN---------------------IPKLQ------------------------------------- 277
Cdd:cd05107 121 EYCRYGDLVDYLHRNKHtflqyyldknrddgslisggsTPLSQrkshvslgsesdggymdmskdesadyvpmqdmkgtvk 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 278 ----------------------------------------ILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKI 317
Cdd:cd05107 201 yadiessnyespydqylpsapertrrdtlinespalsymdLVGFSYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKI 280
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 17542550 318 SDFGLS---LQGTEVTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTEL 368
Cdd:cd05107 281 CDFGLArdiMRDSNYISKGSTFLPLKWMAPESIFNNLYTTLSDVWSFGILLWEI 334
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
175-437 8.11e-22

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: 95.51  E-value: 8.11e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKAvgstnppiEVAVKRILGNAKR-KQIQEFCNEAQIMTVLQHENIVAFYGFASlEEPIMV 253
Cdd:cd14151  10 ITVGQRIGSGSFGTVYKGKWHG--------DVAVKMLNVTAPTpQQLQAFKNEVGVLRKTRHVNILLFMGYST-KPQLAI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQN-IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVT-T 331
Cdd:cd14151  81 VTQWCEGSSLYHHLHIIETkFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSgS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 332 KNLEK--APIRWLAPESLK---SGMFNEKTDVWSYGVFLTELMArcehDPLYPKSLKDAKAWILTEERPH------KMEN 400
Cdd:cd14151 161 HQFEQlsGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT----GQLPYSNINNRDQIIFMVGRGYlspdlsKVRS 236
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 17542550 401 GDPKELMVLIDACCERNPNERLNFNTVKRQITDIYME 437
Cdd:cd14151 237 NCPKAMKRLMAECLKKKRDERPLFPQILASIELLARS 273
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
177-421 8.78e-22

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: 94.80  E-value: 8.78e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGSTNppiEVAV-KRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:cd08222   4 VVRKLGSGNFGTVYLVSDLKATADE---ELKVlKEIsVGELQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDL----RKYLQTTQNIPKLQIL-WFaMNVASGMRHLSSKGIIHRDLAARNCLVTQDLkAKISDFGLS--LQGT 327
Cdd:cd08222  81 TEYCEGGDLddkiSEYKKSGTTIDENQILdWF-IQLLLAVQYMHERRILHRDLKAKNIFLKNNV-IKVGDFGISriLMGT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 328 EVTTKNLEKAPIrWLAPESLKSGMFNEKTDVWSYGVFLTELMarCEHDPLYPKSLKDAKAWILTEERPhKMENGDPKELM 407
Cdd:cd08222 159 SDLATTFTGTPY-YMSPEVLKHEGYNSKSDIWSLGCILYEMC--CLKHAFDGQNLLSVMYKIVEGETP-SLPDKYSKELN 234
                       250
                ....*....|....
gi 17542550 408 VLIDACCERNPNER 421
Cdd:cd08222 235 AIYSRMLNKDPALR 248
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
181-422 1.20e-21

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: 94.54  E-value: 1.20e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQykavgSTNPPIEVAVKRILGNAKRKQ-------------IQEFCNEAQIMTVLQHENIVAFYGFasL 247
Cdd:cd14008   1 LGRGSFGKVKLAL-----DTETGQLYAIKIFNKSRLRKRregkndrgkiknaLDDVRREIAIMKKLDHPNIVRLYEV--I 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 248 EEP----IMVVMELVTGGDL--RKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFG 321
Cdd:cd14008  74 DDPesdkLYLVLEYCEGGPVmeLDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 322 LS--LQGTEVTTKNLEKAPIrWLAPESLKSGMFN---EKTDVWSYGVFL-TELMARCehdPLYPKSLKDAKAWILTEERP 395
Cdd:cd14008 154 VSemFEDGNDTLQKTAGTPA-FLAPELCDGDSKTysgKAADIWALGVTLyCLVFGRL---PFNGDNILELYEAIQNQNDE 229
                       250       260
                ....*....|....*....|....*..
gi 17542550 396 HKMENGDPKELMVLIDACCERNPNERL 422
Cdd:cd14008 230 FPIPPELSPELKDLLRRMLEKDPEKRI 256
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
180-421 2.41e-21

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: 94.32  E-value: 2.41e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGStnppieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIV----AFYgfasLEEPIMVVM 255
Cdd:cd06643  12 ELGDGAFGKVYKAQNKETGI------LAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVklldAFY----YENNLWILI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRK-YLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTK-- 332
Cdd:cd06643  82 EFCAGGAVDAvMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTLQRrd 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 333 NLEKAPIrWLAPESL-----KSGMFNEKTDVWSYGVFLTElMARCE--HDPLYPKS--LKDAKAWILTEERPHKMEngdp 403
Cdd:cd06643 162 SFIGTPY-WMAPEVVmcetsKDRPYDYKADVWSLGVTLIE-MAQIEppHHELNPMRvlLKIAKSEPPTLAQPSRWS---- 235
                       250
                ....*....|....*...
gi 17542550 404 KELMVLIDACCERNPNER 421
Cdd:cd06643 236 PEFKDFLRKCLEKNVDAR 253
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
179-369 2.47e-21

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: 93.57  E-value: 2.47e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRI----LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:cd06625   6 KLLGQGAFGQVYLCYDADTGR-----ELAVKQVeidpINTEASKEVKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGG----DLRKYLQTTQNIPK---LQILwfamnvaSGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQ 325
Cdd:cd06625  81 MEYMPGGsvkdEIKAYGALTENVTRkytRQIL-------EGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASkrLQ 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17542550 326 G--TEVTTKNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd06625 154 TicSSTGMKSVTGTP-YWMSPEVINGEGYGRKADIWSVGCTVVEML 198
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
179-421 2.91e-21

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: 93.85  E-value: 2.91e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKavgSTNPPieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd06609   7 ERIGKGSFGEVYKGIDK---RTNQV--VAIKVIDLEEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEYC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTtQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKN--LEK 336
Cdd:cd06609  82 GGGSVLDLLKP-GPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTMSKRntFVG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 337 APIrWLAPESLKSGMFNEKTDVWSYGVFLTELMA----RCEHDP-----LYPKSlkdakawilteERPHKMENGDPKELM 407
Cdd:cd06609 161 TPF-WMAPEVIKQSGYDEKADIWSLGITAIELAKgeppLSDLHPmrvlfLIPKN-----------NPPSLEGNKFSKPFK 228
                       250
                ....*....|....
gi 17542550 408 VLIDACCERNPNER 421
Cdd:cd06609 229 DFVELCLNKDPKER 242
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
179-434 3.19e-21

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: 93.55  E-value: 3.19e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQykavgSTNPPIEVAVKRILGNAKRKQiQEFCNEAQIMTVL-QHENIVAFYGFASLEEP----IMV 253
Cdd:cd13985   6 KQLGEGGFSYVYLAH-----DVNTGRRYALKRMYFNDEEQL-RVAIKEIEIMKRLcGHPNIVQYYDSAILSSEgrkeVLL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVtGGDLRKYLQTTQNIP--KLQILWFAMNVASGMRHLSSKG--IIHRDLAARNCLVTQDLKAKISDFG-LSLQGTE 328
Cdd:cd13985  80 LMEYC-PGSLVDILEKSPPSPlsEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGsATTEHYP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 329 VTTK---NLEKAPIR------WLAPESL---KSGMFNEKTDVWSYGVFLTELMARceHDPLYPKSlkdaKAWILTEERPH 396
Cdd:cd13985 159 LERAeevNIIEEEIQknttpmYRAPEMIdlySKKPIGEKADIWALGCLLYKLCFF--KLPFDESS----KLAIVAGKYSI 232
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 17542550 397 KMENGDPKELMVLIDACCERNPNERLNFNTVKRQITDI 434
Cdd:cd13985 233 PEQPRYSPELHDLIRHMLTPDPAERPDIFQVINIITKD 270
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
171-386 3.51e-21

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


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 93.21  E-value: 3.51e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 171 IHSTINLDKKLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEP 250
Cdd:cd14083   1 IRDKYEFKEVLGTGAFSEVVLAEDKATGKL-----VAIKCIDKKALKGKEDSLENEIAVLRKIKHPNIVQLLDIYESKSH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMELVTGGDL-----RKYLQTTQNIPKL--QILwfamnvaSGMRHLSSKGIIHRDLAARNCLV---TQDLKAKISDF 320
Cdd:cd14083  76 LYLVMELVTGGELfdrivEKGSYTEKDASHLirQVL-------EAVDYLHSLGIVHRDLKPENLLYyspDEDSKIMISDF 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17542550 321 GLS------LQGTEVTTKNlekapirWLAPESLKSGMFNEKTDVWSYGVFLTELMarCEHDPLYPKSlkDAK 386
Cdd:cd14083 149 GLSkmedsgVMSTACGTPG-------YVAPEVLAQKPYGKAVDCWSIGVISYILL--CGYPPFYDEN--DSK 209
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
181-424 4.10e-21

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: 93.36  E-value: 4.10e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTNPPIEVAVKRIlgnAKRKQIQEFCNEAQIMTVLQHENIVAF-YGFASlEEPIMVVMELVT 259
Cdd:cd05577   1 LGRGGFGEVCACQVKATGKMYACKKLDKKRI---KKKKGETMALNEKIILEKVSSPFIVSLaYAFET-KDKLCLVLTLMN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 260 GGDLRKYLQT--TQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLEKA 337
Cdd:cd05577  77 GGDLKYHIYNvgTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKGGKKIKGRVG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 338 PIRWLAPESLKSGM-FNEKTDVWSYGVFLTELMArcEHDPLYPKSLKDAKAWI--LTEERPHKMENGDPKELMVLIDACC 414
Cdd:cd05577 157 THGYMAPEVLQKEVaYDFSVDWFALGCMLYEMIA--GRSPFRQRKEKVDKEELkrRTLEMAVEYPDSFSPEARSLCEGLL 234
                       250
                ....*....|
gi 17542550 415 ERNPNERLNF 424
Cdd:cd05577 235 QKDPERRLGC 244
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
180-402 4.84e-21

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: 93.66  E-value: 4.84e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVfkgqYKAVGSTNPPIEVAVKRIL------GNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMV 253
Cdd:cd14096   8 KIGEGAFSNV----YKAVPLRNTGKPVAIKVVRkadlssDNLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYYI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDL----RKYLQTTQNIPKLQILwfamNVASGMRHLSSKGIIHRDLAARNCL-------------VTQDL--- 313
Cdd:cd14096  84 VLELADGGEIfhqiVRLTYFSEDLSRHVIT----QVASAVKYLHEIGVVHRDIKPENLLfepipfipsivklRKADDdet 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 314 -----------------KAKISDFGLSLQgteVTTKNLeKAP---IRWLAPESLKSGMFNEKTDVWSYGVFLTELMarCE 373
Cdd:cd14096 160 kvdegefipgvggggigIVKLADFGLSKQ---VWDSNT-KTPcgtVGYTAPEVVKDERYSKKVDMWALGCVLYTLL--CG 233
                       250       260
                ....*....|....*....|....*....
gi 17542550 374 HDPLYPKSLKdakawILTEerphKMENGD 402
Cdd:cd14096 234 FPPFYDESIE-----TLTE----KISRGD 253
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
181-378 6.97e-21

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


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 92.57  E-value: 6.97e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVfkgqYKAVGSTNPPIEVAVKRI------LGNAKR---KQIQEFCNEAQIM-TVLQHENIVAFYGFASLEEP 250
Cdd:cd08528   8 LGSGAFGCV----YKVRKKSNGQTLLALKEInmtnpaFGRTEQerdKSVGDIISEVNIIkEQLRHPNIVRYYKTFLENDR 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMELVTGGDLRKYLQTTQ----NIPKLQILWFAMNVASGMRHL-SSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ 325
Cdd:cd08528  84 LYIVMELIEGAPLGEHFSSLKekneHFTEDRIWNIFVQMVLALRYLhKEKQIVHRDLKPNNIMLGEDDKVTITDFGLAKQ 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17542550 326 GTEVTTKNLEKA-PIRWLAPESLKSGMFNEKTDVWSYGVFLTELmarCEHDPLY 378
Cdd:cd08528 164 KGPESSKMTSVVgTILYSCPEIVQNEPYGEKADIWALGCILYQM---CTLQPPF 214
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
176-421 7.20e-21

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: 91.99  E-value: 7.20e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 176 NLDKKLGCGAFGEVFKGQYKAVGStnppiEVAVKRIL----GNAKRK-QIQEFCNEaqiMTVLQHENIVAFYgfASLEEP 250
Cdd:cd14050   4 TILSKLGEGSFGEVFKVRSREDGK-----LYAVKRSRsrfrGEKDRKrKLEEVERH---EKLGEHPNCVRFI--KAWEEK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVV--MELVtGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTE 328
Cdd:cd14050  74 GILYiqTELC-DTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELDK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 329 VTTKNLEKAPIRWLAPESLKsGMFNEKTDVWSYGVFLTELMarCEHD-PLYPKSLKDAKAWILteerPHKMENGDPKELM 407
Cdd:cd14050 153 EDIHDAQEGDPRYMAPELLQ-GSFTKAADIFSLGITILELA--CNLElPSGGDGWHQLRQGYL----PEEFTAGLSPELR 225
                       250
                ....*....|....
gi 17542550 408 VLIDACCERNPNER 421
Cdd:cd14050 226 SIIKLMMDPDPERR 239
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
181-422 9.47e-21

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: 92.15  E-value: 9.47e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQEFCNEAQIMTVLQH---ENIVAFYGfASLEEP-IMVVME 256
Cdd:cd06917   9 VGRGSYGAVYRGYHVKTGRV-----VALKVLNLDTDDDDVSDIQKEVALLSQLKLgqpKNIIKYYG-SYLKGPsLWIIMD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKyLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGL--SLQGTEVTTKNL 334
Cdd:cd06917  83 YCEGGSIRT-LMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVaaSLNQNSSKRSTF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 335 EKAPIrWLAPESLKSG-MFNEKTDVWSYGVFLTElMAR-----CEHDPLYPKSLkdakawiLTEERPHKME-NGDPKELM 407
Cdd:cd06917 162 VGTPY-WMAPEVITEGkYYDTKADIWSLGITTYE-MATgnppySDVDALRAVML-------IPKSKPPRLEgNGYSPLLK 232
                       250
                ....*....|....*
gi 17542550 408 VLIDACCERNPNERL 422
Cdd:cd06917 233 EFVAACLDEEPKDRL 247
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
180-367 9.50e-21

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: 92.72  E-value: 9.50e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGstnppIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVA-------FYGFASLEEPIM 252
Cdd:cd14038   1 RLGTGGFGNVLRWINQETG-----EQVAIKQCRQELSPKNRERWCLEIQIMKRLNHPNVVAardvpegLQKLAPNDLPLL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VvMELVTGGDLRKYLQTTQNIPKLQ---ILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQD---LKAKISDFGLS--L 324
Cdd:cd14038  76 A-MEYCQGGDLRKYLNQFENCCGLRegaILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGeqrLIHKIIDLGYAkeL 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 17542550 325 QGTEVTTKNLekAPIRWLAPESLKSGMFNEKTDVWSYGVFLTE 367
Cdd:cd14038 155 DQGSLCTSFV--GTLQYLAPELLEQQKYTVTVDYWSFGTLAFE 195
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
181-421 9.55e-21

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: 91.72  E-value: 9.55e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIqefcNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd08221   8 LGRGAFGEAVLYRKTEDNSLVVWKEVNLSRLSEKERRDAL----NEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYL--QTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ-GTEVTTKNLEKA 337
Cdd:cd08221  84 GNLHDKIaqQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVlDSESSMAESIVG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 338 PIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCE-HDPLYPKSLkdaKAWILTEERphKMENGD-PKELMVLIDACCE 415
Cdd:cd08221 164 TPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRtFDATNPLRL---AVKIVQGEY--EDIDEQySEEIIQLVHDCLH 238

                ....*.
gi 17542550 416 RNPNER 421
Cdd:cd08221 239 QDPEDR 244
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
181-421 1.00e-20

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: 92.06  E-value: 1.00e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTnppieVAVKRI------LGNAKRKQ---IQEFCNEAQIMTVLQHENIVAFYGFASLEEPI 251
Cdd:cd06629   9 IGKGTYGRVYLAMNATTGEM-----LAVKQVelpktsSDRADSRQktvVDALKSEIDTLKDLDHPNIVQYLGFEETEDYF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 MVVMELVTGGD----LRKYLQTTQNIPKlqilWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGT 327
Cdd:cd06629  84 SIFLEYVPGGSigscLRKYGKFEEDLVR----FFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKSD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 328 EVTTKN---LEKAPIRWLAPE---SLKSGmFNEKTDVWSYGVFLTELMA--RcehdplyPKSLKDAKAWIL----TEERP 395
Cdd:cd06629 160 DIYGNNgatSMQGSVFWMAPEvihSQGQG-YSAKVDIWSLGCVVLEMLAgrR-------PWSDDEAIAAMFklgnKRSAP 231
                       250       260
                ....*....|....*....|....*..
gi 17542550 396 HKMENGD-PKELMVLIDACCERNPNER 421
Cdd:cd06629 232 PVPEDVNlSPEALDFLNACFAIDPRDR 258
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
184-423 1.03e-20

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: 91.61  E-value: 1.03e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 184 GAFGEVFKGQykavgSTNPPIEVAVKRIlgnakrkQIQEF-CNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTGGD 262
Cdd:cd13995  15 GAFGKVYLAQ-----DTKTKKRMACKLI-------PVEQFkPSDVEIQACFRHENIAELYGALLWEETVHLFMEAGEGGS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 263 LRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNcLVTQDLKAKISDFGLSLQGTE--VTTKNLEKAPIr 340
Cdd:cd13995  83 VLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSN-IVFMSTKAVLVDFGLSVQMTEdvYVPKDLRGTEI- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 341 WLAPESLKSGMFNEKTDVWSYGVFLTELMARCEhdPL---YPKSLKDAKAWILTEERP--HKMENGDPKELMVLIDACCE 415
Cdd:cd13995 161 YMSPEVILCRGHNTKADIYSLGATIIHMQTGSP--PWvrrYPRSAYPSYLYIIHKQAPplEDIAQDCSPAMRELLEAALE 238

                ....*...
gi 17542550 416 RNPNERLN 423
Cdd:cd13995 239 RNPNHRSS 246
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
184-372 1.20e-20

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: 92.39  E-value: 1.20e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 184 GAFGEVFKGQYkavgsTNppIEVAVKRILGNAKrkqiQEFCNEAQIMTV--LQHENIVAFYGFASLEEPIMVVMELVTG- 260
Cdd:cd14053   6 GRFGAVWKAQY-----LN--RLVAVKIFPLQEK----QSWLTEREIYSLpgMKHENILQFIGAEKHGESLEAEYWLITEf 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 ---GDLRKYLqtTQNIPKL-QILWFAMNVASGMRHL----------SSKGIIHRDLAARNCLVTQDLKAKISDFGLSL-- 324
Cdd:cd14053  75 herGSLCDYL--KGNVISWnELCKIAESMARGLAYLhedipatnggHKPSIAHRDFKSKNVLLKSDLTACIADFGLALkf 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17542550 325 -QGTE-------VTTKnlekapiRWLAPESLKSGM-FNE----KTDVWSYGVFLTELMARC 372
Cdd:cd14053 153 ePGKScgdthgqVGTR-------RYMAPEVLEGAInFTRdaflRIDMYAMGLVLWELLSRC 206
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
179-430 1.23e-20

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: 91.41  E-value: 1.23e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRIlgnaKRKQIQEFCNEAQIMTVLQHENIVAFYgfASLEE--PIMVVME 256
Cdd:cd08218   6 KKIGEGSFGKALLVKSKEDGKQYVIKEINISKM----SPKEREESRKEVAVLSKMKHPNIVQYQ--ESFEEngNLYIVMD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQNI--PKLQIL-WFaMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEVTT 331
Cdd:cd08218  80 YCDGGDLYKRINAQRGVlfPEDQILdWF-VQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIArvLNSTVELA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 332 KNLEKAPIrWLAPESLKSGMFNEKTDVWSYGVFLTElMARCEHdPLYPKSLKDAKAWILTEERPhKMENGDPKELMVLID 411
Cdd:cd08218 159 RTCIGTPY-YLSPEICENKPYNNKSDIWALGCVLYE-MCTLKH-AFEAGNMKNLVLKIIRGSYP-PVPSRYSYDLRSLVS 234
                       250
                ....*....|....*....
gi 17542550 412 ACCERNPNERLNFNTVKRQ 430
Cdd:cd08218 235 QLFKRNPRDRPSINSILEK 253
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
174-422 1.33e-20

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: 92.18  E-value: 1.33e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 174 TINLDKKLGCGAFGEVFKGQYKAVGSTnppieVAVKRILgnakrkQIQEFCN-EAQIMTVLQHENIVAFYGF--ASLEEP 250
Cdd:cd14137   5 SYTIEKVIGSGSFGVVYQAKLLETGEV-----VAIKKVL------QDKRYKNrELQIMRRLKHPNIVKLKYFfySSGEKK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMV----VMELV--TGGD-LRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLV---TQDLkaKISDF 320
Cdd:cd14137  74 DEVylnlVMEYMpeTLYRvIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVdpeTGVL--KLCDF 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 321 GlslqgtevTTKNLEK-----API-----RwlAPES-LKSGMFNEKTDVWSYGVFLTELMArceHDPLYP-KSLKDAKAW 388
Cdd:cd14137 152 G--------SAKRLVPgepnvSYIcsryyR--APELiFGATDYTTAIDIWSAGCVLAELLL---GQPLFPgESSVDQLVE 218
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17542550 389 IL------TEER-----PHKME----------------NGDPKELMVLIDACCERNPNERL 422
Cdd:cd14137 219 IIkvlgtpTREQikamnPNYTEfkfpqikphpwekvfpKRTPPDAIDLLSKILVYNPSKRL 279
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
181-379 2.22e-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: 91.65  E-value: 2.22e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAvgstnppIEVAVKRILGNAKrkqiQEFCNEAQIMTV--LQHENIVAFYGFA------SLEEPiM 252
Cdd:cd14054   3 IGQGRYGTVWKGSLDE-------RPVAVKVFPARHR----QNFQNEKDIYELplMEHSNILRFIGADerptadGRMEY-L 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYL-QTTQNIPKLQILwfAMNVASGMRHLSSK---------GIIHRDLAARNCLVTQDLKAKISDFGL 322
Cdd:cd14054  71 LVLEYAPKGSLCSYLrENTLDWMSSCRM--ALSLTRGLAYLHTDlrrgdqykpAIAHRDLNSRNVLVKADGSCVICDFGL 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17542550 323 SLQ-----------GTEVTTKNLEKAPIRWLAPESLK-------SGMFNEKTDVWSYGVFLTELMARCEHdpLYP 379
Cdd:cd14054 149 AMVlrgsslvrgrpGAAENASISEVGTLRYMAPEVLEgavnlrdCESALKQVDVYALGLVLWEIAMRCSD--LYP 221
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
175-371 6.59e-20

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 89.28  E-value: 6.59e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVfkgqyKAVGSTNPPIEVAVKRIlgnAKRKQIQEFCN-----EAQIMTVLQHENIVAFYGFASLEE 249
Cdd:cd14162   2 YIVGKTLGHGSYAVV-----KKAYSTKHKCKVAIKIV---SKKKAPEDYLQkflprEIEVIKGLKHPNLICFYEAIETTS 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 250 PIMVVMELVTGGDLRKYLQTTQNIPKLQI-LWFAMNVAsGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLqgTE 328
Cdd:cd14162  74 RVYIIMELAENGDLLDYIRKNGALPEPQArRWFRQLVA-GVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFAR--GV 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17542550 329 VTTKNLEKAPIR-------WLAPESLKSGMFNEK-TDVWSYGVFL-TELMAR 371
Cdd:cd14162 151 MKTKDGKPKLSEtycgsyaYASPEILRGIPYDPFlSDIWSMGVVLyTMVYGR 202
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
175-370 6.89e-20

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: 91.20  E-value: 6.89e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHE-NIVAFYGFASLEE-PIM 252
Cdd:cd05103   9 LKLGKPLGRGAFGQVIEADAFGIDKTATCRTVAVKMLKEGATHSEHRALMSELKILIHIGHHlNVVNLLGACTKPGgPLM 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYLQTTQN---------------------IPKL----------------------------------- 276
Cdd:cd05103  89 VIVEFCKFGNLSAYLRSKRSefvpyktkgarfrqgkdyvgdISVDlkrrldsitssqssassgfveekslsdveeeeagq 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 277 -----------QILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS---LQGTEVTTKNLEKAPIRWL 342
Cdd:cd05103 169 edlykdfltleDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLArdiYKDPDYVRKGDARLPLKWM 248
                       250       260
                ....*....|....*....|....*...
gi 17542550 343 APESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd05103 249 APETIFDRVYTIQSDVWSFGVLLWEIFS 276
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
177-369 7.84e-20

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: 89.21  E-value: 7.84e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQykavgSTNPPIEVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYG--FASLEEPIMV 253
Cdd:cd13983   5 FNEVLGRGSFKTVYRAF-----DTEEGIEVAWNEIkLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDswESKSKKEVIF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQNiPKLQIL--WfAMNVASGMRHLSSKG--IIHRDLAARNCLVTQDL-KAKISDFGLSlqgte 328
Cdd:cd13983  80 ITELMTSGTLKQYLKRFKR-LKLKVIksW-CRQILEGLNYLHTRDppIIHRDLKCDNIFINGNTgEVKIGDLGLA----- 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 17542550 329 vTTKNLEKA------PiRWLAPEsLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd13983 153 -TLLRQSFAksvigtP-EFMAPE-MYEEHYDEKVDIYAFGMCLLEMA 196
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
179-365 8.93e-20

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: 89.37  E-value: 8.93e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRI----LGNAKRKQIQE---FCNEAQIMTVLQHENIVAFYGFASLEEPI 251
Cdd:cd14084  12 RTLGSGACGEVKLAYDKSTCK-----KVAIKIInkrkFTIGSRREINKprnIETEIEILKKLSHPCIIKIEDFFDAEDDY 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 MVVMELVTGGDL----RKYLQTTQNIPKLqilwFAMNVASGMRHLSSKGIIHRDLAARNCLVT---QDLKAKISDFGLSl 324
Cdd:cd14084  87 YIVLELMEGGELfdrvVSNKRLKEAICKL----YFYQMLLAVKYLHSNGIIHRDLKPENVLLSsqeEECLIKITDFGLS- 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17542550 325 qgtevttKNLEKAPI--------RWLAPESLKSGM---FNEKTDVWSYGVFL 365
Cdd:cd14084 162 -------KILGETSLmktlcgtpTYLAPEVLRSFGtegYTRAVDCWSLGVIL 206
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
177-368 9.11e-20

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


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 89.32  E-value: 9.11e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGstnppiEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVME 256
Cdd:cd06646  13 LIQRVGSGTYGDVYKARNLHTG------ELAAVKIIKLEPGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICME 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEVTTKNL 334
Cdd:cd06646  87 YCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAakITATIAKRKSF 166
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 17542550 335 EKAPIrWLAPESL---KSGMFNEKTDVWSYGVFLTEL 368
Cdd:cd06646 167 IGTPY-WMAPEVAaveKNGGYNQLCDIWAVGITAIEL 202
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
181-427 9.51e-20

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: 88.76  E-value: 9.51e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQykavgSTNPPIEVAVKRILGNAKRK--QIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd14186   9 LGKGSFACVYRAR-----SLHTGLEVAIKMIDKKAMQKagMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEMC 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQN-IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLEKA 337
Cdd:cd14186  84 HNGEMSRYLKNRKKpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHEKHFTMC 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 338 PI-RWLAPESLKSGMFNEKTDVWSYG-VFLTELMARcehDPLYPKSLKDAKAWILTEErpHKMENGDPKELMVLIDACCE 415
Cdd:cd14186 164 GTpNYISPEIATRSAHGLESDVWSLGcMFYTLLVGR---PPFDTDTVKNTLNKVVLAD--YEMPAFLSREAQDLIHQLLR 238
                       250
                ....*....|..
gi 17542550 416 RNPNERLNFNTV 427
Cdd:cd14186 239 KNPADRLSLSSV 250
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
180-421 1.20e-19

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: 89.66  E-value: 1.20e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGStnppiEVAVKRIlgNAKRKQIQEFC-NEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd06659  28 KIGEGSTGVVCIAREKHSGR-----QVAVKMM--DLRKQQRRELLfNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYL 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQnIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTK--NLEK 336
Cdd:cd06659 101 QGGALTDIVSQTR-LNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDVPKrkSLVG 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 337 APIrWLAPESLKSGMFNEKTDVWSYGVFLTELMarcEHDPLYPKSLKDAKAWILTEERPHKMENGDPKE--LMVLIDACC 414
Cdd:cd06659 180 TPY-WMAPEVISRCPYGTEVDIWSLGIMVIEMV---DGEPPYFSDSPVQAMKRLRDSPPPKLKNSHKASpvLRDFLERML 255

                ....*..
gi 17542550 415 ERNPNER 421
Cdd:cd06659 256 VRDPQER 262
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
179-370 1.45e-19

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: 89.18  E-value: 1.45e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKrILGNAK---RKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVM 255
Cdd:cd05580   7 KTLGTGSFGRVRLVKHKDSGKY-----YALK-ILKKAKiikLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGL---------SLQG 326
Cdd:cd05580  81 EYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFakrvkdrtyTLCG 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 17542550 327 TevttknlekaPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd05580 161 T----------P-EYLAPEIILSKGHGKAVDWWALGILIYEMLA 193
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
181-421 1.70e-19

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 88.78  E-value: 1.70e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAvgstnPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYgFASLEEP---------- 250
Cdd:cd14048  14 LGRGGFGVVFEAKNKV-----DDCNYAVKRIRLPNNELAREKVLREVRALAKLDHPGIVRYF-NAWLERPpegwqekmde 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 --IMVVMELVTGGDLRKYLQTTQNIPKLQIL----WFaMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS- 323
Cdd:cd14048  88 vyLYIQMQLCRKENLKDWMNRRCTMESRELFvclnIF-KQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLVt 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 324 -----------LQGTEVTTKNLEKAPIR-WLAPESLKSGMFNEKTDVWSYGVFLTELmarcehdpLYPKSLKDAKAWILT 391
Cdd:cd14048 167 amdqgepeqtvLTPMPAYAKHTGQVGTRlYMSPEQIHGNQYSEKVDIFALGLILFEL--------IYSFSTQMERIRTLT 238
                       250       260       270
                ....*....|....*....|....*....|....
gi 17542550 392 EER----PHKMENGDPKELMVLIDAcCERNPNER 421
Cdd:cd14048 239 DVRklkfPALFTNKYPEERDMVQQM-LSPSPSER 271
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
179-378 1.95e-19

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: 88.06  E-value: 1.95e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRIlgNAKRKQIQEFC-NEAQIMTVLQHENIVAFYGFASLEEPIMVVMEL 257
Cdd:cd06647  13 EKIGQGASGTVYTAIDVATGQ-----EVAIKQM--NLQQQPKKELIiNEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTQnIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGT-EVTTKNLEK 336
Cdd:cd06647  86 LAGGSLTDVVTETC-MDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITpEQSKRSTMV 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 17542550 337 APIRWLAPESLKSGMFNEKTDVWSYGVFLTELMarcEHDPLY 378
Cdd:cd06647 165 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMV---EGEPPY 203
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
177-372 2.01e-19

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: 87.85  E-value: 2.01e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGStnppiEVAVK-----RILGNAKRKQIQEfcnEAQIMTVLQHENIVAFYGFASLEEPI 251
Cdd:cd14663   4 LGRTLGEGTFAKVKFARNTKTGE-----SVAIKiidkeQVAREGMVEQIKR---EIAIMKLLRHPNIVELHEVMATKTKI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 MVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS-------- 323
Cdd:cd14663  76 FFVMELVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSalseqfrq 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17542550 324 --LQGTEVTTKNlekapirWLAPESL-KSGMFNEKTDVWSYGVFLTELMARC 372
Cdd:cd14663 156 dgLLHTTCGTPN-------YVAPEVLaRRGYDGAKADIWSCGVILFVLLAGY 200
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
179-421 2.35e-19

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: 87.98  E-value: 2.35e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEP--IMVVM 255
Cdd:cd08217   6 ETIGKGSFGTVRKVRRKSDGKI-----LVWKEIdYGKMSEKEKQQLVSEVNILRELKHPNIVRYYDRIVDRANttLYIVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDL----RKYLQTTQNIPKLQILWFAMNVASGM-----RHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--L 324
Cdd:cd08217  81 EYCEGGDLaqliKKCKKENQYIPEEFIWKIFTQLLLALyechnRSVGGGKILHRDLKPANIFLDSDNNVKLGDFGLArvL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 325 QGTEVTTKNLEKAPIrWLAPESLKSGMFNEKTDVWSYGVFLTELMARceHDPLYPKSLKDAKAWILTEERPHkMENGDPK 404
Cdd:cd08217 161 SHDSSFAKTYVGTPY-YMSPELLNEQSYDEKSDIWSLGCLIYELCAL--HPPFQAANQLELAKKIKEGKFPR-IPSRYSS 236
                       250
                ....*....|....*..
gi 17542550 405 ELMVLIDACCERNPNER 421
Cdd:cd08217 237 ELNEVIKSMLNVDPDKR 253
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
217-422 2.35e-19

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: 87.80  E-value: 2.35e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 217 RKQIQEFCNEAQIMTVLQHENIVAFYGFaSLEEP-------IMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGM 289
Cdd:cd14012  39 KKQIQLLEKELESLKKLRHPNLVSYLAF-SIERRgrsdgwkVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEAL 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 290 RHLSSKGIIHRDLAARNCLV---TQDLKAKISDFGLS--LQGTEVTTKNLEKAPIRWLAPESLKSGM-FNEKTDVWSYGV 363
Cdd:cd14012 118 EYLHRNGVVHKSLHAGNVLLdrdAGTGIVKLTDYSLGktLLDMCSRGSLDEFKQTYWLPPELAQGSKsPTRKTDVWDLGL 197
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17542550 364 FLTELMarcehdplypkSLKDAKAWiLTEERPHKMENGDPKELMVLIDACCERNPNERL 422
Cdd:cd14012 198 LFLQML-----------FGLDVLEK-YTSPNPVLVSLDLSASLQDFLSKCLSLDPKKRP 244
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
177-368 2.56e-19

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: 88.18  E-value: 2.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGstnppiEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVME 256
Cdd:cd06645  15 LIQRIGSGTYGDVYKARNVNTG------ELAAIKVIKLEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICME 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ--GTEVTTKNL 334
Cdd:cd06645  89 FCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQitATIAKRKSF 168
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 17542550 335 EKAPIrWLAPESL---KSGMFNEKTDVWSYGVFLTEL 368
Cdd:cd06645 169 IGTPY-WMAPEVAaveRKGGYNQLCDIWAVGITAIEL 204
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
180-422 2.96e-19

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: 88.56  E-value: 2.96e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVfkgqYKAVGSTNPPIeVAVKRILGNAKR--KQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMEL 257
Cdd:cd06633  28 EIGHGSFGAV----YFATNSHTNEV-VAIKKMSYSGKQtnEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEY 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGG--DL----RKYLQttqnipKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGlslQGTEVTT 331
Cdd:cd06633 103 CLGSasDLlevhKKPLQ------EVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG---SASIASP 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 332 KNLEKAPIRWLAPE---SLKSGMFNEKTDVWSYGVFLTELMARceHDPLYPKSLKDAKAWILTEERPHKMENGDPKELMV 408
Cdd:cd06633 174 ANSFVGTPYWMAPEvilAMDEGQYDGKVDIWSLGITCIELAER--KPPLFNMNAMSALYHIAQNDSPTLQSNEWTDSFRG 251
                       250
                ....*....|....
gi 17542550 409 LIDACCERNPNERL 422
Cdd:cd06633 252 FVDYCLQKIPQERP 265
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
179-365 3.27e-19

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: 87.22  E-value: 3.27e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRILGN--AKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVME 256
Cdd:cd14099   7 KFLGKGGFAKCYEVTDMSTGK-----VYAGKVVPKSslTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSlqgTEVTTKNLEK 336
Cdd:cd14099  82 LCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLA---ARLEYDGERK 158
                       170       180       190
                ....*....|....*....|....*....|....
gi 17542550 337 API----RWLAPESL-KSGMFNEKTDVWSYGVFL 365
Cdd:cd14099 159 KTLcgtpNYIAPEVLeKKKGHSFEVDIWSLGVIL 192
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
179-434 4.62e-19

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: 87.71  E-value: 4.62e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKavGStnppiEVAVKRIlgnaKRKQIQEFCNEAQIM-TV-LQHENIVAFYGFASLEEPIMVVME 256
Cdd:cd14056   1 KTIGKGRYGEVWLGKYR--GE-----KVAVKIF----SSRDEDSWFRETEIYqTVmLRHENILGFIAADIKSTGSWTQLW 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVT----GGDLRKYLQTTQ-NIPKLqiLWFAMNVASGMRHL-------SSK-GIIHRDLAARNCLVTQDLKAKISDFGLS 323
Cdd:cd14056  70 LITeyheHGSLYDYLQRNTlDTEEA--LRLAYSAASGLAHLhteivgtQGKpAIAHRDLKSKNILVKRDGTCCIADLGLA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 324 LqgTEVTTKNLEKAPI-------RWLAPE----SLKSGMFN--EKTDVWSYGVFLTELMARCE----------------- 373
Cdd:cd14056 148 V--RYDSDTNTIDIPPnprvgtkRYMAPEvlddSINPKSFEsfKMADIYSFGLVLWEIARRCEiggiaeeyqlpyfgmvp 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17542550 374 HDPlypkSLKDAKAWILTEE-RP--HKMENGDP--KELMVLIDACCERNPNERLNFNTVKRQITDI 434
Cdd:cd14056 226 SDP----SFEEMRKVVCVEKlRPpiPNRWKSDPvlRSMVKLMQECWSENPHARLTALRVKKTLAKL 287
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
179-422 4.96e-19

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: 86.52  E-value: 4.96e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRILGnakRKQIQEF-CNEAQIMTVL----QHENIVAFYG--FASLEEPI 251
Cdd:cd05118   5 RKIGEGAFGTVWLARDKVTGE-----KVAIKKIKN---DFRHPKAaLREIKLLKHLndveGHPNIVKLLDvfEHRGGNHL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 MVVMELVtGGDLRKYLQTT-QNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDL-KAKISDFGLSLQGTEv 329
Cdd:cd05118  77 CLVFELM-GMNLYELIKDYpRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELgQLKLADFGLARSFTS- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 TTKNLEKAPIRWLAPES-LKSGMFNEKTDVWSYGVFLTELMarcEHDPLYP-KSLKDAKAWIlteerphkMENGDPKELM 407
Cdd:cd05118 155 PPYTPYVATRWYRAPEVlLGAKPYGSSIDIWSLGCILAELL---TGRPLFPgDSEVDQLAKI--------VRLLGTPEAL 223
                       250
                ....*....|....*
gi 17542550 408 VLIDACCERNPNERL 422
Cdd:cd05118 224 DLLSKMLKYDPAKRI 238
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
181-383 5.50e-19

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


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 87.24  E-value: 5.50e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTNPPIEVAVKRIlgnAKRKQIQEFCNEAQIMTVLQHENIVAF-YGFASLEEpIMVVMELVT 259
Cdd:cd05608   9 LGKGGFGEVSACQMRATGKLYACKKLNKKRL---KKRKGYEGAMVEKRILAKVHSRFIVSLaYAFQTKTD-LCLVMTIMN 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 260 GGDLRKYL----QTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEVTTKN 333
Cdd:cd05608  85 GGDLRYHIynvdEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAveLKDGQTKTKG 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17542550 334 LEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMA-----RCEHDPLYPKSLK 383
Cdd:cd05608 165 YAGTP-GFMAPELLLGEEYDYSVDYFTLGVTLYEMIAargpfRARGEKVENKELK 218
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
181-372 7.55e-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: 86.39  E-value: 7.55e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTnppieVAVKRI-LGNAKRKQiqefcnEAQIMTVLQHENIVAFYGF--------------- 244
Cdd:cd14047  14 IGSGGFGQVFKAKHRIDGKT-----YAIKRVkLNNEKAER------EVKALAKLDHPNIVRYNGCwdgfdydpetsssns 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 245 -ASLEEPIMVVMELVTGGDLRKYLQTTQNIP--KLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFG 321
Cdd:cd14047  83 sRSKTKCLFIQMEFCEKGTLESWIEKRNGEKldKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFG 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17542550 322 LSLQGTEVTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARC 372
Cdd:cd14047 163 LVTSLKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVC 213
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
206-434 7.56e-19

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: 86.68  E-value: 7.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 206 VAVKRILGN--AKRKQIQEFCNEAQimtvLQHENIVAFYGFASLEEPIMVVMELVTGGDLRKYLQTtQNIP-----KLQi 278
Cdd:cd13992  28 VAIKHITFSrtEKRTILQELNQLKE----LVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLN-REIKmdwmfKSS- 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 279 lwFAMNVASGMRHL-SSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLEKAPIR----WLAPESLKSGMF- 352
Cdd:cd13992 102 --FIKDIVKGMNYLhSSSIGYHGRLKSSNCLVDSRWVVKLTDFGLRNLLEEQTNHQLDEDAQHkkllWTAPELLRGSLLe 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 353 ---NEKTDVWSYGVFLTELMARCEH------DPLYPKSLKDAKAWILTEerPHKMENGDPKELMVLIDACCERNPNERLN 423
Cdd:cd13992 180 vrgTQKGDVYSFAIILYEILFRSDPfalereVAIVEKVISGGNKPFRPE--LAVLLDEFPPRLVLLVKQCWAENPEKRPS 257
                       250
                ....*....|.
gi 17542550 424 FNTVKRQITDI 434
Cdd:cd13992 258 FKQIKKTLTEN 268
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
179-430 7.64e-19

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: 86.13  E-value: 7.64e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGN--AKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVME 256
Cdd:cd14189   7 RLLGKGGFARCYEMTDLATNKT-----YAVKVIPHSrvAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEVTTKNL 334
Cdd:cd14189  82 LCSRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAarLEPPEQRKKTI 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 335 EKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMarCEHDPLYPKSLKDAKAWIltEERPHKMENGDPKELMVLIDACC 414
Cdd:cd14189 162 CGTP-NYLAPEVLLRQGHGPESDVWSLGCVMYTLL--CGNPPFETLDLKETYRCI--KQVKYTLPASLSLPARHLLAGIL 236
                       250
                ....*....|....*.
gi 17542550 415 ERNPNERLNFNTVKRQ 430
Cdd:cd14189 237 KRNPGDRLTLDQILEH 252
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
181-422 8.89e-19

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: 86.13  E-value: 8.89e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTnppieVAVKRIlgnaKRKQIQE------FCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRT-----FALKCV----KKRHIVQtrqqehIFSEKEILEECNSPFIVKLYRTFKDKKYLYML 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGlslqgtevTTKNL 334
Cdd:cd05572  72 MEYCLGGELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFG--------FAKKL 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 335 EKAPIRW--------LAPESLKSGMFNEKTDVWSYGVFLTELMarC--------EHDPLypKSLKDakawILTEERPHKM 398
Cdd:cd05572 144 GSGRKTWtfcgtpeyVAPEIILNKGYDFSVDYWSLGILLYELL--TgrppfggdDEDPM--KIYNI----ILKGIDKIEF 215
                       250       260
                ....*....|....*....|....
gi 17542550 399 ENGDPKELMVLIDACCERNPNERL 422
Cdd:cd05572 216 PKYIDKNAKNLIKQLLRRNPEERL 239
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
181-421 1.18e-18

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: 86.27  E-value: 1.18e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGStnppiEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGfASLEEPIMVV-MELVT 259
Cdd:cd14046  14 LGKGAFGQVVKVRNKLDGR-----YYAIKKIKLRSESKNNSRILREVMLLSRLNHQHVVRYYQ-AWIERANLYIqMEYCE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 260 GGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLqgTEVTTKNLEKAPI 339
Cdd:cd14046  88 KSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLAT--SNKLNVELATQDI 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 340 R---------------------WLAPESLKS--GMFNEKTDVWSYGVFLTELMarcehdplYPKSLKDAKAWILTEER-- 394
Cdd:cd14046 166 NkstsaalgssgdltgnvgtalYVAPEVQSGtkSTYNEKVDMYSLGIIFFEMC--------YPFSTGMERVQILTALRsv 237
                       250       260       270
                ....*....|....*....|....*....|.
gi 17542550 395 ----PHKMENGDPKELMVLIDACCERNPNER 421
Cdd:cd14046 238 siefPPDFDDNKHSKQAKLIRWLLNHDPAKR 268
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
206-442 1.21e-18

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: 86.11  E-value: 1.21e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 206 VAVKRIlgNAKRKQI-QEFCNEAQIMTVLQHENIVAFYGfASLEEP-IMVVMELVTGGDLRKYLQTtQNIpKLQ---ILW 280
Cdd:cd14042  33 VAIKKV--NKKRIDLtREVLKELKHMRDLQHDNLTRFIG-ACVDPPnICILTEYCPKGSLQDILEN-EDI-KLDwmfRYS 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 281 FAMNVASGMRHLSSKGII-HRDLAARNCLVTQDLKAKISDFGL---------SLQGTEVTTKNLekapirWLAPESLKSG 350
Cdd:cd14042 108 LIHDIVKGMHYLHDSEIKsHGNLKSSNCVVDSRFVLKITDFGLhsfrsgqepPDDSHAYYAKLL------WTAPELLRDP 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 351 MFN----EKTDVWSYGVFLTELMAR------CEHDpLYPKSLKDAKAWILTEE--RPHKMENGDPKELMVLIDACCERNP 418
Cdd:cd14042 182 NPPppgtQKGDVYSFGIILQEIATRqgpfyeEGPD-LSPKEIIKKKVRNGEKPpfRPSLDELECPDEVLSLMQRCWAEDP 260
                       250       260
                ....*....|....*....|....
gi 17542550 419 NERLNFNTVKrqitdIYMEALNKG 442
Cdd:cd14042 261 EERPDFSTLR-----NKLKKLNKG 279
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
180-369 1.49e-18

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: 86.25  E-value: 1.49e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGStnppiEVAVKRIlgNAKRKQIQEFC-NEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd06658  29 KIGEGSTGIVCIATEKHTGK-----QVAVKKM--DLRKQQRRELLfNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQnIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ-GTEVTTKNLEKA 337
Cdd:cd06658 102 EGGALTDIVTHTR-MNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQvSKEVPKRKSLVG 180
                       170       180       190
                ....*....|....*....|....*....|..
gi 17542550 338 PIRWLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd06658 181 TPYWMAPEVISRLPYGTEVDIWSLGIMVIEMI 212
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
177-370 1.55e-18

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: 85.26  E-value: 1.55e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGstnppIEVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVM 255
Cdd:cd14072   4 LLKTIGKGNFAKVKLARHVLTG-----REVAIKIIdKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLE 335
Cdd:cd14072  79 EYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPGNKLDTF 158
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17542550 336 KAPIRWLAPESLKSGMFN-EKTDVWSYGVFLTELMA 370
Cdd:cd14072 159 CGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVS 194
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
181-422 1.74e-18

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: 85.85  E-value: 1.74e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTNPPIEVAVKRIlgnAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd05630   8 LGKGGFGEVCACQVRATGKMYACKKLEKKRI---KKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLR--KYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLEKAP 338
Cdd:cd05630  85 GDLKfhIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKGRVGT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 339 IRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHDPLYPKSLKDAKAWILTEERPHKMENGDPKELMVLIDACCERNP 418
Cdd:cd05630 165 VGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSEKFSPQARSLCSMLLCKDP 244

                ....
gi 17542550 419 NERL 422
Cdd:cd05630 245 AERL 248
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
181-413 2.23e-18

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: 85.01  E-value: 2.23e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAvGStnppiEVAVKRILGNaKRKQIQEFCN---EAQIMTVLQHENIVAFYGFASLEEPIMVVMEL 257
Cdd:cd14161  11 LGKGTYGRVKKARDSS-GR-----LVAIKSIRKD-RIKDEQDLLHirrEIEIMSSLNHPHIISVYEVFENSSKIVIVMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS-LQGTEVTTKNLEK 336
Cdd:cd14161  84 ASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSnLYNQDKFLQTYCG 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17542550 337 APIrWLAPESLKSGMF-NEKTDVWSYGVFLTELMARCehdplYPKSLKDAKAWIlteerpHKMENGDPKELMVLIDAC 413
Cdd:cd14161 164 SPL-YASPEIVNGRPYiGPEVDSWSLGVLLYILVHGT-----MPFDGHDYKILV------KQISSGAYREPTKPSDAC 229
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
180-421 2.75e-18

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: 85.46  E-value: 2.75e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGSTnppieVAVKRIlgNAKRKQIQEFC-NEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd06657  27 KIGEGSTGIVCIATVKSSGKL-----VAVKKM--DLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQnIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ-GTEVTTKNLEKA 337
Cdd:cd06657 100 EGGALTDIVTHTR-MNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQvSKEVPRRKSLVG 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 338 PIRWLAPESLKSGMFNEKTDVWSYGVFLTELMarcEHDPLYPKSLKDAKAWILTEERPHKMENGDPKE--LMVLIDACCE 415
Cdd:cd06657 179 TPYWMAPELISRLPYGPEVDIWSLGIMVIEMV---DGEPPYFNEPPLKAMKMIRDNLPPKLKNLHKVSpsLKGFLDRLLV 255

                ....*.
gi 17542550 416 RNPNER 421
Cdd:cd06657 256 RDPAQR 261
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
181-421 2.82e-18

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: 84.62  E-value: 2.82e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVgstnppiEVAVKRILGNAKRKQIQEfcnEAQIMTVLQHENIVAFygFASLEEPIMVVMELVTG 260
Cdd:cd14068   2 LGDGGFGSVYRAVYRGE-------DVAVKIFNKHTSFRLLRQ---ELVVLSHLHHPSLVAL--LAAGTAPRMLVMELAPK 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQTTQN--IPKLQILwFAMNVASGMRHLSSKGIIHRDLAARNCLV-----TQDLKAKISDFGLSLQGTEVTTKN 333
Cdd:cd14068  70 GSLDALLQQDNAslTRTLQHR-IALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQYCCRMGIKT 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 334 LEKAPiRWLAPESLKSGM-FNEKTDVWSYGVFLTELM---ARCEHDPLYPKSLkDAKAWILTEERPHKMENGDP-KELMV 408
Cdd:cd14068 149 SEGTP-GFRAPEVARGNViYNQQADVYSFGLLLYDILtcgERIVEGLKFPNEF-DELAIQGKLPDPVKEYGCAPwPGVEA 226
                       250
                ....*....|...
gi 17542550 409 LIDACCERNPNER 421
Cdd:cd14068 227 LIKDCLKENPQCR 239
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
173-381 2.86e-18

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 86.03  E-value: 2.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  173 STINLDKKLGCGAFGEVFKGQYKAVGstnppiEVAVKRILGNA---KRKQIQEFCNEAQIMTVLQHENIVAFY-GFASlE 248
Cdd:PTZ00263  18 SDFEMGETLGTGSFGRVRIAKHKGTG------EYYAIKCLKKReilKMKQVQHVAQEKSILMELSHPFIVNMMcSFQD-E 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  249 EPIMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTE 328
Cdd:PTZ00263  91 NRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPD 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 17542550  329 vTTKNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMArcEHDPLYPKS 381
Cdd:PTZ00263 171 -RTFTLCGTP-EYLAPEVIQSKGHGKAVDWWTMGVLLYEFIA--GYPPFFDDT 219
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
164-378 3.03e-18

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 86.19  E-value: 3.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  164 PRGSNVLIHSTINLDKKLGCGAFGEVFKGQYKavGSTNPPieVAVKRILGNA--KRKQIQEFCNEAQIMTVLQHENIVAF 241
Cdd:PTZ00426  21 PKRKNKMKYEDFNFIRTLGTGSFGRVILATYK--NEDFPP--VAIKRFEKSKiiKQKQVDHVFSERKILNYINHPFCVNL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  242 YGFASLEEPIMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFG 321
Cdd:PTZ00426  97 YGSFKDESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFG 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17542550  322 LSlQGTEVTTKNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEhdPLY 378
Cdd:PTZ00426 177 FA-KVVDTRTYTLCGTP-EYIAPEILLNVGHGKAADWWTLGIFIYEILVGCP--PFY 229
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
173-421 3.40e-18

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: 84.69  E-value: 3.40e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 173 STINLDKKLGCGAFGEVFKGQYKAvgsTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIM 252
Cdd:cd08228   2 ANFQIEKKIGRGQFSEVYRATCLL---DRKPVALKKVQIFEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLR---KYLQTTQN-IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTE 328
Cdd:cd08228  79 IVLELADAGDLSqmiKYFKKQKRlIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 329 VTT--KNLEKAPIrWLAPESLKSGMFNEKTDVWSYGVFLTELMARceHDPLYPKSLKdakawilTEERPHKMENGD---- 402
Cdd:cd08228 159 KTTaaHSLVGTPY-YMSPERIHENGYNFKSDIWSLGCLLYEMAAL--QSPFYGDKMN-------LFSLCQKIEQCDyppl 228
                       250       260
                ....*....|....*....|....
gi 17542550 403 PKE-----LMVLIDACCERNPNER 421
Cdd:cd08228 229 PTEhysekLRELVSMCIYPDPDQR 252
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
181-423 3.89e-18

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 84.97  E-value: 3.89e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGStnppiEVAVK--RILGNAKRKQiqEFCNEAQIMTVLQHENIVAF------YGFASLEEPIM 252
Cdd:cd14039   1 LGTGGFGNVCLYQNQETGE-----KIAIKscRLELSVKNKD--RWCHEIQIMKKLNHPNVVKAcdvpeeMNFLVNDVPLL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VvMELVTGGDLRKYLQTTQNIPKL---QILWFAMNVASGMRHLSSKGIIHRDLAARNcLVTQDLKA----KISDFGLSL- 324
Cdd:cd14039  74 A-MEYCSGGDLRKLLNKPENCCGLkesQVLSLLSDIGSGIQYLHENKIIHRDLKPEN-IVLQEINGkivhKIIDLGYAKd 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 325 --QGTEVTTKnleKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARcehdplYPKSLKDAKAWILTEerphKMENGD 402
Cdd:cd14039 152 ldQGSLCTSF---VGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAG------FRPFLHNLQPFTWHE----KIKKKD 218
                       250       260
                ....*....|....*....|.
gi 17542550 403 PKELMvlidACCERNPNERLN 423
Cdd:cd14039 219 PKHIF----AVEEMNGEVRFS 235
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
181-393 4.08e-18

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: 85.34  E-value: 4.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNA--KRKQIQEFCNEAQIMTVLQHENIVA--FYGFASLEEpIMVVME 256
Cdd:cd05590   3 LGKGSFGKVMLARLKESGRL-----YAVKVLKKDVilQDDDVECTMTEKRILSLARNHPFLTqlYCCFQTPDR-LFFVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTE--VTTKNL 334
Cdd:cd05590  77 FVNGGDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFngKTTSTF 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17542550 335 EKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMarCEHDPLYPKSLKDAKAWILTEE 393
Cdd:cd05590 157 CGTP-DYIAPEILQEMLYGPSVDWWAMGVLLYEML--CGHAPFEAENEDDLFEAILNDE 212
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
181-421 4.18e-18

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: 84.31  E-value: 4.18e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd14167  11 LGTGAFSEVVLAEEKRTQKL-----VAIKCIAKKALEGKETSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDL-----RKYLQTTQNIPKL--QILwfamnvaSGMRHLSSKGIIHRDLAARNCL---VTQDLKAKISDFGLS-LQGTEV 329
Cdd:cd14167  86 GELfdrivEKGFYTERDASKLifQIL-------DAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSkIEGSGS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 TTKNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMarCEHDPLYPKSlkDAKAW--ILTEE----RPHKMENGDP 403
Cdd:cd14167 159 VMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAYILL--CGYPPFYDEN--DAKLFeqILKAEyefdSPYWDDISDS 233
                       250
                ....*....|....*...
gi 17542550 404 KElmVLIDACCERNPNER 421
Cdd:cd14167 234 AK--DFIQHLMEKDPEKR 249
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
205-369 4.77e-18

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 87.16  E-value: 4.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  205 EVAVKrILgnakRKQIQE-------FCNEAQIMTVLQHENIVAFY--GFaslEEPI-MVVMELVTGGDLRKYLQTTQNIP 274
Cdd:NF033483  34 DVAVK-VL----RPDLARdpefvarFRREAQSAASLSHPNIVSVYdvGE---DGGIpYIVMEYVDGRTLKDYIREHGPLS 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  275 KLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGL--SLQGTEVTTKNlekAPI---RWLAPESLKS 349
Cdd:NF033483 106 PEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIarALSSTTMTQTN---SVLgtvHYLSPEQARG 182
                        170       180
                 ....*....|....*....|
gi 17542550  350 GMFNEKTDVWSYGVFLTELM 369
Cdd:NF033483 183 GTVDARSDIYSLGIVLYEML 202
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
179-370 4.78e-18

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: 84.28  E-value: 4.78e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVfkgqYKAVGSTNPPIeVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMEL 257
Cdd:cd06626   6 NKIGEGTFGKV----YTAVNLDTGEL-MAMKEIrFQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTT------ 331
Cdd:cd06626  81 CQEGTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNTTtmapge 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 17542550 332 -KNLEKAPIrWLAPESLKSGMFNEK---TDVWSYGVFLTELMA 370
Cdd:cd06626 161 vNSLVGTPA-YMAPEVITGNKGEGHgraADIWSLGCVVLEMAT 202
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
171-381 4.89e-18

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


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 84.56  E-value: 4.89e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 171 IHSTINLDKKLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEP 250
Cdd:cd14169   1 INSVYELKEKLGEGAFSEVVLAQERGSQRL-----VALKCIPKKALRGKEAMVENEIAVLRRINHENIVSLEDIYESPTH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMELVTGGDL------RKYLqTTQNIPKLqilwfAMNVASGMRHLSSKGIIHRDLAARNCLVT---QDLKAKISDFG 321
Cdd:cd14169  76 LYLAMELVTGGELfdriieRGSY-TEKDASQL-----IGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFG 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17542550 322 LS------LQGTEVTTKNlekapirWLAPESLKSGMFNEKTDVWSYGVFLTELMarCEHDPLYPKS 381
Cdd:cd14169 150 LSkieaqgMLSTACGTPG-------YVAPELLEQKPYGKAVDVWAIGVISYILL--CGYPPFYDEN 206
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
179-421 5.17e-18

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: 84.33  E-value: 5.17e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd06640  10 ERIGKGSFGEVFKGIDNRTQQV-----VAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQnIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEVTTKNLEK 336
Cdd:cd06640  85 GGGSALDLLRAGP-FDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAgqLTDTQIKRNTFVG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 337 APIrWLAPESLKSGMFNEKTDVWSYGVFLTELmarCEHDPlyPKS-LKDAKAWILTEERPHKMENGD-PKELMVLIDACC 414
Cdd:cd06640 164 TPF-WMAPEVIQQSAYDSKADIWSLGITAIEL---AKGEP--PNSdMHPMRVLFLIPKNNPPTLVGDfSKPFKEFIDACL 237

                ....*..
gi 17542550 415 ERNPNER 421
Cdd:cd06640 238 NKDPSFR 244
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
177-369 5.91e-18

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: 83.94  E-value: 5.91e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGStnppiEVAVKRILGNAKR----KQIQEFCNEAQIMTVLQHENIVAFYGFA--SLEEP 250
Cdd:cd06652   6 LGKLLGQGAFGRVYLCYDADTGR-----ELAVKQVQFDPESpetsKEVNALECEIQLLKNLLHERIVQYYGCLrdPQERT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS------- 323
Cdd:cd06652  81 LSIFMEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASkrlqtic 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17542550 324 LQGTEVttKNLEKAPIrWLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd06652 161 LSGTGM--KSVTGTPY-WMSPEVISGEGYGRKADIWSVGCTVVEML 203
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
179-370 6.12e-18

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: 84.37  E-value: 6.12e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFK-GQYKAVGSTNPPIevAVKRI---LGNAKRKQIQE-FCNEAQIMTVLQHENIVAFYGFASLEEPIM- 252
Cdd:cd14001   5 KKLGYGTGVNVYLmKRSPRGGSSRSPW--AVKKInskCDKGQRSLYQErLKEEAKILKSLNHPNIVGFRAFTKSEDGSLc 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMEL--VTGGDL--RKYLQTTQNIPKLQILWFAMNVASGMRHL-SSKGIIHRDLAARNCLVTQDLKA-KISDFGLSLQG 326
Cdd:cd14001  83 LAMEYggKSLNDLieERYEAGLGPFPAATILKVALSIARALEYLhNEKKILHGDIKSGNVLIKGDFESvKLCDFGVSLPL 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17542550 327 TEvtTKNLEKAPIR-------WLAPESL-KSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd14001 163 TE--NLEVDSDPKAqyvgtepWKAKEALeEGGVITDKADIFAYGLVLWEMMT 212
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
180-421 6.98e-18

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: 83.55  E-value: 6.98e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVfkgqYKAVGSTNPpIEVAVKRIL------GNAKRKQIQEFCNEAQIMT-VLQHENIVAFYGFASLEEPIM 252
Cdd:cd13993   7 PIGEGAYGVV----YLAVDLRTG-RKYAIKCLYksgpnsKDGNDFQKLPQLREIDLHRrVSRHPNIITLHDVFETEVAIY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYLQTTQNIPKLQILW--FAMNVASGMRHLSSKGIIHRDLAARNCLVTQD-LKAKISDFGLSLqgTEV 329
Cdd:cd13993  82 IVLEYCPNGDLFEAITENRIYVGKTELIknVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCDFGLAT--TEK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 TTKNLEKAPIRWLAPESL------KSGMFNEKTDVWSYGV-FLTELMARC------EHDPLYPKSLKDAKAW---ILTee 393
Cdd:cd13993 160 ISMDFGVGSEFYMAPECFdevgrsLKGYPCAAGDIWSLGIiLLNLTFGRNpwkiasESDPIFYDYYLNSPNLfdvILP-- 237
                       250       260
                ....*....|....*....|....*...
gi 17542550 394 rphkMENgdpkELMVLIDACCERNPNER 421
Cdd:cd13993 238 ----MSD----DFYNLLRQIFTVNPNNR 257
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
174-370 7.43e-18

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 83.42  E-value: 7.43e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 174 TINLDKKLGCGAFGEVFKGQYKAVGstnppIEVAVKrILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMV 253
Cdd:cd14193   5 NVNKEEILGGGRFGQVHKCEEKSSG-----LKLAAK-IIKARSQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDL-RKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARN--CLVTQDLKAKISDFGLSLQgtevt 330
Cdd:cd14193  79 VMEYVDGGELfDRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENilCVSREANQVKIIDFGLARR----- 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17542550 331 TKNLEKAPI-----RWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd14193 154 YKPREKLRVnfgtpEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLS 198
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
206-434 7.73e-18

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: 83.75  E-value: 7.73e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 206 VAVKRILGNA--KRKQIQEfcnEAQIMTVLQHENIVAFYGfASLEEP-IMVVMELVTGGDLRKYLqTTQNIPklqILW-- 280
Cdd:cd14045  33 VAIKKIAKKSftLSKRIRK---EVKQVRELDHPNLCKFIG-GCIEVPnVAIITEYCPKGSLNDVL-LNEDIP---LNWgf 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 281 ---FAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLEKAPIR----WLAPESLKSGMF- 352
Cdd:cd14045 105 rfsFATDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADYGLTTYRKEDGSENASGYQQRlmqvYLPPENHSNTDTe 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 353 -NEKTDVWSYGVFLTELMARCEHDPLYPKSLKDAKAWILTEERPHKMENG--DPKELMVLIDACCERNPNERLNFNTVKR 429
Cdd:cd14045 185 pTQATDVYSYAIILLEIATRNDPVPEDDYSLDEAWCPPLPELISGKTENScpCPADYVELIRRCRKNNPAQRPTFEQIKK 264

                ....*
gi 17542550 430 QITDI 434
Cdd:cd14045 265 TLHKI 269
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
177-370 8.21e-18

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: 84.01  E-value: 8.21e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGstnppIEVAVKRIlgNAKR---KQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMV 253
Cdd:cd14086   5 LKEELGKGAFSVVRRCVQKSTG-----QEFAAKII--NTKKlsaRDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDL------RK-YLQTTQNIPKLQILwfamnvaSGMRHLSSKGIIHRDLAARNCLVTQDLK---AKISDFGLS 323
Cdd:cd14086  78 VFDLVTGGELfedivaREfYSEADASHCIQQIL-------ESVNHCHQNGIVHRDLKPENLLLASKSKgaaVKLADFGLA 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17542550 324 L--QGTEVTTKNLEKAPIrWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd14086 151 IevQGDQQAWFGFAGTPG-YLSPEVLRKDPYGKPVDIWACGVILYILLV 198
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
154-421 9.88e-18

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: 83.93  E-value: 9.88e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 154 PQATPFLIPTP-RGSNVLihSTINLDKKLGCGAFGEVFKGQYKAVGstnppIEVAVKRI----LGNAKRKQiqEFCNEAQ 228
Cdd:cd08229   6 PQFQPQKALRPdMGYNTL--ANFRIEKKIGRGQFSEVYRATCLLDG-----VPVALKKVqifdLMDAKARA--DCIKEID 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 229 IMTVLQHENIVAFYGFASLEEPIMVVMELVTGGDL----RKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAA 304
Cdd:cd08229  77 LLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLsrmiKHFKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 305 RNCLVTQDLKAKISDFGLSLQGTEVTT--KNLEKAPIrWLAPESLKSGMFNEKTDVWSYGVFLTELMARceHDPLY--PK 380
Cdd:cd08229 157 ANVFITATGVVKLGDLGLGRFFSSKTTaaHSLVGTPY-YMSPERIHENGYNFKSDIWSLGCLLYEMAAL--QSPFYgdKM 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 17542550 381 SLKDAKAWILTEERPHKMENGDPKELMVLIDACCERNPNER 421
Cdd:cd08229 234 NLYSLCKKIEQCDYPPLPSDHYSEELRQLVNMCINPDPEKR 274
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
179-379 1.03e-17

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: 83.68  E-value: 1.03e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd07836   6 EKLGEGTYATVYKGRNRTTGEI-----VALKEIHLDAEEGTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEYM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGgDLRKYLQTTQN---IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ-GTEVTTKNL 334
Cdd:cd07836  81 DK-DLKKYMDTHGVrgaLDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAfGIPVNTFSN 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17542550 335 EKAPIRWLAPESL-KSGMFNEKTDVWSYGVFLTELMArceHDPLYP 379
Cdd:cd07836 160 EVVTLWYRAPDVLlGSRTYSTSIDIWSVGCIMAEMIT---GRPLFP 202
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
179-428 1.28e-17

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: 82.91  E-value: 1.28e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKrILGNAK---RKQIQEFCNEAQIMTVLQHENIVA--FYGFASlEEPIMV 253
Cdd:cd05611   2 KPISKGAFGSVYLAKKRSTGDY-----FAIK-VLKKSDmiaKNQVTNVKAERAIMMIQGESPYVAklYYSFQS-KDYLYL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKN 333
Cdd:cd05611  75 VMEYLNGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLEKRHNK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 334 LEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMArcEHDPLYPKSLKDAKAWILTEE--RPHKMENGDPKELMVLID 411
Cdd:cd05611 155 KFVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLF--GYPPFHAETPDAVFDNILSRRinWPEEVKEFCSPEAVDLIN 232
                       250
                ....*....|....*..
gi 17542550 412 ACCERNPNERLNFNTVK 428
Cdd:cd05611 233 RLLCMDPAKRLGANGYQ 249
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
180-378 1.29e-17

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: 83.14  E-value: 1.29e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQEFC-NEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd07833   8 VVGEGAYGVVLKCRNKATGEI-----VAIKKFKESEDDEDVKKTAlREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEYV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 tGGDLRKYLQTTQN-IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNL-EK 336
Cdd:cd07833  83 -ERTLLELLEASPGgLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTARPASPLtDY 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17542550 337 APIRWL-APESL-KSGMFNEKTDVWSYGVFLTELMA-------RCEHDPLY 378
Cdd:cd07833 162 VATRWYrAPELLvGDTNYGKPVDVWAIGCIMAELLDgeplfpgDSDIDQLY 212
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
179-370 1.43e-17

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: 83.25  E-value: 1.43e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILgnaKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd05612   7 KTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVI---RLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEYV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEvTTKNLEKAP 338
Cdd:cd05612  84 PGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLRD-RTWTLCGTP 162
                       170       180       190
                ....*....|....*....|....*....|..
gi 17542550 339 iRWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd05612 163 -EYLAPEVIQSKGHNKAVDWWALGILIYEMLV 193
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
175-421 1.46e-17

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: 82.74  E-value: 1.46e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQykavgSTNPPIEVAVKRILGNA-KRKQIQEFCNEAQIMTVLQHENIVAFY-GFASL---EE 249
Cdd:cd14033   3 LKFNIEIGRGSFKTVYRGL-----DTETTVEVAWCELQTRKlSKGERQRFSEEVEMLKGLQHPNIVRFYdSWKSTvrgHK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 250 PIMVVMELVTGGDLRKYLQTTQNIpKLQIL--WfAMNVASGMRHLSSKG--IIHRDLAARNCLVTQDLKA-KISDFGLSL 324
Cdd:cd14033  78 CIILVTELMTSGTLKTYLKRFREM-KLKLLqrW-SRQILKGLHFLHSRCppILHRDLKCDNIFITGPTGSvKIGDLGLAT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 325 QGTEVTTKNLEKAPiRWLAPESLKSgMFNEKTDVWSYGVFLTElMARCEhdplYPKSLKDAKAWILTE----ERPHKMEN 400
Cdd:cd14033 156 LKRASFAKSVIGTP-EFMAPEMYEE-KYDEAVDVYAFGMCILE-MATSE----YPYSECQNAAQIYRKvtsgIKPDSFYK 228
                       250       260
                ....*....|....*....|.
gi 17542550 401 GDPKELMVLIDACCERNPNER 421
Cdd:cd14033 229 VKVPELKEIIEGCIRTDKDER 249
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
179-422 1.69e-17

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: 83.52  E-value: 1.69e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTNPpIEVAVKRILgnAKRKQIQEFCNEAQIMTVLQHENIVAF-YGFASlEEPIMVVMEL 257
Cdd:cd05595   1 KLLGKGTFGKVILVREKATGRYYA-MKILRKEVI--IAKDEVAHTVTESRVLQNTRHPFLTALkYAFQT-HDRLCFVMEY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGT--EVTTKNLE 335
Cdd:cd05595  77 ANGGELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGItdGATMKTFC 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 336 KAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMarCEHDPLYPKSLKDAKAWILTEE--RPHKMEngdpKELMVLIDAC 413
Cdd:cd05595 157 GTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMM--CGRLPFYNQDHERLFELILMEEirFPRTLS----PEAKSLLAGL 229

                ....*....
gi 17542550 414 CERNPNERL 422
Cdd:cd05595 230 LKKDPKQRL 238
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
179-378 1.72e-17

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: 83.23  E-value: 1.72e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRIlgNAKRKQIQEFC-NEAQIMTVLQHENIVAFYGFASLEEPIMVVMEL 257
Cdd:cd06655  25 EKIGQGASGTVFTAIDVATGQ-----EVAIKQI--NLQKQPKKELIiNEILVMKELKNPNIVNFLDSFLVGDELFVVMEY 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTqNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGT-EVTTKNLEK 336
Cdd:cd06655  98 LAGGSLTDVVTET-CMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITpEQSKRSTMV 176
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 17542550 337 APIRWLAPESLKSGMFNEKTDVWSYGVFLTELMarcEHDPLY 378
Cdd:cd06655 177 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMV---EGEPPY 215
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
177-386 1.86e-17

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: 83.43  E-value: 1.86e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQEFCN--EAQIMTVL-QHENIVAFYGFASLEEPIMV 253
Cdd:cd05619   9 LHKMLGKGSFGKVFLAELKGTNQF-----FAIKALKKDVVLMDDDVECTmvEKRVLSLAwEHPFLTHLFCTFQTKENLFF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGT--EVTT 331
Cdd:cd05619  84 VMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMlgDAKT 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17542550 332 KNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELM-----------------ARCEhDPLYPKSL-KDAK 386
Cdd:cd05619 164 STFCGTP-DYIAPEILLGQKYNTSVDWWSFGVLLYEMLigqspfhgqdeeelfqsIRMD-NPFYPRWLeKEAK 234
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
179-379 2.42e-17

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: 83.39  E-value: 2.42e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQI-QEFCNEAQIMTVLQHENIVAFYG-FASLEEPIMVVME 256
Cdd:cd07856  16 QPVGMGAFGLVCSARDQLTGQN-----VAVKKIMKPFSTPVLaKRTYRELKLLKHLRHENIISLSDiFISPLEDIYFVTE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVtGGDLRKYLqTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS-LQGTEVTTKNLE 335
Cdd:cd07856  91 LL-GTDLHRLL-TSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLArIQDPQMTGYVST 168
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17542550 336 KapiRWLAPE-SLKSGMFNEKTDVWSYGVFLTELMarcEHDPLYP 379
Cdd:cd07856 169 R---YYRAPEiMLTWQKYDVEVDIWSAGCIFAEML---EGKPLFP 207
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
213-435 2.43e-17

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: 82.24  E-value: 2.43e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 213 GNAKRKQIQEFCNEAQImtvlQHENIVAFYGFASLEEPIMVVMELVTGGDLRKYLQTTQNIP---------KLQILWfam 283
Cdd:cd14044  44 GNFTEKQKIELNKLLQI----DYYNLTKFYGTVKLDTMIFGVIEYCERGSLRDVLNDKISYPdgtfmdwefKISVMY--- 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 284 NVASGMRHL-SSKGIIHRDLAARNCLVTQDLKAKISDFGlslqgtevTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYG 362
Cdd:cd14044 117 DIAKGMSYLhSSKTEVHGRLKSTNCVVDSRMVVKITDFG--------CNSILPPSKDLWTAPEHLRQAGTSQKGDVYSYG 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 363 VFLTELMARCEhdPLYPKSLKDAKAWILTEERPHKMENGDP-----------KELMVLIDACCERNPNERLNFNTVKRQI 431
Cdd:cd14044 189 IIAQEIILRKE--TFYTAACSDRKEKIYRVQNPKGMKPFRPdlnlesagereREVYGLVKNCWEEDPEKRPDFKKIENTL 266

                ....
gi 17542550 432 TDIY 435
Cdd:cd14044 267 AKIF 270
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
179-427 2.75e-17

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: 81.93  E-value: 2.75e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVF---KGQYKAVGStnppIEVAVKRILGNAKRKQiqEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVM 255
Cdd:cd14116  11 RPLGKGKFGNVYlarEKQSKFILA----LKVLFKAQLEKAGVEH--QLRREVEIQSHLRHPNILRLYGYFHDATRVYLIL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLe 335
Cdd:cd14116  85 EYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTL- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 336 KAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELmarcehdpLYPKSLKDAKAWILTEERPHKMENGDP----KELMVLID 411
Cdd:cd14116 164 CGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEF--------LVGKPPFEANTYQETYKRISRVEFTFPdfvtEGARDLIS 235
                       250
                ....*....|....*.
gi 17542550 412 ACCERNPNERLNFNTV 427
Cdd:cd14116 236 RLLKHNPSQRPMLREV 251
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
179-421 2.75e-17

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: 82.03  E-value: 2.75e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKG---QYKAVgstnppieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVM 255
Cdd:cd06642  10 ERIGKGSFGEVYKGidnRTKEV--------VAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRKYLQTTQnIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTK-NL 334
Cdd:cd06642  82 EYLGGGSALDLLKPGP-LEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKrNT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 335 EKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELmARCE--HDPLYPKSLkdakAWILTEERPHKMENGDPKELMVLIDA 412
Cdd:cd06642 161 FVGTPFWMAPEVIKQSAYDFKADIWSLGITAIEL-AKGEppNSDLHPMRV----LFLIPKNSPPTLEGQHSKPFKEFVEA 235

                ....*....
gi 17542550 413 CCERNPNER 421
Cdd:cd06642 236 CLNKDPRFR 244
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
184-368 3.11e-17

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: 81.88  E-value: 3.11e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 184 GAFGEVFKGQYKAVGSTnppieVAVKRI-LGNAKRK-QIQEFCNEAQIMTVLQHENIV-AFYGFASlEEPIMVVMELVTG 260
Cdd:cd05579   4 GAYGRVYLAKKKSTGDL-----YAIKVIkKRDMIRKnQVDSVLAERNILSQAQNPFVVkLYYSFQG-KKNLYLVMEYLPG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLEKAPIR 340
Cdd:cd05579  78 GDLYSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVGLVRRQIKLSIQKKS 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 17542550 341 ----------------WLAPESLKSGMFNEKTDVWSYGVFLTEL 368
Cdd:cd05579 158 ngapekedrrivgtpdYLAPEILLGQGHGKTVDWWSLGVILYEF 201
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
176-368 3.12e-17

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: 81.56  E-value: 3.12e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 176 NLDKKLGCGAFGEVFKGQYKavgstNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVM 255
Cdd:cd08219   3 NVLRVVGEGSFGRALLVQHV-----NSDQKYAMKEIRLPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRKY--LQTTQNIPKLQIL-WFaMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFG--------LSL 324
Cdd:cd08219  78 EYCDGGDLMQKikLQRGKLFPEDTILqWF-VQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGsarlltspGAY 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 17542550 325 QGTEVTTKnlekapiRWLAPESLKSGMFNEKTDVWSYGVFLTEL 368
Cdd:cd08219 157 ACTYVGTP-------YYVPPEIWENMPYNNKSDIWSLGCILYEL 193
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
184-422 3.33e-17

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 82.07  E-value: 3.33e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 184 GAFGEVFKGQYKAVGStnppiEVAVKRILGNAK--RKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTGG 261
Cdd:cd05609  11 GAYGAVYLVRHRETRQ-----RFAMKKINKQNLilRNQIQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVMEYVEGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 262 DLRKYLQTTQNIP-KLQILWFAMNVAsGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLEKAPI- 339
Cdd:cd05609  86 DCATLLKNIGPLPvDMARMYFAETVL-ALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKIGLMSLTTNLYEGHIe 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 340 ---------------RWLAPESLKSGMFNEKTDVWSYGVFLTELMARC------EHDPLYPKSLKDAKAWILTEERPhkm 398
Cdd:cd05609 165 kdtrefldkqvcgtpEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCvpffgdTPEELFGQVISDEIEWPEGDDAL--- 241
                       250       260
                ....*....|....*....|....
gi 17542550 399 engdPKELMVLIDACCERNPNERL 422
Cdd:cd05609 242 ----PDDAQDLITRLLQQNPLERL 261
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
177-370 3.45e-17

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: 81.76  E-value: 3.45e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRIlgnaKRKQIQEFCNEAQIM------TVLQHENIVAFYGFASLEEP 250
Cdd:cd14076   5 LGRTLGEGEFGKVKLGWPLPKANHRSGVQVAIKLI----RRDTQQENCQTSKIMreinilKGLTHPNIVRLLDVLKTKKY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLslqgteVT 330
Cdd:cd14076  81 IGIVLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGF------AN 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17542550 331 TKNLEKAPIR--------WLAPE--SLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd14076 155 TFDHFNGDLMstscgspcYAAPElvVSDSMYAGRKADIWSCGVILYAMLA 204
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
175-373 3.60e-17

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: 82.10  E-value: 3.60e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKavGSTnppieVAVKRIlgnAKRKQiQEFCNEAQIM-TV-LQHENIVAFYG--FASL--E 248
Cdd:cd14142   7 ITLVECIGKGRYGEVWRGQWQ--GES-----VAVKIF---SSRDE-KSWFRETEIYnTVlLRHENILGFIAsdMTSRnsC 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 249 EPIMVVMELVTGGDLRKYLQTTQnIPKLQILWFAMNVASGMRHLSSK--------GIIHRDLAARNCLVTQDLKAKISDF 320
Cdd:cd14142  76 TQLWLITHYHENGSLYDYLQRTT-LDHQEMLRLALSAASGLVHLHTEifgtqgkpAIAHRDLKSKNILVKSNGQCCIADL 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17542550 321 GLSLQGTEVTTK-----NLEKAPIRWLAPESLKSGMFNE------KTDVWSYGVFLTELMARCE 373
Cdd:cd14142 155 GLAVTHSQETNQldvgnNPRVGTKRYMAPEVLDETINTDcfesykRVDIYAFGLVLWEVARRCV 218
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
179-363 3.73e-17

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: 81.40  E-value: 3.73e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRILGNAKRKQ---IQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVM 255
Cdd:cd14070   8 RKLGEGSFAKVREGLHAVTGE-----KVAIKVIDKKKAKKDsyvTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ------GTEV 329
Cdd:cd14070  83 ELCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCagilgySDPF 162
                       170       180       190
                ....*....|....*....|....*....|....
gi 17542550 330 TTKNLEKApirWLAPESLKSGMFNEKTDVWSYGV 363
Cdd:cd14070 163 STQCGSPA---YAAPELLARKKYGPKVDVWSIGV 193
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
254-387 3.92e-17

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: 82.44  E-value: 3.92e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGT--EVTT 331
Cdd:cd05587  75 VMEYVNGGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIfgGKTT 154
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17542550 332 KNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMAR----------------CEHDPLYPKSL-KDAKA 387
Cdd:cd05587 155 RTFCGTP-DYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGqppfdgededelfqsiMEHNVSYPKSLsKEAVS 226
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
181-369 4.56e-17

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: 82.33  E-value: 4.56e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTNPPIEVAVKRIlgnAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd05632  10 LGKGGFGEVCACQVRATGKMYACKRLEKKRI---KKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQTTQN--IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLEKAP 338
Cdd:cd05632  87 GDLKFHIYNMGNpgFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGESIRGRVGT 166
                       170       180       190
                ....*....|....*....|....*....|.
gi 17542550 339 IRWLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd05632 167 VGYMAPEVLNNQRYTLSPDYWGLGCLIYEMI 197
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
181-425 4.73e-17

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: 81.70  E-value: 4.73e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQEFCNEAQI-MTVLQHENIVAFYGFASLEEPIMVVMELV- 258
Cdd:cd06617   9 LGRGAYGVVDKMRHVPTGTI-----MAVKRIRATVNSQEQKRLLMDLDIsMRSVDCPYTVTFYGALFREGDVWICMEVMd 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGD--LRKYLQTTQNIPKLQILWFAMNVASGMRHLSSK-GIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLE 335
Cdd:cd06617  84 TSLDkfYKKVYDKGLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFGISGYLVDSVAKTID 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 336 KAPIRWLAPESLKSGM----FNEKTDVWSYGVFLTELMA-----RCEHDPLypKSLKDakawILTEERPHKMENGDPKEL 406
Cdd:cd06617 164 AGCKPYMAPERINPELnqkgYDVKSDVWSLGITMIELATgrfpyDSWKTPF--QQLKQ----VVEEPSPQLPAEKFSPEF 237
                       250
                ....*....|....*....
gi 17542550 407 MVLIDACCERNPNERLNFN 425
Cdd:cd06617 238 QDFVNKCLKKNYKERPNYP 256
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
175-423 5.52e-17

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: 81.31  E-value: 5.52e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQykavgSTNPPIEVA----VKRILGNAKRKQIQEfcnEAQIMTVLQHENIVAFY-GFASL-- 247
Cdd:cd14031  12 LKFDIELGRGAFKTVYKGL-----DTETWVEVAwcelQDRKLTKAEQQRFKE---EAEMLKGLQHPNIVRFYdSWESVlk 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 248 -EEPIMVVMELVTGGDLRKYLQTTQNI-PKLQILWfAMNVASGMR--HLSSKGIIHRDLAARNCLVTQDL-KAKISDFGL 322
Cdd:cd14031  84 gKKCIVLVTELMTSGTLKTYLKRFKVMkPKVLRSW-CRQILKGLQflHTRTPPIIHRDLKCDNIFITGPTgSVKIGDLGL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 323 SLQGTEVTTKNLEKAPiRWLAPESLKSgMFNEKTDVWSYGVFLTElMARCEhdplYPKSLKDAKAWILTEE----RPHKM 398
Cdd:cd14031 163 ATLMRTSFAKSVIGTP-EFMAPEMYEE-HYDESVDVYAFGMCMLE-MATSE----YPYSECQNAAQIYRKVtsgiKPASF 235
                       250       260
                ....*....|....*....|....*
gi 17542550 399 ENGDPKELMVLIDACCERNPNERLN 423
Cdd:cd14031 236 NKVTDPEVKEIIEGCIRQNKSERLS 260
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
181-423 6.27e-17

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: 80.81  E-value: 6.27e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTnppIEVAVK---RILGNAKRKQIQEFC-NEAQIMTVLQHENIV-AFYGFASLEEPIMVVM 255
Cdd:cd13994   1 IGKGATSVVRIVTKKNPRSG---VLYAVKeyrRRDDESKRKDYVKRLtSEYIISSKLHHPNIVkVLDLCQDLHGKWCLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSlqgtEVTTKNLE 335
Cdd:cd13994  78 EYCPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTA----EVFGMPAE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 336 KAPIR---------WLAPESLKSGMFNEK-TDVWSYGVFLTELMAR-------CEHDPLYPKSLkdaKAWILTEERPHKM 398
Cdd:cd13994 154 KESPMsaglcgsepYMAPEVFTSGSYDGRaVDVWSCGIVLFALFTGrfpwrsaKKSDSAYKAYE---KSGDFTNGPYEPI 230
                       250       260
                ....*....|....*....|....*
gi 17542550 399 ENGDPKELMVLIDACCERNPNERLN 423
Cdd:cd13994 231 ENLLPSECRRLIYRMLHPDPEKRIT 255
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
178-379 6.77e-17

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: 81.46  E-value: 6.77e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 178 DKKLGCGAFGEVFKGQYKAVGSTnppieVAVKRI-LGnaKRKQIQEFCN-----EAQIMTVLQHENIVAFYGFASLEEPI 251
Cdd:cd07841   5 GKKLGEGTYAVVYKARDKETGRI-----VAIKKIkLG--ERKEAKDGINftalrEIKLLQELKHPNIIGLLDVFGHKSNI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 MVVMELVtGGDLRKYLQ------TTQNIpK---LQILwfamnvaSGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGL 322
Cdd:cd07841  78 NLVFEFM-ETDLEKVIKdksivlTPADI-KsymLMTL-------RGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGL 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17542550 323 SLQ----GTEVTTknleKAPIRWL-APESL-KSGMFNEKTDVWSYGVFLTELMARcehDPLYP 379
Cdd:cd07841 149 ARSfgspNRKMTH----QVVTRWYrAPELLfGARHYGVGVDMWSVGCIFAELLLR---VPFLP 204
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
177-427 7.89e-17

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: 80.60  E-value: 7.89e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVfkgqyKAVGSTNPPIEVAVKRI-LGNAKRKQIQEFC-NEAQIMTVLQHENIVAFYG-FASLEEPIMV 253
Cdd:cd14165   5 LGINLGEGSYAKV-----KSAYSERLKCNVAIKIIdKKKAPDDFVEKFLpRELEILARLNHKSIIKTYEiFETSDGKVYI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ------GT 327
Cdd:cd14165  80 VMELGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRclrdenGR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 328 EVTTKNLEKAPIrWLAPESLKSGMFNEKT-DVWSYGVFLTELMarCEHDPLYPKSLKDakawILTEERPHKME----NGD 402
Cdd:cd14165 160 IVLSKTFCGSAA-YAAPEVLQGIPYDPRIyDIWSLGVILYIMV--CGSMPYDDSNVKK----MLKIQKEHRVRfprsKNL 232
                       250       260
                ....*....|....*....|....*
gi 17542550 403 PKELMVLIDACCERNPNERLNFNTV 427
Cdd:cd14165 233 TSECKDLIYRLLQPDVSQRLCIDEV 257
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
181-370 8.13e-17

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: 80.53  E-value: 8.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQykavgSTNPPIEVAVKRILGNAKRkQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd06624  16 LGKGTFGVVYAAR-----DLSTQVRIAIKEIPERDSR-EVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQTTQNIPKLQ---ILWFAMNVASGMRHLSSKGIIHRDLAARNCLV-TQDLKAKISDFGLS--LQGTEVTTKNL 334
Cdd:cd06624  90 GSLSALLRSKWGPLKDNentIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVnTYSGVVKISDFGTSkrLAGINPCTETF 169
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 17542550 335 eKAPIRWLAPESLKSGM--FNEKTDVWSYGVFLTElMA 370
Cdd:cd06624 170 -TGTLQYMAPEVIDKGQrgYGPPADIWSLGCTIIE-MA 205
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
179-421 8.20e-17

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


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 80.19  E-value: 8.20e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVfkgqYKAVGSTNPPIeVAVKRILGNAKRKQ--IQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVME 256
Cdd:cd06607   7 REIGHGSFGAV----YYARNKRTSEV-VAIKKMSYSGKQSTekWQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTG--GDL----RKYLQttqnipKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGlslQGTEVT 330
Cdd:cd06607  82 YCLGsaSDIvevhKKPLQ------EVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFG---SASLVC 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 331 TKNLEKAPIRWLAPE---SLKSGMFNEKTDVWSYGVFLTELMARceHDPLYPKSLKDAKAWILTEERPHKMENGDPKELM 407
Cdd:cd06607 153 PANSFVGTPYWMAPEvilAMDEGQYDGKVDVWSLGITCIELAER--KPPLFNMNAMSALYHIAQNDSPTLSSGEWSDDFR 230
                       250
                ....*....|....
gi 17542550 408 VLIDACCERNPNER 421
Cdd:cd06607 231 NFVDSCLQKIPQDR 244
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
180-421 9.85e-17

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: 80.54  E-value: 9.85e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGN---AKRKQIqefCNEAQIMTVLQHENIVAFYGfASLEEP---IMV 253
Cdd:cd06621   8 SLGEGAGGSVTKCRLRNTKTI-----FALKTITTDpnpDVQKQI---LRELEINKSCASPYIVKYYG-AFLDEQdssIGI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDL----RKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS------ 323
Cdd:cd06621  79 AMEYCEGGSLdsiyKKVKKKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSgelvns 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 324 LQGTEVTTKnlekapiRWLAPESLKSGMFNEKTDVWSYGVFLTELMARC---EHDPLYPKSLKDAKAWILTEERPH-KME 399
Cdd:cd06621 159 LAGTFTGTS-------YYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRfpfPPEGEPPLGPIELLSYIVNMPNPElKDE 231
                       250       260
                ....*....|....*....|....*.
gi 17542550 400 NGD----PKELMVLIDACCERNPNER 421
Cdd:cd06621 232 PENgikwSESFKDFIEKCLEKDGTRR 257
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
181-371 1.01e-16

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: 80.17  E-value: 1.01e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFkgqykaVGSTNPPIEVAVKRILGN-----AKRKQIQEFCNEAQIMTVLQHENIVAFYGfASLEEPIM-VV 254
Cdd:cd06631   9 LGKGAYGTVY------CGLTSTGQLIAVKQVELDtsdkeKAEKEYEKLQEEVDLLKTLKHVNIVGYLG-TCLEDNVVsIF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFG----LSLQGTEVT 330
Cdd:cd06631  82 MEFVPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGcakrLCINLSSGS 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17542550 331 TKNLEKA----PIrWLAPESLKSGMFNEKTDVWSYGVFLTELMAR 371
Cdd:cd06631 162 QSQLLKSmrgtPY-WMAPEVINETGHGRKSDIWSIGCTVFEMATG 205
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
254-387 1.19e-16

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: 81.20  E-value: 1.19e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGT--EVTT 331
Cdd:cd05616  79 VMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIwdGVTT 158
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17542550 332 KNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMAR----------------CEHDPLYPKSL-KDAKA 387
Cdd:cd05616 159 KTFCGTP-DYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGqapfegededelfqsiMEHNVAYPKSMsKEAVA 230
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
179-422 1.42e-16

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: 80.89  E-value: 1.42e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKRIlgnaKRKQIQE----FCN--EAQIMTV-LQHENIVAFYGFASLEEPI 251
Cdd:cd05592   1 KVLGKGSFGKVMLAELKGTNQY-----FAIKAL----KKDVVLEdddvECTmiERRVLALaSQHPFLTHLFCTFQTESHL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 MVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGT--EV 329
Cdd:cd05592  72 FFVMEYLNGGDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIygEN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 TTKNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELM------ARCEHDPLYpkslkdakaWILTEERPH--KMENG 401
Cdd:cd05592 152 KASTFCGTP-DYIAPEILKGQKYNQSVDWWSFGVLLYEMLigqspfHGEDEDELF---------WSICNDTPHypRWLTK 221
                       250       260
                ....*....|....*....|.
gi 17542550 402 DPKELMVLIdacCERNPNERL 422
Cdd:cd05592 222 EAASCLSLL---LERNPEKRL 239
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
179-422 1.81e-16

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: 80.34  E-value: 1.81e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKrILgnaKRKQIQEFCNEAQIMT---VL----QHENIVAFYGFASLEEPI 251
Cdd:cd05570   1 KVLGKGSFGKVMLAERKKTDEL-----YAIK-VL---KKEVIIEDDDVECTMTekrVLalanRHPFLTGLHACFQTEDRL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 MVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGT--EV 329
Cdd:cd05570  72 YFVMEYVNGGDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIwgGN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 TTKNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMA--------------RC--EHDPLYPKSLkdakawiltee 393
Cdd:cd05570 152 TTSTFCGTP-DYIAPEILREQDYGFSVDWWALGVLLYEMLAgqspfegddedelfEAilNDEVLYPRWL----------- 219
                       250       260
                ....*....|....*....|....*....
gi 17542550 394 rphkmengdPKELMVLIDACCERNPNERL 422
Cdd:cd05570 220 ---------SREAVSILKGLLTKDPARRL 239
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
177-369 2.07e-16

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: 79.30  E-value: 2.07e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGStnppiEVAVKRILGNAKRKQIQEFCN----EAQIMTVLQHENIVAFYGfaSLEEP-- 250
Cdd:cd06653   6 LGKLLGRGAFGEVYLCYDADTGR-----ELAVKQVPFDPDSQETSKEVNalecEIQLLKNLRHDRIVQYYG--CLRDPee 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 --IMVVMELVTGGDLRKYLQT----TQNIPKLqilwFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS- 323
Cdd:cd06653  79 kkLSIFVEYMPGGSVKDQLKAygalTENVTRR----YTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASk 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17542550 324 ------LQGTEVttKNLEKAPIrWLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd06653 155 riqticMSGTGI--KSVTGTPY-WMSPEVISGEGYGRKADVWSVACTVVEML 203
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
180-379 2.21e-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: 79.45  E-value: 2.21e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGSTnppieVAVKRIlgnakrKQIQEF-------CNEAQIMTVLQHENIVAFYGFASLEEPIM 252
Cdd:cd07829   6 KLGEGTYGVVYKAKDKKTGEI-----VALKKI------RLDNEEegipstaLREISLLKELKHPNIVKLLDVIHTENKLY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGgDLRKYLQT-TQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGT---- 327
Cdd:cd07829  75 LVFEYCDQ-DLKKYLDKrPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAFGiplr 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17542550 328 ----EVTTknlekapiRW-LAPESLksgmFNEKT-----DVWSYGVFLTELMARCehdPLYP 379
Cdd:cd07829 154 tythEVVT--------LWyRAPEIL----LGSKHystavDIWSVGCIFAELITGK---PLFP 200
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
215-430 2.27e-16

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: 78.90  E-value: 2.27e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 215 AKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSS 294
Cdd:cd14188  40 SKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHE 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 295 KGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEVTTKNLEKAPiRWLAPESLKSGMFNEKTDVWSYG-VFLTELMAR 371
Cdd:cd14188 120 QEILHRDLKLGNFFINENMELKVGDFGLAarLEPLEHRRRTICGTP-NYLSPEVLNKQGHGCESDIWALGcVMYTMLLGR 198
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17542550 372 cehDPLYPKSLKDAKAWIltEERPHKMengdPKELMV----LIDACCERNPNERLNFNTVKRQ 430
Cdd:cd14188 199 ---PPFETTNLKETYRCI--REARYSL----PSSLLApakhLIASMLSKNPEDRPSLDEIIRH 252
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
176-365 2.57e-16

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: 78.91  E-value: 2.57e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 176 NLDKKLGCGAFGEVFKGQYKAVGStnppiEVAVKrILGNA----KRKQIQefcNEAQIMTVLQHENIVAFYGFASLEEPI 251
Cdd:cd14095   3 DIGRVIGDGNFAVVKECRDKATDK-----EYALK-IIDKAkckgKEHMIE---NEVAILRRVKHPNIVQLIEEYDTDTEL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 MVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQD----LKAKISDFGLSlqgT 327
Cdd:cd14095  74 YLVMELVKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHedgsKSLKLADFGLA---T 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17542550 328 EVttknleKAPI-------RWLAPESLKSGMFNEKTDVWSYGVFL 365
Cdd:cd14095 151 EV------KEPLftvcgtpTYVAPEILAETGYGLKVDIWAAGVIT 189
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
179-422 2.59e-16

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: 80.51  E-value: 2.59e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTNPpIEVAVKRILgnAKRKQIQEFCNEAQIMTVLQHENIVAF-YGFASlEEPIMVVMEL 257
Cdd:cd05593  21 KLLGKGTFGKVILVREKASGKYYA-MKILKKEVI--IAKDEVAHTLTESRVLKNTRHPFLTSLkYSFQT-KDRLCFVMEY 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQG-TEVTTKNLEK 336
Cdd:cd05593  97 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGiTDAATMKTFC 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 337 APIRWLAPESLKSGMFNEKTDVWSYGVFLTELMarCEHDPLYPKSLKDAKAWILTEE-RPHKMENGDPKELM--VLIdac 413
Cdd:cd05593 177 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM--CGRLPFYNQDHEKLFELILMEDiKFPRTLSADAKSLLsgLLI--- 251

                ....*....
gi 17542550 414 ceRNPNERL 422
Cdd:cd05593 252 --KDPNKRL 258
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
175-421 2.71e-16

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: 78.97  E-value: 2.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQykavgSTNPPIEVA----VKRILGNAKRKQIQEfcnEAQIMTVLQHENIVAFYGF----AS 246
Cdd:cd14032   3 LKFDIELGRGSFKTVYKGL-----DTETWVEVAwcelQDRKLTKVERQRFKE---EAEMLKGLQHPNIVRFYDFwescAK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 247 LEEPIMVVMELVTGGDLRKYLQTTQNI-PKLQILWfAMNVASGM--RHLSSKGIIHRDLAARNCLVTQDL-KAKISDFGL 322
Cdd:cd14032  75 GKRCIVLVTELMTSGTLKTYLKRFKVMkPKVLRSW-CRQILKGLlfLHTRTPPIIHRDLKCDNIFITGPTgSVKIGDLGL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 323 SLQGTEVTTKNLEKAPiRWLAPESLKSgMFNEKTDVWSYGVFLTElMARCEhdplYPKSLKDAKAWILTEE----RPHKM 398
Cdd:cd14032 154 ATLKRASFAKSVIGTP-EFMAPEMYEE-HYDESVDVYAFGMCMLE-MATSE----YPYSECQNAAQIYRKVtcgiKPASF 226
                       250       260
                ....*....|....*....|...
gi 17542550 399 ENGDPKELMVLIDACCERNPNER 421
Cdd:cd14032 227 EKVTDPEIKEIIGECICKNKEER 249
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
179-430 3.19e-16

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: 78.63  E-value: 3.19e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFY-GFASLEEPIMVVME 256
Cdd:cd08223   6 RVIGKGSYGEVWLVRHKRDRK-----QYVIKKLnLKNASKRERKAAEQEAKLLSKLKHPNIVSYKeSFEGEDGFLYIVMG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYL--QTTQNIPKLQIL-WFaMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEVTT 331
Cdd:cd08223  81 FCEGGDLYTRLkeQKGVLLEERQVVeWF-VQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIArvLESSSDMA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 332 KNLEKAPIrWLAPESLKSGMFNEKTDVWSYGVFLTElMARCEHdPLYPKSLKDAKAWILTEERPhKMENGDPKELMVLID 411
Cdd:cd08223 160 TTLIGTPY-YMSPELFSNKPYNHKSDVWALGCCVYE-MATLKH-AFNAKDMNSLVYKILEGKLP-PMPKQYSPELGELIK 235
                       250
                ....*....|....*....
gi 17542550 412 ACCERNPNERLNFNTVKRQ 430
Cdd:cd08223 236 AMLHQDPEKRPSVKRILRQ 254
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
181-369 3.25e-16

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: 78.46  E-value: 3.25e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGstnppIEVAVKRIlgNAKRKQIQEFCNEAQIMTVLQHENIVAFY-GFASLEEPIMVvMELVT 259
Cdd:cd14006   1 LGRGRFGVVKRCIEKATG-----REFAAKFI--PKRDKKKEAVLREISILNQLQHPRIIQLHeAYESPTELVLI-LELCS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 260 GGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVT--QDLKAKISDFGLSLQ-GTEVTTKNLEK 336
Cdd:cd14006  73 GGELLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLAdrPSPQIKIIDFGLARKlNPGEELKEIFG 152
                       170       180       190
                ....*....|....*....|....*....|...
gi 17542550 337 APiRWLAPESLKSGMFNEKTDVWSYGVfLTELM 369
Cdd:cd14006 153 TP-EFVAPEIVNGEPVSLATDMWSIGV-LTYVL 183
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
179-381 3.31e-16

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: 78.74  E-value: 3.31e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGsTNPPIEVAVKRILGNAKRKQIQefcNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd14097   7 RKLGQGSFGVVIEATHKETQ-TKWAIKKINREKAGSSAVKLLE---REVDILKHVNHAHIIHLEEVFETPKRMYLVMELC 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQD-------LKAKISDFGLSLQGTEVTT 331
Cdd:cd14097  83 EDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSiidnndkLNIKVTDFGLSVQKYGLGE 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17542550 332 KNLEKA---PIrWLAPESLKSGMFNEKTDVWSYGVFLTELMarCEHDPLYPKS 381
Cdd:cd14097 163 DMLQETcgtPI-YMAPEVISAHGYSQQCDIWSIGVIMYMLL--CGEPPFVAKS 212
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
179-421 3.36e-16

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: 79.71  E-value: 3.36e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFkgqYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd06635  31 REIGHGSFGAVY---FARDVRTSEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYC 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGlslQGTEVTTKNLEKAP 338
Cdd:cd06635 108 LGSASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG---SASIASPANSFVGT 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 339 IRWLAPE---SLKSGMFNEKTDVWSYGVFLTELMARceHDPLYPKSLKDAKAWILTEERPHKMENGDPKELMVLIDACCE 415
Cdd:cd06635 185 PYWMAPEvilAMDEGQYDGKVDVWSLGITCIELAER--KPPLFNMNAMSALYHIAQNESPTLQSNEWSDYFRNFVDSCLQ 262

                ....*.
gi 17542550 416 RNPNER 421
Cdd:cd06635 263 KIPQDR 268
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
181-435 3.48e-16

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: 78.70  E-value: 3.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGstnppiEVAVKRILGNAKRKQIQE-FCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVT 259
Cdd:cd14027   1 LDSGGFGKVSLCFHRTQG------LVVLKTVYTGPNCIEHNEaLLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYME 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 260 GGDLRKYLQTTQnIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSL-----QGTEVTTKNL 334
Cdd:cd14027  75 KGNLMHVLKKVS-VPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsKLTKEEHNEQ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 335 EK---------APIRWLAPESLKS--GMFNEKTDVWSYGVFLTELMARCEHdplYPKSLKDAKAW--ILTEERPHKMENG 401
Cdd:cd14027 154 REvdgtakknaGTLYYMAPEHLNDvnAKPTEKSDVYSFAIVLWAIFANKEP---YENAINEDQIImcIKSGNRPDVDDIT 230
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 17542550 402 D--PKELMVLIDACCERNPNERLNFNTVKRQITDIY 435
Cdd:cd14027 231 EycPREIIDLMKLCWEANPEARPTFPGIEEKFRPFY 266
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
181-363 4.09e-16

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: 78.04  E-value: 4.09e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGStnppiEVAVKrILGNAKRKQIQEFCNEAQIMTVLQHENIVAFY-GFASLEEPIMvVMELVT 259
Cdd:cd14103   1 LGRGKFGTVYRCVEKATGK-----ELAAK-FIKCRKAKDREDVRNEIEIMNQLRHPRLLQLYdAFETPREMVL-VMEYVA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 260 GGDL-RKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARN--CLVTQDLKAKISDFGLSlqgtevtTKNLEK 336
Cdd:cd14103  74 GGELfERVVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENilCVSRTGNQIKIIDFGLA-------RKYDPD 146
                       170       180       190
                ....*....|....*....|....*....|....
gi 17542550 337 APIR-------WLAPESLKSGMFNEKTDVWSYGV 363
Cdd:cd14103 147 KKLKvlfgtpeFVAPEVVNYEPISYATDMWSVGV 180
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
179-428 5.18e-16

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: 79.24  E-value: 5.18e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTNPpIEVAVKRILGNaKRKQIQEFCNEAQIMTVLQHENIVAF-YGFASLEEpIMVVMEL 257
Cdd:cd05604   2 KVIGKGSFGKVLLAKRKRDGKYYA-VKVLQKKVILN-RKEQKHIMAERNVLLKNVKHPFLVGLhYSFQTTDK-LYFVLDF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEV--TTKNLE 335
Cdd:cd05604  79 VNGGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNsdTTTTFC 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 336 KAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEhdPLYPKSLKDAKAWILteERPHKMENGDPKELMVLIDACCE 415
Cdd:cd05604 159 GTP-EYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLP--PFYCRDTAEMYENIL--HKPLVLRPGISLTAWSILEELLE 233
                       250
                ....*....|....*..
gi 17542550 416 RNPNERL----NFNTVK 428
Cdd:cd05604 234 KDRQLRLgakeDFLEIK 250
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
171-381 5.53e-16

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


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 78.50  E-value: 5.53e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 171 IHSTINLDKKLGCGAFGEVFKGQYKAVGSTnppieVAVKRIlgnaKRKQI---QEFCNEAQIMTVLQHENIVAFYGFASL 247
Cdd:cd14166   1 IRETFIFMEVLGSGAFSEVYLVKQRSTGKL-----YALKCI----KKSPLsrdSSLENEIAVLKRIKHENIVTLEDIYES 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 248 EEPIMVVMELVTGGDLRK-------YLQTTQNIPKLQILwfamnvaSGMRHLSSKGIIHRDLAARNCL-VTQDLKAK--I 317
Cdd:cd14166  72 TTHYYLVMQLVSGGELFDrilergvYTEKDASRVINQVL-------SAVKYLHENGIVHRDLKPENLLyLTPDENSKimI 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17542550 318 SDFGLSLQGTEVTTKNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMarCEHDPLYPKS 381
Cdd:cd14166 145 TDFGLSKMEQNGIMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVITYILL--CGYPPFYEET 205
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
181-372 5.72e-16

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: 78.16  E-value: 5.72e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGStnppiEVAVK--RILGNAKRKQ-----IQEFCNEAQIMTVLQ-HENIVAFYGFASLEEPIM 252
Cdd:cd14093  11 LGRGVSSTVRRCIEKETGQ-----EFAVKiiDITGEKSSENeaeelREATRREIEILRQVSgHPNIIELHDVFESPTFIF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTE-VTT 331
Cdd:cd14093  86 LVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDEgEKL 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 17542550 332 KNLEKAPiRWLAPESLKSGMF------NEKTDVWSYGVFLTELMARC 372
Cdd:cd14093 166 RELCGTP-GYLAPEVLKCSMYdnapgyGKEVDMWACGVIMYTLLAGC 211
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
180-421 6.14e-16

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: 77.81  E-value: 6.14e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGSTnppieVAVKR----ILGNAKR-KQIQEFcnEAQiMTVLQHENIVAFYgfASLEEP--IM 252
Cdd:cd13997   7 QIGSGSFSEVFKVRSKVDGCL-----YAVKKskkpFRGPKERaRALREV--EAH-AALGQHPNIVRYY--SSWEEGghLY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYLQT---TQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSlqgTEV 329
Cdd:cd13997  77 IQMELCENGSLQDALEElspISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLA---TRL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 TTK-NLEKAPIRWLAPESLK-SGMFNEKTDVWSYGVFLTELmarcehdplypkslkdAKAWILTEERP--HKMENGDP-- 403
Cdd:cd13997 154 ETSgDVEEGDSRYLAPELLNeNYTHLPKADIFSLGVTVYEA----------------ATGEPLPRNGQqwQQLRQGKLpl 217
                       250       260
                ....*....|....*....|....*
gi 17542550 404 -------KELMVLIDACCERNPNER 421
Cdd:cd13997 218 ppglvlsQELTRLLKVMLDPDPTRR 242
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
179-421 9.54e-16

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: 78.14  E-value: 9.54e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVfkgqYKAVGSTNPPIeVAVKRIL--GNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVME 256
Cdd:cd06634  21 REIGHGSFGAV----YFARDVRNNEV-VAIKKMSysGKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVME 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGlslQGTEVTTKNLEK 336
Cdd:cd06634  96 YCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFG---SASIMAPANSFV 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 337 APIRWLAPE---SLKSGMFNEKTDVWSYGVFLTELMARceHDPLYPKSLKDAKAWILTEERPHKMENGDPKELMVLIDAC 413
Cdd:cd06634 173 GTPYWMAPEvilAMDEGQYDGKVDVWSLGITCIELAER--KPPLFNMNAMSALYHIAQNESPALQSGHWSEYFRNFVDSC 250

                ....*...
gi 17542550 414 CERNPNER 421
Cdd:cd06634 251 LQKIPQDR 258
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
178-449 9.65e-16

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: 78.16  E-value: 9.65e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 178 DKKLGCGAFGEVFKGQYKAVGSTNPpIEVAVKRILGNAKRkqiqefcnEAQIMTVLQ-HENIVAFYGFASLEEPIMVVME 256
Cdd:cd14179  12 DKPLGEGSFSICRKCLHKKTNQEYA-VKIVSKRMEANTQR--------EIAALKLCEgHPNIVKLHEVYHDQLHTFLVME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVT---QDLKAKISDFGLSLqgTEVTTKN 333
Cdd:cd14179  83 LLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTdesDNSEIKIIDFGFAR--LKPPDNQ 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 334 LEKAP---IRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHDPLYPKSLKDAKAwiltEERPHKMENGD-------- 402
Cdd:cd14179 161 PLKTPcftLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKSLTCTSA----EEIMKKIKQGDfsfegeaw 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 17542550 403 ---PKELMVLIDACCERNPNERLNFNTVKrqitdiYMEALNKGPQDGRKP 449
Cdd:cd14179 237 knvSQEAKDLIQGLLTVDPNKRIKMSGLR------YNEWLQDGSQLSSNP 280
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
181-381 9.89e-16

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: 78.49  E-value: 9.89e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGstnppIEVAVKRI------LGNAKRKQiqefcNEAQIMTVLQHENIV----AFYGFASLE-- 248
Cdd:cd07851  23 VGSGAYGQVCSAFDTKTG-----RKVAIKKLsrpfqsAIHAKRTY-----RELRLLKHMKHENVIglldVFTPASSLEdf 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 249 EPIMVVMELVtGGDLRKYLQTtQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTE 328
Cdd:cd07851  93 QDVYLVTHLM-GADLNNIVKC-QKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHTDD 170
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 329 -----VTTknlekapiRW-LAPESLKSGM-FNEKTDVWSYGVFLTELMARcehDPLYPKS 381
Cdd:cd07851 171 emtgyVAT--------RWyRAPEIMLNWMhYNQTVDIWSVGCIMAELLTG---KTLFPGS 219
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
179-371 1.01e-15

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: 78.21  E-value: 1.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKavgSTNPPIEVAVKRIlGNAKRKQIqeFCNEA-QIMTVLQ----HENIVAFYG----FASLEE 249
Cdd:cd07857   6 KELGQGAYGIVCSARNA---ETSEEETVAIKKI-TNVFSKKI--LAKRAlRELKLLRhfrgHKNITCLYDmdivFPGNFN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 250 PIMVVMELVTGgDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEV 329
Cdd:cd07857  80 ELYLYEELMEA-DLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGFSEN 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 TTKN----LEKAPIRWL-APESLKSgmFNEKT---DVWSYGVFLTELMAR 371
Cdd:cd07857 159 PGENagfmTEYVATRWYrAPEIMLS--FQSYTkaiDVWSVGCILAELLGR 206
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
174-368 1.54e-15

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: 76.97  E-value: 1.54e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 174 TINLDKKLGCGAFGEVFKGQYKAVGStnppiEVAVKrILgNAKRKQIQEFCNEAQIMTVLQ-HENIVAFYGFASLEE--- 249
Cdd:cd06638  19 TWEIIETIGKGTYGKVFKVLNKKNGS-----KAAVK-IL-DPIHDIDEEIEAEYNILKALSdHPNVVKFYGMYYKKDvkn 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 250 --PIMVVMELVTGG---DLRK-YLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS 323
Cdd:cd06638  92 gdQLWLVLELCNGGsvtDLVKgFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVS 171
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17542550 324 LQGTEVT-TKNLEKAPIRWLAPESLK-----SGMFNEKTDVWSYGVFLTEL 368
Cdd:cd06638 172 AQLTSTRlRRNTSVGTPFWMAPEVIAceqqlDSTYDARCDVWSLGITAIEL 222
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
181-363 1.64e-15

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: 76.97  E-value: 1.64e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGqYKAVGSTnppiEVAVKRILGN------AKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMV- 253
Cdd:cd13990   8 LGKGGFSEVYKA-FDLVEQR----YVACKIHQLNkdwseeKKQNYIKHALREYEIHKSLDHPRIVKLYDVFEIDTDSFCt 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQNIP-KLQILWFaMNVASGMRHLSSK--GIIHRDLAARNCLVTQDLKA---KISDFGLS---- 323
Cdd:cd13990  83 VLEYCDGNDLDFYLKQHKSIPeREARSII-MQVVSALKYLNEIkpPIIHYDLKPGNILLHSGNVSgeiKITDFGLSkimd 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17542550 324 -----LQGTEVTTKNlekAPIRW-LAPESLKSG----MFNEKTDVWSYGV 363
Cdd:cd13990 162 desynSDGMELTSQG---AGTYWyLPPECFVVGktppKISSKVDVWSVGV 208
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
177-370 1.72e-15

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: 76.52  E-value: 1.72e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGN--AKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:cd14081   5 LGKTLGKGQTGLVKLAKHCVTGQK-----VAIKIVNKEklSKESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGL-SLQGTEVTTKN 333
Cdd:cd14081  80 LEYVSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMaSLQPEGSLLET 159
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 17542550 334 LEKAPiRWLAPESLKSGMFN-EKTDVWSYGVFLTELMA 370
Cdd:cd14081 160 SCGSP-HYACPEVIKGEKYDgRKADIWSCGVILYALLV 196
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
180-379 1.94e-15

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


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 76.93  E-value: 1.94e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGStnppiEVAVKRIlgNAKRKQIQEF--CNEAQIMTVLQ-HENIVAFY--------GFASLe 248
Cdd:cd07831   6 KIGEGTFSEVLKAQSRKTGK-----YYAIKCM--KKHFKSLEQVnnLREIQALRRLSpHPNILRLIevlfdrktGRLAL- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 249 epIMVVM-----ELVTGgdlRKYLqttqnIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLkAKISDFGlS 323
Cdd:cd07831  78 --VFELMdmnlyELIKG---RKRP-----LPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDI-LKLADFG-S 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17542550 324 LQGTEVTTKNLEKAPIRWL-APES-LKSGMFNEKTDVWSYGVFLTELMARcehDPLYP 379
Cdd:cd07831 146 CRGIYSKPPYTEYISTRWYrAPEClLTDGYYGPKMDIWAVGCVFFEILSL---FPLFP 200
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
171-379 2.22e-15

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: 77.41  E-value: 2.22e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 171 IHSTINLDKKLGCGAFGEVFKGQYKAVGStnppiEVAVKRI------LGNAKRKqiqefCNEAQIMTVLQHENIVAFY-- 242
Cdd:cd07855   3 VGDRYEPIETIGSGAYGVVCSAIDTKSGQ-----KVAIKKIpnafdvVTTAKRT-----LRELKILRHFKHDNIIAIRdi 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 243 ----GFASLEEPIMVVMELVTGgDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKIS 318
Cdd:cd07855  73 lrpkVPYADFKDVYVVLDLMES-DLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIG 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17542550 319 DFG----LSLQGTEVTTKNLEKAPIRWL-APESLKSgmFNEKT---DVWSYGVFLTELMARcehDPLYP 379
Cdd:cd07855 152 DFGmargLCTSPEEHKYFMTEYVATRWYrAPELMLS--LPEYTqaiDMWSVGCIFAEMLGR---RQLFP 215
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
180-379 2.34e-15

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: 77.34  E-value: 2.34e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGstnppIEVAVKRILGNAKrkqiQEFC----NEAQIMTVLQHENIVAFY------GFASLEE 249
Cdd:cd07849  12 YIGEGAYGMVCSAVHKPTG-----QKVAIKKISPFEH----QTYClrtlREIKILLRFKHENIIGILdiqrppTFESFKD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 250 pIMVVMELVTGgDLRKYLQTtQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS---LQG 326
Cdd:cd07849  83 -VYIVQELMET-DLYKLIKT-QHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLAriaDPE 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17542550 327 TEVTTKNLEKAPIRWL-APE-SLKSGMFNEKTDVWSYGVFLTELMARcehDPLYP 379
Cdd:cd07849 160 HDHTGFLTEYVATRWYrAPEiMLNSKGYTKAIDIWSVGCILAEMLSN---RPLFP 211
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
181-363 2.76e-15

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 76.76  E-value: 2.76e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGStnppiEVAVKRI--LGNAKRKQIQEfcNEAQIMTVLQHENIVAFygFASLEEPI----MVV 254
Cdd:cd13988   1 LGQGATANVFRGRHKKTGD-----LYAVKVFnnLSFMRPLDVQM--REFEVLKKLNHKNIVKL--FAIEEELTtrhkVLV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTTQN---IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCL--VTQDLKA--KISDFG------ 321
Cdd:cd13988  72 MELCPCGSLYTVLEEPSNaygLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQSvyKLTDFGaarele 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17542550 322 -----LSLQGTE--VTTKNLEKAPIRWLAPEslksgMFNEKTDVWSYGV 363
Cdd:cd13988 152 ddeqfVSLYGTEeyLHPDMYERAVLRKDHQK-----KYGATVDLWSIGV 195
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
181-369 2.97e-15

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 77.00  E-value: 2.97e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFkgqykAVGSTNPPIEVAVKRI------LGNAKRKQiqefcNEAQIMTVLQHENIVA----FYGFASLEE- 249
Cdd:cd07877  25 VGSGAYGSVC-----AAFDTKTGLRVAVKKLsrpfqsIIHAKRTY-----RELRLLKHMKHENVIGlldvFTPARSLEEf 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 250 -PIMVVMELVtGGDLRKYLQTtQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTE 328
Cdd:cd07877  95 nDVYLVTHLM-GADLNNIVKC-QKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDD 172
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 17542550 329 VTTKNLekaPIRWL-APESLKSGM-FNEKTDVWSYGVFLTELM 369
Cdd:cd07877 173 EMTGYV---ATRWYrAPEIMLNWMhYNQTVDIWSVGCIMAELL 212
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
181-369 3.29e-15

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: 77.01  E-value: 3.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVfkgqyKAVGSTNPPIEVAVKRI------LGNAKRKQiqefcNEAQIMTVLQHENIVA----FYGFASLEE- 249
Cdd:cd07878  23 VGSGAYGSV-----CSAYDTRLRQKVAVKKLsrpfqsLIHARRTY-----RELRLLKHMKHENVIGlldvFTPATSIENf 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 250 -PIMVVMELVtGGDLRKYLQTtQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTE 328
Cdd:cd07878  93 nEVYLVTNLM-GADLNNIVKC-QKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQADD 170
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 17542550 329 VTTKNLekaPIRWL-APESLKSGM-FNEKTDVWSYGVFLTELM 369
Cdd:cd07878 171 EMTGYV---ATRWYrAPEIMLNWMhYNQTVDIWSVGCIMAELL 210
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
179-378 3.30e-15

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: 76.30  E-value: 3.30e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRIlgNAKRKQIQEFC-NEAQIMTVLQHENIVAFYGFASLEEPIMVVMEL 257
Cdd:cd06654  26 EKIGQGASGTVYTAMDVATGQ-----EVAIRQM--NLQQQPKKELIiNEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTqNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGT-EVTTKNLEK 336
Cdd:cd06654  99 LAGGSLTDVVTET-CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITpEQSKRSTMV 177
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 17542550 337 APIRWLAPESLKSGMFNEKTDVWSYGVFLTELMarcEHDPLY 378
Cdd:cd06654 178 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMI---EGEPPY 216
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
177-369 3.36e-15

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: 75.50  E-value: 3.36e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGSTnppieVAVKRI----LG-NAKRKQIqefcnEAQIMTVLQHENIVAFYGFASLEEPI 251
Cdd:cd14078   7 LHETIGSGGFAKVKLATHILTGEK-----VAIKIMdkkaLGdDLPRVKT-----EIEALKNLSHQHICRLYHVIETDNKI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 MVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTT 331
Cdd:cd14078  77 FMVLEYCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGGMD 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 17542550 332 KNLEK---APIrWLAPEsLKSGM--FNEKTDVWSYGVFLTELM 369
Cdd:cd14078 157 HHLETccgSPA-YAAPE-LIQGKpyIGSEADVWSMGVLLYALL 197
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
181-422 3.85e-15

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: 75.80  E-value: 3.85e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTNPPIEVAVKRIlgnAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd05631   8 LGKGGFGEVCACQVRATGKMYACKKLEKKRI---KKRKGEAMALNEKRILEKVNSRFVVSLAYAYETKDALCLVLTIMNG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQTTQN--IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLEKAP 338
Cdd:cd05631  85 GDLKFHIYNMGNpgFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPEGETVRGRVGT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 339 IRWLAPESLKSGMFNEKTDVWSYGVFLTELMArcEHDPL--YPKSLK----DAKAWILTEERPHKMENgDPKELMVLIDA 412
Cdd:cd05631 165 VGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQ--GQSPFrkRKERVKreevDRRVKEDQEEYSEKFSE-DAKSICRMLLT 241
                       250
                ....*....|
gi 17542550 413 cceRNPNERL 422
Cdd:cd05631 242 ---KNPKERL 248
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
171-381 3.95e-15

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 75.82  E-value: 3.95e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 171 IHSTINLDKkLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEP 250
Cdd:cd07871   4 LETYVKLDK-LGEGTYATVFKGRSKLTENL-----VALKEIRLEHEEGAPCTAIREVSLLKNLKHANIVTLHDIIHTERC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMELVTGgDLRKYLQTTQNIPKLQ-ILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSlQGTEV 329
Cdd:cd07871  78 LTLVFEYLDS-DLKQYLDNCGNLMSMHnVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLA-RAKSV 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17542550 330 TTKNLEKAPIR-WLAPES--LKSGMFNEKTDVWSYGVFLTELMArceHDPLYPKS 381
Cdd:cd07871 156 PTKTYSNEVVTlWYRPPDvlLGSTEYSTPIDMWGVGCILYEMAT---GRPMFPGS 207
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
254-382 4.40e-15

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: 76.57  E-value: 4.40e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGT--EVTT 331
Cdd:cd05615  89 VMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMveGVTT 168
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17542550 332 KNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMAR----------------CEHDPLYPKSL 382
Cdd:cd05615 169 RTFCGTP-DYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGqppfdgededelfqsiMEHNVSYPKSL 234
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
181-431 5.03e-15

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: 75.33  E-value: 5.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKG-QYKAVGSTNPPIEVAVKRIlgNAKRKQIQE-FCNEAQIMTVLQHENIVAFYGFASLEEPIMVvMELV 258
Cdd:cd14208   7 LGKGSFTKIYRGlRTDEEDDERCETEVLLKVM--DPTHGNCQEsFLEAASIMSQISHKHLVLLHGVCVGKDSIMV-QEFV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQNIPKLQILW---FAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKA------KISDFGLSLQgteV 329
Cdd:cd14208  84 CHGALDLYLKKQQQKGPVAISWklqVVKQLAYALNYLEDKQLVHGNVSAKKVLLSREGDKgsppfiKLSDPGVSIK---V 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 TTKNLEKAPIRWLAPESLKSGM-FNEKTDVWSYGVFLTELMArcehDPLYPKSLKDAKAWILTEERPHKMENGDPKELMV 408
Cdd:cd14208 161 LDEELLAERIPWVAPECLSDPQnLALEADKWGFGATLWEIFS----GGHMPLSALDPSKKLQFYNDRKQLPAPHWIELAS 236
                       250       260
                ....*....|....*....|...
gi 17542550 409 LIDACCERNPNERLNFNTVKRQI 431
Cdd:cd14208 237 LIQQCMSYNPLLRPSFRAIIRDL 259
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
181-421 5.12e-15

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: 75.91  E-value: 5.12e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTnppIEVAVKRILGNAKRKQIQEFcneAQIMTVLQHENIVAFYGF------ASLEEPIMVV 254
Cdd:cd06637  14 VGNGTYGQVYKGRHVKTGQL---AAIKVMDVTGDEEEEIKQEI---NMLKKYSHHRNIATYYGAfikknpPGMDDQLWLV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTTQ--NIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ-GTEVTT 331
Cdd:cd06637  88 MEFCGAGSVTDLIKNTKgnTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQlDRTVGR 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 332 KNLEKAPIRWLAPESLK-----SGMFNEKTDVWSYGVFLTELM----ARCEHDPLYPKSLkdakawILTEERPHKMENGD 402
Cdd:cd06637 168 RNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAegapPLCDMHPMRALFL------IPRNPAPRLKSKKW 241
                       250
                ....*....|....*....
gi 17542550 403 PKELMVLIDACCERNPNER 421
Cdd:cd06637 242 SKKFQSFIESCLVKNHSQR 260
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
182-368 5.23e-15

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: 75.42  E-value: 5.23e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 182 GCGAFGEVFKGQYKAVGSTnppieVAVKrILGNAKRKQiQEFCNEAQIMTVL-QHENIVAFYGFASLEEP------IMVV 254
Cdd:cd06608  15 GEGTYGKVYKARHKKTGQL-----AAIK-IMDIIEDEE-EEIKLEINILRKFsNHPNIATFYGAFIKKDPpggddqLWLV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGG---DL-RKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ----- 325
Cdd:cd06608  88 MEYCGGGsvtDLvKGLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSAQldstl 167
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17542550 326 ---GTEVTTKNlekapirWLAPE--SLKSGM---FNEKTDVWSYGVFLTEL 368
Cdd:cd06608 168 grrNTFIGTPY-------WMAPEviACDQQPdasYDARCDVWSLGITAIEL 211
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
178-364 5.28e-15

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: 75.39  E-value: 5.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 178 DKKLGCGAFGE-VFKGQYKAVgstnppiEVAVKRILgnakrkqiQEFCNEA-QIMTVLQ----HENIVAFYGFASLEEPI 251
Cdd:cd13982   6 PKVLGYGSEGTiVFRGTFDGR-------PVAVKRLL--------PEFFDFAdREVQLLResdeHPNVIRYFCTEKDRQFL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 MVVMEL--VTGGDL----RKYLQTTQNIPK-LQILWfamNVASGMRHLSSKGIIHRDLAARNCLVTQD-----LKAKISD 319
Cdd:cd13982  71 YIALELcaASLQDLvespRESKLFLRPGLEpVRLLR---QIASGLAHLHSLNIVHRDLKPQNILISTPnahgnVRAMISD 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17542550 320 FGLS--LQGTEVTTKNLEKAP--IRWLAPESLKSGMFNEKT---DVWSYG-VF 364
Cdd:cd13982 148 FGLCkkLDVGRSSFSRRSGVAgtSGWIAPEMLSGSTKRRQTravDIFSLGcVF 200
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
171-378 6.20e-15

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


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 75.47  E-value: 6.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 171 IHSTINLDKKLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEP 250
Cdd:cd14168   8 IKKIFEFKEVLGTGAFSEVVLAEERATGKL-----FAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNH 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMELVTGGDL-----RKYLQTTQNIPKLqilwfAMNVASGMRHLSSKGIIHRDLAARNCL-VTQDLKAK--ISDFGL 322
Cdd:cd14168  83 LYLVMQLVSGGELfdrivEKGFYTEKDASTL-----IRQVLDAVYYLHRMGIVHRDLKPENLLyFSQDEESKimISDFGL 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17542550 323 S-LQGTEVTTKNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMarCEHDPLY 378
Cdd:cd14168 158 SkMEGKGDVMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAYILL--CGYPPFY 211
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
179-378 6.40e-15

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: 75.53  E-value: 6.40e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRIlgNAKRKQIQEFC-NEAQIMTVLQHENIVAFYGFASLEEPIMVVMEL 257
Cdd:cd06656  25 EKIGQGASGTVYTAIDIATGQ-----EVAIKQM--NLQQQPKKELIiNEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTqNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGT-EVTTKNLEK 336
Cdd:cd06656  98 LAGGSLTDVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITpEQSKRSTMV 176
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 17542550 337 APIRWLAPESLKSGMFNEKTDVWSYGVFLTELMarcEHDPLY 378
Cdd:cd06656 177 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMV---EGEPPY 215
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
181-370 6.50e-15

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 75.00  E-value: 6.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKavgSTNPPIEVAVKRILGNAKRKQIQefcNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd14192  12 LGGGRFGQVHKCTEL---STGLTLAAKIIKVKGAKEREEVK---NEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDL-RKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARN--CLVTQDLKAKISDFGLSLQGTEVTTKNLEKA 337
Cdd:cd14192  86 GELfDRITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENilCVNSTGNQIKIIDFGLARRYKPREKLKVNFG 165
                       170       180       190
                ....*....|....*....|....*....|...
gi 17542550 338 PIRWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd14192 166 TPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLS 198
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
180-379 6.56e-15

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: 75.44  E-value: 6.56e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQ-EFCNEAQIMTVLQ-HENIVAFYGFASLEEPIMVVMEL 257
Cdd:cd07832   7 RIGEGAHGIVFKAKDRETGET-----VALKKVALRKLEGGIPnQALREIKALQACQgHPYVVKLRDVFPHGTGFVLVFEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VtGGDLRKYLQTTQN-IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSlqgtEVTTKNLEK 336
Cdd:cd07832  82 M-LSSLSEVLRDEERpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLA----RLFSEEDPR 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17542550 337 AP-----IRWL-APESL-KSGMFNEKTDVWSYGVFLTELMARCehdPLYP 379
Cdd:cd07832 157 LYshqvaTRWYrAPELLyGSRKYDEGVDLWAVGCIFAELLNGS---PLFP 203
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
180-405 6.83e-15

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: 75.86  E-value: 6.83e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGstnppIEVAVKRI---LGNAKRKQIqefCNEAQIMTVLQHENIVAFYGFASLEEPIMVVME 256
Cdd:cd06650  12 ELGAGNGGVVFKVSHKPSG-----LVMARKLIhleIKPAIRNQI---IRELQVLHECNSPYIVGFYGAFYSDGEISICME 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSK-GIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEvTTKNLE 335
Cdd:cd06650  84 HMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLID-SMANSF 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17542550 336 KAPIRWLAPESLKSGMFNEKTDVWSYGVFLTEL-MARcehdplYPKSLKDAKAwilTEERPHKMENGDPKE 405
Cdd:cd06650 163 VGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMaVGR------YPIPPPDAKE---LELMFGCQVEGDAAE 224
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
179-371 6.98e-15

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: 75.23  E-value: 6.98e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQEFC-NEAQIMTVLQHENIVAFYGFASLEEPIMVVMEL 257
Cdd:cd07860   6 EKIGEGTYGVVYKARNKLTGEV-----VALKKIRLDTETEGVPSTAiREISLLKELNHPNIVKLLDVIHTENKLYLVFEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGgDLRKYLQTTQ--NIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ-GTEVTTKNL 334
Cdd:cd07860  81 LHQ-DLKKFMDASAltGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAfGVPVRTYTH 159
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 17542550 335 EKAPIRWLAPES-LKSGMFNEKTDVWSYGVFLTELMAR 371
Cdd:cd07860 160 EVVTLWYRAPEIlLGCKYYSTAVDIWSLGCIFAEMVTR 197
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
181-379 7.13e-15

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: 75.00  E-value: 7.13e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKR--------------KQIQEFcneaqimtvlQHENIV----AFY 242
Cdd:cd07838   7 IGEGAYGTVYKARDLQDGRF-----VALKKVRVPLSEegiplstireiallKQLESF----------EHPNVVrlldVCH 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 243 GFASLEE-PIMVVMELVTGgDLRKYLQ--TTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISD 319
Cdd:cd07838  72 GPRTDRElKLTLVFEHVDQ-DLATYLDkcPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLAD 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17542550 320 FGLSlqgtEVTTKNLEKAPI---RWL-APESLKSGMFNEKTDVWSYGVFLTELMARcehDPLYP 379
Cdd:cd07838 151 FGLA----RIYSFEMALTSVvvtLWYrAPEVLLQSSYATPVDMWSVGCIFAELFNR---RPLFR 207
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
179-369 7.97e-15

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: 75.39  E-value: 7.97e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILgnAKRKQIQEFCNEAQIMTVLQHENIVAF-YGFASLEEpIMVVMEL 257
Cdd:cd05603   1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTIL--KKKEQNHIMAERNVLLKNLKHPFLVGLhYSFQTSEK-LYFVLDY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEV--TTKNLE 335
Cdd:cd05603  78 VNGGELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPeeTTSTFC 157
                       170       180       190
                ....*....|....*....|....*....|....
gi 17542550 336 KAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd05603 158 GTP-EYLAPEVLRKEPYDRTVDWWCLGAVLYEML 190
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
179-370 8.24e-15

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: 75.13  E-value: 8.24e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKrILGN---AKRKQIQEFCNEAQIMTVLQHENIV----AFYGFASLeepi 251
Cdd:cd14209   7 KTLGTGSFGRVMLVRHKETGNY-----YAMK-ILDKqkvVKLKQVEHTLNEKRILQAINFPFLVkleySFKDNSNL---- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 MVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSlQGTEVTT 331
Cdd:cd14209  77 YMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFA-KRVKGRT 155
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 17542550 332 KNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd14209 156 WTLCGTP-EYLAPEIILSKGYNKAVDWWALGVLIYEMAA 193
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
177-369 9.51e-15

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: 74.23  E-value: 9.51e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGSTnppieVAVKrILGNAKRKQ---IQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMV 253
Cdd:cd14079   6 LGKTLGVGSFGKVKLAEHELTGHK-----VAVK-ILNRQKIKSldmEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--------LQ 325
Cdd:cd14079  80 VMEYVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSnimrdgefLK 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17542550 326 gTEVTTKNlekapirWLAPE----SLKSGmfnEKTDVWSYGVFLTELM 369
Cdd:cd14079 160 -TSCGSPN-------YAAPEvisgKLYAG---PEVDVWSCGVILYALL 196
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
173-370 1.10e-14

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: 74.19  E-value: 1.10e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 173 STINLDKK--LGCGAFGEVFKGQYKAVGstnppIEVAVKRI-LGNAKRKQIqeFCNEAQIMTVLQHENIVAFYGFASLEE 249
Cdd:cd14190   2 STFSIHSKevLGGGKFGKVHTCTEKRTG-----LKLAAKVInKQNSKDKEM--VLLEIQVMNQLNHRNLIQLYEAIETPN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 250 PIMVVMELVTGGDL-RKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARN--CLVTQDLKAKISDFGLSLQG 326
Cdd:cd14190  75 EIVLFMEYVEGGELfERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENilCVNRTGHQVKIIDFGLARRY 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 17542550 327 TEVTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd14190 155 NPREKLKVNFGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLS 198
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
181-421 1.24e-14

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: 74.27  E-value: 1.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGstnppiEVAVKRILgNAKRKQIQEFCNEAQIMTVL-QHENIVAFYGFASLEEP------IMV 253
Cdd:cd06636  24 VGNGTYGQVYKGRHVKTG------QLAAIKVM-DVTEDEEEEIKLEINMLKKYsHHRNIATYYGAFIKKSPpghddqLWL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQN--IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ-GTEVT 330
Cdd:cd06636  97 VMEFCGAGSVTDLVKNTKGnaLKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQlDRTVG 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 331 TKNLEKAPIRWLAPESLK-----SGMFNEKTDVWSYGVFLTElMAR-----CEHDPLypKSLkdakaWILTEERPHKMEN 400
Cdd:cd06636 177 RRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIE-MAEgapplCDMHPM--RAL-----FLIPRNPPPKLKS 248
                       250       260
                ....*....|....*....|..
gi 17542550 401 GD-PKELMVLIDACCERNPNER 421
Cdd:cd06636 249 KKwSKKFIDFIEGCLVKNYLSR 270
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
181-370 1.33e-14

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: 74.23  E-value: 1.33e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEV-FKGQY-------------KAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFAS 246
Cdd:cd14067   1 LGQGGSGTViYRARYqgqpvavkrfhikKCKKRTDGSADTMLKHLRAADAMKNFSEFRQEASMLHSLQHPCIVYLIGISI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 247 leEPIMVVMELVTGGDLRKYLQTTQN----IPKLQILWF--AMNVASGMRHLSSKGIIHRDLAARNCLV-----TQDLKA 315
Cdd:cd14067  81 --HPLCFALELAPLGSLNTVLEENHKgssfMPLGHMLTFkiAYQIAAGLAYLHKKNIIFCDLKSDNILVwsldvQEHINI 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17542550 316 KISDFGLSLQGTEVTTKNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd14067 159 KLSDYGISRQSFHEGALGVEGTP-GYQAPEIRPRIVYDEKVDMFSYGMVLYELLS 212
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
181-368 1.44e-14

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: 74.26  E-value: 1.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGStnppieVAVKRILgNAKRKQIQEFCNEAQIMTVL-QHENIVAFYG-FASLEE----PIMVV 254
Cdd:cd06639  30 IGKGTYGKVYKVTNKKDGS------LAAVKIL-DPISDVDEEIEAEYNILRSLpNHPNVVKFYGmFYKADQyvggQLWLV 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGD----LRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVT 330
Cdd:cd06639 103 LELCNGGSvtelVKGLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSAR 182
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 17542550 331 -TKNLEKAPIRWLAPESLKSGM-----FNEKTDVWSYGVFLTEL 368
Cdd:cd06639 183 lRRNTSVGTPFWMAPEVIACEQqydysYDARCDVWSLGITAIEL 226
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
181-321 1.77e-14

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: 70.55  E-value: 1.77e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAvgstnPPIEVAVK--RILGNAKRKQIQefcNEAQIMT-VLQHE-NIVAFYGFASLEEPIMVVME 256
Cdd:cd13968   1 MGEGASAKVFWAEGEC-----TTIGVAVKigDDVNNEEGEDLE---SEMDILRrLKGLElNIPKVLVTEDVDGPNILLME 72
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17542550 257 LVTGGDLRKYLQTTQnIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFG 321
Cdd:cd13968  73 LVKGGTLIAYTQEEE-LDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
179-431 1.82e-14

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: 74.05  E-value: 1.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVgstnppiEVAVKRILGNAKRKQIQEfcNEAQIMTVLQHENIVAFY-----GFASLEEpIMV 253
Cdd:cd14144   1 RSVGKGRYGEVWKGKWRGE-------KVAVKIFFTTEEASWFRE--TEIYQTVLMRHENILGFIaadikGTGSWTQ-LYL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQnIPKLQILWFAMNVASGMRHLSSK--------GIIHRDLAARNCLVTQDLKAKISDFGLSL- 324
Cdd:cd14144  71 ITDYHENGSLYDFLRGNT-LDTQSMLKLAYSAACGLAHLHTEifgtqgkpAIAHRDIKSKNILVKKNGTCCIADLGLAVk 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 325 -----------QGTEVTTKnlekapiRWLAPESLKSGM----FNE--KTDVWSYGVFLTELMARC--------------- 372
Cdd:cd14144 150 fisetnevdlpPNTRVGTK-------RYMAPEVLDESLnrnhFDAykMADMYSFGLVLWEIARRCisggiveeyqlpyyd 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17542550 373 --EHDPlypkSLKDAKAWILTEER----PHKMENGDPKELMV-LIDACCERNPNERLNFNTVKRQI 431
Cdd:cd14144 223 avPSDP----SYEDMRRVVCVERRrpsiPNRWSSDEVLRTMSkLMSECWAHNPAARLTALRVKKTL 284
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
179-373 2.04e-14

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: 73.95  E-value: 2.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTNPPIeVAVKRILgnakRKQIQEFCNEAQIMT--VLQHENIVAFYGF----ASLEEPIM 252
Cdd:cd14055   1 KLVGKGRFAEVWKAKLKQNASGQYET-VAVKIFP----YEEYASWKNEKDIFTdaSLKHENILQFLTAeergVGLDRQYW 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYLqTTQNIPKLQILWFAMNVASGMRHLSSK---------GIIHRDLAARNCLVTQDLKAKISDFGLS 323
Cdd:cd14055  76 LITAYHENGSLQDYL-TRHILSWEDLCKMAGSLARGLAHLHSDrtpcgrpkiPIAHRDLKSSNILVKNDGTCVLADFGLA 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17542550 324 LQ-GTEVTTKNLEKA----PIRWLAPESLKSGMFNE------KTDVWSYGVFLTELMARCE 373
Cdd:cd14055 155 LRlDPSLSVDELANSgqvgTARYMAPEALESRVNLEdlesfkQIDVYSMALVLWEMASRCE 215
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
180-421 2.09e-14

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: 73.73  E-value: 2.09e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGSTnppieVAVKRI---LGNAKRKQIqefCNEAQIMTVLQHENIVAFYGFASLEEPIMVVME 256
Cdd:cd06622   8 ELGKGNYGSVYKVLHRPTGVT-----MAMKEIrleLDESKFNQI---IMELDILHKAVSPYIVDFYGAFFIEGAVYMCME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYL---QTTQNIPKLQILWFAMNVASGMRHLSSK-GIIHRDLAARNCLVTQDLKAKISDFGLSLQgtevTTK 332
Cdd:cd06622  80 YMDAGSLDKLYaggVATEGIPEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQVKLCDFGVSGN----LVA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 333 NLEKAPI---RWLAPESLKSGMFNE------KTDVWSYGVFLTELMARCEhdPLYPKSLKD--AKAWILTEERPHKMENG 401
Cdd:cd06622 156 SLAKTNIgcqSYMAPERIKSGGPNQnptytvQSDVWSLGLSILEMALGRY--PYPPETYANifAQLSAIVDGDPPTLPSG 233
                       250       260
                ....*....|....*....|
gi 17542550 402 DPKELMVLIDACCERNPNER 421
Cdd:cd06622 234 YSDDAQDFVAKCLNKIPNRR 253
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
181-372 2.28e-14

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: 73.63  E-value: 2.28e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVgstnppiEVAVKRILGNAKRKQIQEfcneAQI-MTV-LQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd14143   3 IGKGRFGEVWRGRWRGE-------DVAVKIFSSREERSWFRE----AEIyQTVmLRHENILGFIAADNKDNGTWTQLWLV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 T----GGDLRKYLQTTQnIPKLQILWFAMNVASGMRHL--------SSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQG 326
Cdd:cd14143  72 SdyheHGSLFDYLNRYT-VTVEGMIKLALSIASGLAHLhmeivgtqGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRH 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17542550 327 TEVTTkNLEKAP------IRWLAPESLKSGM----FN--EKTDVWSYGVFLTELMARC 372
Cdd:cd14143 151 DSATD-TIDIAPnhrvgtKRYMAPEVLDDTInmkhFEsfKRADIYALGLVFWEIARRC 207
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
175-421 2.92e-14

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: 73.55  E-value: 2.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQykavgSTNPPIEVA----VKRILGNAKRKQIQEfcnEAQIMTVLQHENIVAFYGfaSLEEP 250
Cdd:cd14030  27 LKFDIEIGRGSFKTVYKGL-----DTETTVEVAwcelQDRKLSKSERQRFKE---EAGMLKGLQHPNIVRFYD--SWEST 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 ------IMVVMELVTGGDLRKYLQTTQnIPKLQILW-FAMNVASGMRHLSSKG--IIHRDLAARNCLVTQDL-KAKISDF 320
Cdd:cd14030  97 vkgkkcIVLVTELMTSGTLKTYLKRFK-VMKIKVLRsWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDL 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 321 GLSLQGTEVTTKNLEKAPiRWLAPESLKSgMFNEKTDVWSYGVFLTElMARCEHDplYPKSLKDAKAW--ILTEERPHKM 398
Cdd:cd14030 176 GLATLKRASFAKSVIGTP-EFMAPEMYEE-KYDESVDVYAFGMCMLE-MATSEYP--YSECQNAAQIYrrVTSGVKPASF 250
                       250       260
                ....*....|....*....|...
gi 17542550 399 ENGDPKELMVLIDACCERNPNER 421
Cdd:cd14030 251 DKVAIPEVKEIIEGCIRQNKDER 273
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
179-422 3.29e-14

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: 73.82  E-value: 3.29e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKrilgnAKRKQIQEFCNEAQIMTV------LQHEN--IVAFYGFASLEEP 250
Cdd:cd05620   1 KVLGKGSFGKVLLAELKGKGEY-----FAVK-----ALKKDVVLIDDDVECTMVekrvlaLAWENpfLTHLYCTFQTKEH 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGT--E 328
Cdd:cd05620  71 LFFVMEFLNGGDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVfgD 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 329 VTTKNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMARC------EHDPLYPKSLKDA---KAWILTEERPhkme 399
Cdd:cd05620 151 NRASTFCGTP-DYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQspfhgdDEDELFESIRVDTphyPRWITKESKD---- 225
                       250       260
                ....*....|....*....|...
gi 17542550 400 ngdpkelmvLIDACCERNPNERL 422
Cdd:cd05620 226 ---------ILEKLFERDPTRRL 239
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
181-429 3.75e-14

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: 72.29  E-value: 3.75e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVfkgqyKAVGSTNPPIEVAVKrILGNAKRKQI----QEFCNEAQIMTVLQHENIVAFYGFASLEEP--IMVV 254
Cdd:cd14119   1 LGEGSYGKV-----KEVLDTETLCRRAVK-ILKKRKLRRIpngeANVKREIQILRRLNHRNVIKLVDVLYNEEKqkLYMV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTTQN-IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS------LQGT 327
Cdd:cd14119  75 MEYCVGGLQEMLDSAPDKrLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAealdlfAEDD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 328 EVTTKNLEKApirWLAPEsLKSG--MFNE-KTDVWSYGVFLTELMArcehdPLYPksLKDAKAWILTE---ERPHKMENG 401
Cdd:cd14119 155 TCTTSQGSPA---FQPPE-IANGqdSFSGfKVDIWSAGVTLYNMTT-----GKYP--FEGDNIYKLFEnigKGEYTIPDD 223
                       250       260
                ....*....|....*....|....*...
gi 17542550 402 DPKELMVLIDACCERNPNERLNFNTVKR 429
Cdd:cd14119 224 VDPDLQDLLRGMLEKDPEKRFTIEQIRQ 251
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
181-370 3.85e-14

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


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 72.57  E-value: 3.85e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKavgSTNPPIevAVKRILGNAKRKQIQEfcNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd14087   9 IGRGSFSRVVRVEHR---VTRQPY--AIKMIETKCRGREVCE--SELNVLRRVRHTNIIQLIEVFETKERVYMVMELATG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQ---DLKAKISDFGLSLQ---GTEVTTKNL 334
Cdd:cd14087  82 GELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHpgpDSKIMITDFGLASTrkkGPNCLMKTT 161
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17542550 335 EKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd14087 162 CGTP-EYIAPEILLRKPYTQSVDMWAVGVIAYILLS 196
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
181-444 4.31e-14

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: 72.73  E-value: 4.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAvgstnppiEVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVT 259
Cdd:cd14153   8 IGKGRFGQVYHGRWHG--------EVAIRLIdIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 260 GGDLRKYLQTTQNIPKL-QILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDlKAKISDFGL-SLQGTEVTTKNLEK- 336
Cdd:cd14153  80 GRTLYSVVRDAKVVLDVnKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNG-KVVITDFGLfTISGVLQAGRREDKl 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 337 ----------AP--IRWLAPESLKSGM-FNEKTDVWSYGVFLTELMARcehdpLYPKSLKDAKAWIL---TEERPHKMEN 400
Cdd:cd14153 159 riqsgwlchlAPeiIRQLSPETEEDKLpFSKHSDVFAFGTIWYELHAR-----EWPFKTQPAEAIIWqvgSGMKPNLSQI 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 17542550 401 GDPKELMVLIDACCERNPNERLNFNTVkrqitdiyMEALNKGPQ 444
Cdd:cd14153 234 GMGKEISDILLFCWAYEQEERPTFSKL--------MEMLEKLPK 269
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
180-379 5.62e-14

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


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 72.47  E-value: 5.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGSTnppieVAVKRI-LGNAKR----KQIQEFCneaqIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:cd07839   7 KIGEGTYGTVFKAKNRETHEI-----VALKRVrLDDDDEgvpsSALREIC----LLKELKHKNIVRLYDVLHSDKKLTLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGgDLRKYLQTTQNIPKLQILW-FAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ-GTEVTTK 332
Cdd:cd07839  78 FEYCDQ-DLKKYFDSCNGDIDPEIVKsFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAfGIPVRCY 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17542550 333 NLEKAPIRWLAPESL-KSGMFNEKTDVWSYGVFLTELMARCEhdPLYP 379
Cdd:cd07839 157 SAEVVTLWYRPPDVLfGAKLYSTSIDMWSAGCIFAELANAGR--PLFP 202
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
179-382 5.74e-14

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: 73.50  E-value: 5.74e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGstnppiEVAVKRILGN---AKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVM 255
Cdd:cd05621  58 KVIGRGAFGEVQLVRHKASQ------KVYAMKLLSKfemIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVM 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRKyLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFG--LSLQGTEVTTKN 333
Cdd:cd05621 132 EYMPGGDLVN-LMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGtcMKMDETGMVHCD 210
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17542550 334 LEKAPIRWLAPESLKS----GMFNEKTDVWSYGVFLTELMArcEHDPLYPKSL 382
Cdd:cd05621 211 TAVGTPDYISPEVLKSqggdGYYGRECDWWSVGVFLFEMLV--GDTPFYADSL 261
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
179-369 5.96e-14

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: 72.20  E-value: 5.96e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKavgstNPPIEVAVKRILGNAKRKQIQE--FCNEAQIMTVLQHENIVAFYGFASLEEPIMVVME 256
Cdd:cd14117  12 RPLGKGKFGNVYLAREK-----QSKFIVALKVLFKSQIEKEGVEhqLRREIEIQSHLRHPNILRLYNYFHDRKRIYLILE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLeK 336
Cdd:cd14117  87 YAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVHAPSLRRRTM-C 165
                       170       180       190
                ....*....|....*....|....*....|...
gi 17542550 337 APIRWLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd14117 166 GTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELL 198
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
179-371 6.38e-14

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: 72.04  E-value: 6.38e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRILGNAKR----KQIQEFCNEAQIMTVLQHENIVAFYGFAS--LEEPIM 252
Cdd:cd06651  13 KLLGQGAFGRVYLCYDVDTGR-----ELAAKQVQFDPESpetsKEVSALECEIQLLKNLQHERIVQYYGCLRdrAEKTLT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS-------LQ 325
Cdd:cd06651  88 IFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkrlqticMS 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17542550 326 GTEVttKNLEKAPIrWLAPESLKSGMFNEKTDVWSYGVFLTELMAR 371
Cdd:cd06651 168 GTGI--RSVTGTPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLTE 210
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
181-370 6.49e-14

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: 72.24  E-value: 6.49e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTNPPIEVAVKRIlgnaKRKQIQEFC-NEAQIMTVLQHENIVAF-YGFASlEEPIMVVMELV 258
Cdd:cd05607  10 LGKGGFGEVCAVQVKNTGQMYACKKLDKKRL----KKKSGEKMAlLEKEILEKVNSPFIVSLaYAFET-KTHLCLVMSLM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQT--TQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLEK 336
Cdd:cd05607  85 NGGDLKYHIYNvgERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKEGKPITQRA 164
                       170       180       190
                ....*....|....*....|....*....|....
gi 17542550 337 APIRWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd05607 165 GTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVA 198
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
171-381 8.15e-14

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: 72.34  E-value: 8.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 171 IHSTINLDKkLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEP 250
Cdd:cd07873   1 LETYIKLDK-LGEGTYATVYKGRSKLTDNL-----VALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMELVTGgDLRKYLQTTQNIPKLQ-ILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSlQGTEV 329
Cdd:cd07873  75 LTLVFEYLDK-DLKQYLDDCGNSINMHnVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLA-RAKSI 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17542550 330 TTKNLEKAPIR-WLAPES--LKSGMFNEKTDVWSYGVFLTELMArceHDPLYPKS 381
Cdd:cd07873 153 PTKTYSNEVVTlWYRPPDilLGSTDYSTQIDMWGVGCIFYEMST---GRPLFPGS 204
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
178-365 9.06e-14

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: 71.29  E-value: 9.06e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 178 DKKLGCGAFGEVFKGQYKAVGStnppiEVAVKRIlgNAKR---KQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:cd14082   8 DEVLGSGQFGIVYGGKHRKTGR-----DVAIKVI--DKLRfptKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTTQN-IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDL---KAKISDFGLS-LQGTEV 329
Cdd:cd14082  81 MEKLHGDMLEMILSSEKGrLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFArIIGEKS 160
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17542550 330 TTKNLEKAPIrWLAPESLKSGMFNEKTDVWSYGVFL 365
Cdd:cd14082 161 FRRSVVGTPA-YLAPEVLRNKGYNRSLDMWSVGVII 195
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
238-370 1.02e-13

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: 72.75  E-value: 1.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 238 IVAFYGFASLEEPIMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKI 317
Cdd:cd05617  78 LVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKL 157
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17542550 318 SDFGLSLQGTEV--TTKNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd05617 158 TDYGMCKEGLGPgdTTSTFCGTP-NYIAPEILRGEEYGFSVDWWALGVLMFEMMA 211
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
208-432 1.04e-13

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; 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 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. The Tyk2 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: 270661 [Multi-domain]  Cd Length: 273  Bit Score: 71.48  E-value: 1.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 208 VKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTGGDLRKYLQTTQ-NIPKLQILWFAMNVA 286
Cdd:cd05076  47 VLKVLDPSHHDIALAFFETASLMSQVSHTHLVFVHGVCVRGSENIMVEEFVEHGPLDVWLRKEKgHVPMAWKFVVARQLA 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 287 SGMRHLSSKGIIHRDLAARNCLVTQDLKA-------KISDFGLSLqGTEVTTKNLEKAPirWLAPESLKSGM-FNEKTDV 358
Cdd:cd05076 127 SALSYLENKNLVHGNVCAKNILLARLGLEegtspfiKLSDPGVGL-GVLSREERVERIP--WIAPECVPGGNsLSTAADK 203
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17542550 359 WSYGVFLTELMARCEHdPLYPKSLKDAKAWIlteERPHKMENGDPKELMVLIDACCERNPNERLNFNTVKRQIT 432
Cdd:cd05076 204 WGFGATLLEICFNGEA-PLQSRTPSEKERFY---QRQHRLPEPSCPELATLISQCLTYEPTQRPSFRTILRDLT 273
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
180-372 1.07e-13

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: 71.39  E-value: 1.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGstnppIEVAVKRIlgnakrkQIQEFCNEaQIMT--VLQHENIVAFYGfASLEEP-IMVVME 256
Cdd:cd13991  13 RIGRGSFGEVHRMEDKQTG-----FQCAVKKV-------RLEVFRAE-ELMAcaGLTSPRVVPLYG-AVREGPwVNIFMD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQD-LKAKISDFGLSL------QGTEV 329
Cdd:cd13991  79 LKEGGSLGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDgSDAFLCDFGHAEcldpdgLGKSL 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 17542550 330 TTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARC 372
Cdd:cd13991 159 FTGDYIPGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGC 201
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
179-421 1.28e-13

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: 70.88  E-value: 1.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVK-----RILGNA--KRKQIQEFCNEAQIMTVLQ---HENIVAFYGFASLE 248
Cdd:cd14004   6 KEMGEGAYGQVNLAIYKSKGK-----EVVIKfifkeRILVDTwvRDRKLGTVPLEIHILDTLNkrsHPNIVKLLDFFEDD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 249 EPIMVVMELVTGG-DLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGlslqgt 327
Cdd:cd14004  81 EFYYLVMEKHGSGmDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFG------ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 328 evTTKNLEKAP-------IRWLAPESLKSGMFNEK-TDVWSYGVFLTELMARceHDPLYpkslkDAKAWILTEERPHKME 399
Cdd:cd14004 155 --SAAYIKSGPfdtfvgtIDYAAPEVLRGNPYGGKeQDIWALGVLLYTLVFK--ENPFY-----NIEEILEADLRIPYAV 225
                       250       260
                ....*....|....*....|..
gi 17542550 400 NgdpKELMVLIDACCERNPNER 421
Cdd:cd14004 226 S---EDLIDLISRMLNRDVGDR 244
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
179-422 1.28e-13

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


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 72.37  E-value: 1.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTNPpIEVAVKRILgnAKRKQIQEFCNEAQIMTVLQHENIVAF-YGFASlEEPIMVVMEL 257
Cdd:cd05594  31 KLLGKGTFGKVILVKEKATGRYYA-MKILKKEVI--VAKDEVAHTLTENRVLQNSRHPFLTALkYSFQT-HDRLCFVMEY 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHL-SSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTE--VTTKNL 334
Cdd:cd05594 107 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLhSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKdgATMKTF 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 335 EKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMarCEHDPLYPKSLKDAKAWILTEE--RPHKMEngdpKELMVLIDA 412
Cdd:cd05594 187 CGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMM--CGRLPFYNQDHEKLFELILMEEirFPRTLS----PEAKSLLSG 259
                       250
                ....*....|
gi 17542550 413 CCERNPNERL 422
Cdd:cd05594 260 LLKKDPKQRL 269
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
176-363 1.41e-13

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: 70.80  E-value: 1.41e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 176 NLDKKLGCGAFGEVFKGQYKAVGstnppiEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIV----AFYGFASleepI 251
Cdd:cd14191   5 DIEERLGSGKFGQVFRLVEKKTK------KVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVqcvdAFEEKAN----I 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 MVVMELVTGGDL-RKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARN--CLVTQDLKAKISDFGLSLQGTE 328
Cdd:cd14191  75 VMVLEMVSGGELfERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENimCVNKTGTKIKLIDFGLARRLEN 154
                       170       180       190
                ....*....|....*....|....*....|....*
gi 17542550 329 VTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGV 363
Cdd:cd14191 155 AGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGV 189
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
179-379 1.45e-13

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: 72.02  E-value: 1.45e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKgqykAVGS-TNPpiEVAVKRIlGNA--KRKQIQEFCNEAQIMTVLQHENIVAFYGFASLE-----EP 250
Cdd:cd07858  11 KPIGRGAYGIVCS----AKNSeTNE--KVAIKKI-ANAfdNRIDAKRTLREIKLLRHLDHENVIAIKDIMPPPhreafND 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMELVTGgDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVT 330
Cdd:cd07858  84 VYIVYELMDT-DLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARTTSEKG 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17542550 331 TKNLEKAPIRWL-APES-LKSGMFNEKTDVWSYGVFLTELMARcehDPLYP 379
Cdd:cd07858 163 DFMTEYVVTRWYrAPELlLNCSEYTTAIDVWSVGCIFAELLGR---KPLFP 210
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
181-421 1.48e-13

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: 71.38  E-value: 1.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGstnppIEVAVKRIL-GNAKRKQIQEFCNEAQIMTVLQHENIVAFYgfASLEEPI-------M 252
Cdd:cd14049  14 LGKGGYGKVYKVRNKLDG-----QYYAIKKILiKKVTKRDCMKVLREVKVLAGLQHPNIVGYH--TAWMEHVqlmlyiqM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELvtggDLRKYLQTTQNIPKLQ--------------ILWFAMNVASGMRHLSSKGIIHRDLAARNCLVT-QDLKAKI 317
Cdd:cd14049  87 QLCEL----SLWDWIVERNKRPCEEefksapytpvdvdvTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHVRI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 318 SDFGLS-----LQGTEVTTKNLEKAPIR--------WLAPESLKSGMFNEKTDVWSYGVFLTELMARCEHDPLYPKSLKD 384
Cdd:cd14049 163 GDFGLAcpdilQDGNDSTTMSRLNGLTHtsgvgtclYAAPEQLEGSHYDFKSDMYSIGVILLELFQPFGTEMERAEVLTQ 242
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 17542550 385 AKawilTEERPHKMENGDPkELMVLIDACCERNPNER 421
Cdd:cd14049 243 LR----NGQIPKSLCKRWP-VQAKYIKLLTSTEPSER 274
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
181-365 1.78e-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: 70.43  E-value: 1.78e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGStnppiEVAVKRIlgNAKRKQIQEFCNEAQIMTVLQ-HENIVAFYGFA-SLEEPIMVVMELV 258
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGT-----KMALKFV--PKPSTKLKDFLREYNISLELSvHPHIIKTYDVAfETEDYYVFAQEYA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLV-TQDL-KAKISDFGLSL-QGTEVTTKNLE 335
Cdd:cd13987  74 PYGDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfDKDCrRVKLCDFGLTRrVGSTVKRVSGT 153
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17542550 336 kapIRWLAPESLKSGMfNEK------TDVWSYGVFL 365
Cdd:cd13987 154 ---IPYTAPEVCEAKK-NEGfvvdpsIDVWAFGVLL 185
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
72-153 1.93e-13

Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides via 2 surface pockets. Specificity is provided via interaction with residues that are distinct from the phosphotyrosine. Only a single occurrence of a SH2 domain has been found in S. cerevisiae.


Pssm-ID: 214585 [Multi-domain]  Cd Length: 84  Bit Score: 65.71  E-value: 1.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550     72 YHGVLFGSEAEKLLTW--DRAYLVRRAITKPNKFlCISVNWKKKIFHYQLDFNEDGwcckklyeKFPTMPNRRFLHIRQL 149
Cdd:smart00252   4 YHGFISREEAEKLLKNegDGDFLVRDSESSPGDY-VLSVRVKGKVKHYRIRRNEDG--------KFYLEGGRKFPSLVEL 74

                   ....
gi 17542550    150 LEAW 153
Cdd:smart00252  75 VEHY 78
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
181-426 2.01e-13

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: 70.50  E-value: 2.01e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFkgQYKAVGSTNPPIEVAVKrILGNA----KRKQIQEFCNEAQIM-TVLQHENIVA-FYGFASlEEPIMVV 254
Cdd:cd05583   2 LGTGAYGKVF--LVRKVGGHDAGKLYAMK-VLKKAtivqKAKTAEHTMTERQVLeAVRQSPFLVTlHYAFQT-DAKLHLI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSlqgTEVTTKNL 334
Cdd:cd05583  78 LDYVNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLS---KEFLPGEN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 335 EKA-----PIRWLAPESLKSGM--FNEKTDVWSYGVFLTELMARCEhdPLYPKSLKDAKA----WILTEERPhkMENGDP 403
Cdd:cd05583 155 DRAysfcgTIEYMAPEVVRGGSdgHDKAVDWWSLGVLTYELLTGAS--PFTVDGERNSQSeiskRILKSHPP--IPKTFS 230
                       250       260
                ....*....|....*....|...
gi 17542550 404 KELMVLIDACCERNPNERLNFNT 426
Cdd:cd05583 231 AEAKDFILKLLEKDPKKRLGAGP 253
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
177-370 2.02e-13

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: 70.42  E-value: 2.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVME 256
Cdd:cd14195   9 MGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRRGVSREEIEREVNILREIQHPNIITLHDIFENKTDVVLILE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLV----TQDLKAKISDFGLSLQ---GTEV 329
Cdd:cd14195  89 LVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLldknVPNPRIKLIDFGIAHKieaGNEF 168
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 17542550 330 ttKNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd14195 169 --KNIFGTP-EFVAPEIVNYEPLGLEADMWSIGVITYILLS 206
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
180-365 2.15e-13

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: 70.74  E-value: 2.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGStnppiEVAVKrILGNAKRkQIQEfcnEAQIMTVL-QHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd14091   7 EIGKGSYSVCKRCIHKATGK-----EYAVK-IIDKSKR-DPSE---EIEILLRYgQHPNIITLRDVYDDGNSVYLVTELL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDL------RKYL--QTTQNIPKlqilwfamNVASGMRHLSSKGIIHRDLAARNCLVTQDLKA----KISDFGLSLQ- 325
Cdd:cd14091  77 RGGELldrilrQKFFseREASAVMK--------TLTKTVEYLHSQGVVHRDLKPSNILYADESGDpeslRICDFGFAKQl 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 17542550 326 ----GTEVT---TKNlekapirWLAPESLKSGMFNEKTDVWSYGVFL 365
Cdd:cd14091 149 raenGLLMTpcyTAN-------FVAPEVLKKQGYDAACDIWSLGVLL 188
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
225-369 2.66e-13

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: 69.98  E-value: 2.66e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 225 NEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAA 304
Cdd:cd14185  47 SEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKP 126
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17542550 305 RNCLVTQDLKA----KISDFGLSLQGTEvttknlekaPI-------RWLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd14185 127 ENLLVQHNPDKsttlKLADFGLAKYVTG---------PIftvcgtpTYVAPEILSEKGYGLEVDMWAAGVILYILL 193
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
179-421 2.78e-13

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: 70.54  E-value: 2.78e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGstnppIEVAVKRI---LGNAKRKQIqefCNEAQIMTVLQHENIVAFYG-FASLEEpIMVV 254
Cdd:cd06615   7 GELGAGNGGVVTKVLHRPSG-----LIMARKLIhleIKPAIRNQI---IRELKVLHECNSPYIVGFYGaFYSDGE-ISIC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSK-GIIHRDLAARNCLVTQDLKAKISDFGLSLQ------GT 327
Cdd:cd06615  78 MEHMDGGSLDQVLKKAGRIPENILGKISIAVLRGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQlidsmaNS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 328 EVTTKNlekapirWLAPESLKSGMFNEKTDVWSYGVFLTElMA----------RCEHDPLYPKSLKD-AKAWILTEERPH 396
Cdd:cd06615 158 FVGTRS-------YMSPERLQGTHYTVQSDIWSLGLSLVE-MAigrypipppdAKELEAMFGRPVSEgEAKESHRPVSGH 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 17542550 397 KMENGDP------------------------KELMVLIDACCERNPNER 421
Cdd:cd06615 230 PPDSPRPmaifelldyivnepppklpsgafsDEFQDFVDKCLKKNPKER 278
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
177-372 2.85e-13

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: 69.89  E-value: 2.85e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVfkgqyKAVGSTNPPIEVAVKRIlgnAKRKQIQEFCN-----EAQIMTVLQHENIVAFYGFASL-EEP 250
Cdd:cd14164   4 LGTTIGEGSFSKV-----KLATSQKYCCKVAIKIV---DRRRASPDFVQkflprELSILRRVNHPNIVQMFECIEVaNGR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMElVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQD-LKAKISDFGLSLQG--- 326
Cdd:cd14164  76 LYIVME-AAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADdRKIKIADFGFARFVedy 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 17542550 327 TEVTTKNLEKAPirWLAPESLKSGMFN-EKTDVWSYGVFLTELMARC 372
Cdd:cd14164 155 PELSTTFCGSRA--YTPPEVILGTPYDpKKYDVWSLGVVLYVMVTGT 199
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
179-370 3.10e-13

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: 70.05  E-value: 3.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd14194  11 EELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSREDIEREVSILKEIQHPNVITLHEVYENKTDVILILELV 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLV----TQDLKAKISDFGLSLQ---GTEVtt 331
Cdd:cd14194  91 AGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLldrnVPKPRIKIIDFGLAHKidfGNEF-- 168
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 17542550 332 KNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd14194 169 KNIFGTP-EFVAPEIVNYEPLGLEADMWSIGVITYILLS 206
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
179-379 3.43e-13

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: 69.87  E-value: 3.43e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKRIlgNAKRKQIQEFCN--EAQ-IMTVLQHENIVAFYGFASLEEPIMVVM 255
Cdd:cd07830   5 KQLGDGTFGSVYLARNKETGEL-----VAIKKM--KKKFYSWEECMNlrEVKsLRKLNEHPNIVKLKEVFRENDELYFVF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGgDLRKyLQTTQNIPKLQ------ILWfamNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSlqgTEV 329
Cdd:cd07830  78 EYMEG-NLYQ-LMKDRKGKPFSesvirsIIY---QILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLA---REI 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17542550 330 ttknLEKAPI------RWL-APES-LKSGMFNEKTDVWSYGVFLTEL-MARcehdPLYP 379
Cdd:cd07830 150 ----RSRPPYtdyvstRWYrAPEIlLRSTSYSSPVDIWALGCIMAELyTLR----PLFP 200
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
179-370 3.65e-13

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: 70.60  E-value: 3.65e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKavGSTnppiEVAVKRILgnAKRKQIQE---FCN--EAQIMTV-LQHENIVAFYGFASLEEPIM 252
Cdd:cd05591   1 KVLGKGSFGKVMLAERK--GTD----EVYAIKVL--KKDVILQDddvDCTmtEKRILALaAKHPFLTALHSCFQTKDRLF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGT--EVT 330
Cdd:cd05591  73 FVMEYVNGGDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGIlnGKT 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 17542550 331 TKNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd05591 153 TTTFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA 191
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
179-369 3.83e-13

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: 70.58  E-value: 3.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKgqykAVGStNPPIEVAVKRILGNAKRKqIQEFCNEAQIMTVLQHENIVAFY------------GFAS 246
Cdd:cd07854  11 RPLGCGSNGLVFS----AVDS-DCDKRVAVKKIVLTDPQS-VKHALREIKIIRRLDHDNIVKVYevlgpsgsdlteDVGS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 247 LEE--PIMVVMELVTGgDLRKYLQTTQnIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLV-TQDLKAKISDFGL- 322
Cdd:cd07854  85 LTElnSVYIVQEYMET-DLANVLEQGP-LSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFInTEDLVLKIGDFGLa 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17542550 323 -------SLQG--TEVTTKNLEKAPIRWLAPESlksgmFNEKTDVWSYGVFLTELM 369
Cdd:cd07854 163 rivdphySHKGylSEGLVTKWYRSPRLLLSPNN-----YTKAIDMWAAGCIFAEML 213
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
181-370 4.10e-13

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: 70.24  E-value: 4.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVfkgqYKAVGSTNppiEVAVKRILGNAKRKQI---QEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMEL 257
Cdd:cd14159   1 IGEGGFGCV----YQAVMRNT---EYAVKRLKEDSELDWSvvkNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTQNIPKL---QILWFAMNVASGMR--HLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSL-------- 324
Cdd:cd14159  74 LPNGSLEDRLHCQVSCPCLswsQRLHVLLGTARAIQylHSDSPSLIHGDVKSSNILLDAALNPKLGDFGLARfsrrpkqp 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 17542550 325 -QGTEVTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd14159 154 gMSSTLARTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLT 200
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
181-427 4.18e-13

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: 69.91  E-value: 4.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVfkgqYKAVGSTNPPIeVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd06619   9 LGHGNGGTV----YKAYHLLTRRI-LAVKVIPLDITVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYlqttQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ------GTEVTTKnl 334
Cdd:cd06619  84 GSLDVY----RKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQlvnsiaKTYVGTN-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 335 ekapiRWLAPESLKSGMFNEKTDVWSYGVFLTEL-MARCEhdplYPKSLKDAKAWI-------LTEERPHKMENGDPKEL 406
Cdd:cd06619 158 -----AYMAPERISGEQYGIHSDVWSLGISFMELaLGRFP----YPQIQKNQGSLMplqllqcIVDEDPPVLPVGQFSEK 228
                       250       260
                ....*....|....*....|..
gi 17542550 407 MV-LIDACCERNPNERLNFNTV 427
Cdd:cd06619 229 FVhFITQCMRKQPKERPAPENL 250
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
171-381 5.26e-13

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: 70.02  E-value: 5.26e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 171 IHSTINLDKkLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEP 250
Cdd:cd07872   5 METYIKLEK-LGEGTYATVFKGRSKLTENL-----VALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMELVTGgDLRKYLQTTQNIPKLQ-ILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSlQGTEV 329
Cdd:cd07872  79 LTLVFEYLDK-DLKQYMDDCGNIMSMHnVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLA-RAKSV 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17542550 330 TTKNLEKAPIR-WLAPES--LKSGMFNEKTDVWSYGVFLTELMArceHDPLYPKS 381
Cdd:cd07872 157 PTKTYSNEVVTlWYRPPDvlLGSSEYSTQIDMWGVGCIFFEMAS---GRPLFPGS 208
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
177-422 5.28e-13

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


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 69.22  E-value: 5.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGStnppiEVAVKrILGNAKRKQIQEFcNEAQIMTVLQ------HENIVAFYGFASLEEP 250
Cdd:cd14133   3 VLEVLGKGTFGQVVKCYDLLTGE-----EVALK-IIKNNKDYLDQSL-DEIRLLELLNkkdkadKYHIVRLKDVFYFKNH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMELVtGGDLRKYLQTTQ----NIPKLQilWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQ--DLKAKISDFGLSL 324
Cdd:cd14133  76 LCIVFELL-SQNLYEFLKQNKfqylSLPRIR--KIAQQILEALVFLHSLGLIHCDLKPENILLASysRCQIKIIDFGSSC 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 325 QGTEVTTKNLEKAPIRwlAPESLKSGMFNEKTDVWSYGVFLTELMARcehDPLYP-KSLKDAKAWILT--EERPHKM-EN 400
Cdd:cd14133 153 FLTQRLYSYIQSRYYR--APEVILGLPYDEKIDMWSLGCILAELYTG---EPLFPgASEVDQLARIIGtiGIPPAHMlDQ 227
                       250       260
                ....*....|....*....|....
gi 17542550 401 G--DPKELMVLIDACCERNPNERL 422
Cdd:cd14133 228 GkaDDELFVDFLKKLLEIDPKERP 251
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
181-368 5.29e-13

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: 69.70  E-value: 5.29e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGStnppiEVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVT 259
Cdd:cd06616  14 IGRGAFGTVNKMLHKPSGT-----IMAVKRIrSTVDEKEQKRLLMDLDVVMRSSDCPYIVKFYGALFREGDCWICMELMD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 260 GgDLRK-----YLQTTQNIPKlQIL-WFAMNVASGMRHLSSK-GIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTK 332
Cdd:cd06616  89 I-SLDKfykyvYEVLDSVIPE-EILgKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGNIKLCDFGISGQLVDSIAK 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 17542550 333 NLEKAPIRWLAPESLKSGMFNE----KTDVWSYGVFLTEL 368
Cdd:cd06616 167 TRDAGCRPYMAPERIDPSASRDgydvRSDVWSLGITLYEV 206
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
184-434 5.39e-13

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: 69.46  E-value: 5.39e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 184 GAFGEVFKGQYKAVGStnppiEVAVKRILGNAKRKQiQEFCNEAQIMTVLQ-HENIVAFYGFASLEEP--------IMVV 254
Cdd:cd14036  11 GGFAFVYEAQDVGTGK-----EYALKRLLSNEEEKN-KAIIQEINFMKKLSgHPNIVQFCSAASIGKEesdqgqaeYLLL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGG--DLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKG--IIHRDLAARNCLVTQDLKAKISDFGlSLQGTEVT 330
Cdd:cd14036  85 TELCKGQlvDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFG-SATTEAHY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 331 TKNLEKAPIRWLAPESLK---SGMF--------------NEKTDVWSYGVFLTELMARcEHDplYPKSLK----DAKAWI 389
Cdd:cd14036 164 PDYSWSAQKRSLVEDEITrntTPMYrtpemidlysnypiGEKQDIWALGCILYLLCFR-KHP--FEDGAKlriiNAKYTI 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 17542550 390 LTEERPHKMENGdpkelmvLIDACCERNPNERLNFNTVKRQITDI 434
Cdd:cd14036 241 PPNDTQYTVFHD-------LIRSTLKVNPEERLSITEIVEQLQEL 278
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
176-363 5.61e-13

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


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 69.21  E-value: 5.61e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 176 NLDKKLGCGAFGEVFKGQYKAVGstnppIEVAVKRI---LGNAKRKQI--QEFCNEAQIMTVLQHENIVAFYGFASLEEP 250
Cdd:cd14196   8 DIGEELGSGQFAIVKKCREKSTG-----LEYAAKFIkkrQSRASRRGVsrEEIEREVSILRQVLHPNIITLHDVYENRTD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDL----KAKISDFGLSLQG 326
Cdd:cd14196  83 VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEI 162
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 17542550 327 TE-VTTKNLEKAPiRWLAPESLKSGMFNEKTDVWSYGV 363
Cdd:cd14196 163 EDgVEFKNIFGTP-EFVAPEIVNYEPLGLEADMWSIGV 199
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
180-379 5.62e-13

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: 69.24  E-value: 5.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGSTnppieVAVKRIL---------GNAKRkqiqefcnEAQIMTVLQHENIVAFYGFASLEEP 250
Cdd:cd07835   6 KIGEGTYGVVYKARDKLTGEI-----VALKKIRletedegvpSTAIR--------EISLLKELNHPNIVRLLDVVHSENK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMELVTGgDLRKYLQTT--QNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ-GT 327
Cdd:cd07835  73 LYLVFEFLDL-DLKKYMDSSplTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAfGV 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17542550 328 EVTTKNLEKAPIRWLAPES-LKSGMFNEKTDVWSYGVFLTELmarCEHDPLYP 379
Cdd:cd07835 152 PVRTYTHEVVTLWYRAPEIlLGSKHYSTPVDIWSVGCIFAEM---VTRRPLFP 201
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
180-386 6.01e-13

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: 70.08  E-value: 6.01e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGstnppIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVT 259
Cdd:cd06649  12 ELGAGNGGVVTKVQHKPSG-----LIMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 260 GGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSK-GIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEvTTKNLEKAP 338
Cdd:cd06649  87 GGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLID-SMANSFVGT 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17542550 339 IRWLAPESLKSGMFNEKTDVWSYGVFLTEL-MARcehdplYPKSLKDAK 386
Cdd:cd06649 166 RSYMSPERLQGTHYSVQSDIWSMGLSLVELaIGR------YPIPPPDAK 208
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
215-369 6.05e-13

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: 69.19  E-value: 6.05e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 215 AKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSS 294
Cdd:cd14187  46 LKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHR 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 295 KGIIHRDLAARNCLVTQDLKAKISDFGLSlqgTEVT-----TKNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd14187 126 NRVIHRDLKLGNLFLNDDMEVKIGDFGLA---TKVEydgerKKTLCGTP-NYIAPEVLSKKGHSFEVDIWSIGCIMYTLL 201
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
175-448 6.06e-13

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 69.23  E-value: 6.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFKGQYKAvgstnppiEVAVK--RILGNaKRKQIQEFCNEAQIMTVLQHENIVAFYGfASLEEP-I 251
Cdd:cd14152   2 IELGELIGQGRWGKVHRGRWHG--------EVAIRllEIDGN-NQDHLKLFKKEVMNYRQTRHENVVLFMG-ACMHPPhL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 MVVMELVTGGDLRKYL---QTTQNIPKLQILwfAMNVASGMRHLSSKGIIHRDLAARNCLVTQDlKAKISDFGL-SLQGT 327
Cdd:cd14152  72 AIITSFCKGRTLYSFVrdpKTSLDINKTRQI--AQEIIKGMGYLHAKGIVHKDLKSKNVFYDNG-KVVITDFGLfGISGV 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 328 --EVTTKNLEKAPIRW---LAPESLKSGM---------FNEKTDVWSYGVFLTELMARCehdplYPKSLKDAKAWILTEE 393
Cdd:cd14152 149 vqEGRRENELKLPHDWlcyLAPEIVREMTpgkdedclpFSKAADVYAFGTIWYELQARD-----WPLKNQPAEALIWQIG 223
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 394 RPHKMEN-----GDPKELMVLIDACCERNPNERLNFNtvkrqitdIYMEALNKGPQDGRK 448
Cdd:cd14152 224 SGEGMKQvlttiSLGKEVTEILSACWAFDLEERPSFT--------LLMDMLEKLPKLNRR 275
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
179-422 6.76e-13

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 70.24  E-value: 6.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRILGN---AKRKQIqefCNEAQIMTVLQHENIVAFYGFASLEEPIMVVM 255
Cdd:PLN00034  80 NRIGSGAGGTVYKVIHRPTGR-----LYALKVIYGNhedTVRRQI---CREIEILRDVNHPNVVKCHDMFDHNGEIQVLL 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  256 ELVTGGDLrkylQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTeVTTKN 333
Cdd:PLN00034 152 EFMDGGSL----EGTHIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSriLAQT-MDPCN 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  334 LEKAPIRWLAPE----SLKSGMFNEKT-DVWSYGVFLTEL-MARcehdplYPKSLKDAKAW------ILTEERPHKMENG 401
Cdd:PLN00034 227 SSVGTIAYMSPErintDLNHGAYDGYAgDIWSLGVSILEFyLGR------FPFGVGRQGDWaslmcaICMSQPPEAPATA 300
                        250       260
                 ....*....|....*....|.
gi 17542550  402 DPkELMVLIDACCERNPNERL 422
Cdd:PLN00034 301 SR-EFRHFISCCLQREPAKRW 320
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
198-431 6.84e-13

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; 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 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. The Jak1 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: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 68.81  E-value: 6.84e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 198 GSTNPPIEVAVKrILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTGGDLRKYLQTTQNIpkLQ 277
Cdd:cd05077  31 YSYEKEIKVILK-VLDPSHRDISLAFFETASMMRQVSHKHIVLLYGVCVRDVENIMVEEFVEFGPLDLFMHRKSDV--LT 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 278 ILW---FAMNVASGMRHLSSKGIIHRDLAARNCLVTQD-LKAKISDF-GLSLQGTEVTTKNLEKA--PIRWLAPESLK-S 349
Cdd:cd05077 108 TPWkfkVAKQLASALSYLEDKDLVHGNVCTKNILLAREgIDGECGPFiKLSDPGIPITVLSRQECveRIPWIAPECVEdS 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 350 GMFNEKTDVWSYGVFLTELMARCEhDPLYPKSLKDAKAWILTEERPhkmENGDPKELMVLIDACCERNPNERLNFNTVKR 429
Cdd:cd05077 188 KNLSIAADKWSFGTTLWEICYNGE-IPLKDKTLAEKERFYEGQCML---VTPSCKELADLMTHCMNYDPNQRPFFRAIMR 263

                ..
gi 17542550 430 QI 431
Cdd:cd05077 264 DI 265
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
181-370 7.06e-13

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: 69.31  E-value: 7.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTNPPIEVAVKRIlgnAKRKQIQEFCNEAQIMTVLQHENIVAF-YGFASlEEPIMVVMELVT 259
Cdd:cd05605   8 LGKGGFGEVCACQVRATGKMYACKKLEKKRI---KKRKGEAMALNEKQILEKVNSRFVVSLaYAYET-KDALCLVLTIMN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 260 GGDLRKYLQTTQN--IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLEKA 337
Cdd:cd05605  84 GGDLKFHIYNMGNpgFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGETIRGRVG 163
                       170       180       190
                ....*....|....*....|....*....|...
gi 17542550 338 PIRWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd05605 164 TVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIE 196
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
176-365 7.07e-13

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


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 69.64  E-value: 7.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 176 NLDKKLGCGAFGEVFKGQYKAVGStnppiEVAVKRIlgnAKRKQIQEfcnEAQIMTVLQ-HENIVAFYGFASLEEPIMVV 254
Cdd:cd14092   9 LREEALGDGSFSVCRKCVHKKTGQ-----EFAVKIV---SRRLDTSR---EVQLLRLCQgHPNIVKLHEVFQDELHTYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDL----RKYLQTTQN-----IPKLqilwfamnvASGMRHLSSKGIIHRDLAARNCLVTQ---DLKAKISDFGL 322
Cdd:cd14092  78 MELLRGGELleriRKKKRFTESeasriMRQL---------VSAVSFMHSKGVVHRDLKPENLLFTDeddDAEIKIVDFGF 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17542550 323 SLQGTEvttKNLEKAP---IRWLAPESLKSGM----FNEKTDVWSYGVFL 365
Cdd:cd14092 149 ARLKPE---NQPLKTPcftLPYAAPEVLKQALstqgYDESCDLWSLGVIL 195
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
177-377 8.82e-13

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


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 68.48  E-value: 8.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVfkgqyKAVGSTNPPIEVAVKRILGNAKRKQ-IQEFC-NEAQIMTVLQHENIVAFYG-FASLEEPIMV 253
Cdd:cd14163   4 LGKTIGEGTYSKV-----KEAFSKKHQRKVAIKIIDKSGGPEEfIQRFLpRELQIVERLDHKNIIHVYEmLESADGKIYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVtQDLKAKISDFGLSLQgTEVTTKN 333
Cdd:cd14163  79 VMELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFGFAKQ-LPKGGRE 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17542550 334 LEK---APIRWLAPESLKSGMFN-EKTDVWSYGVFLTELMarCEHDPL 377
Cdd:cd14163 157 LSQtfcGSTAYAAPEVLQGVPHDsRKGDIWSMGVVLYVML--CAQLPF 202
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
179-382 8.91e-13

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: 70.03  E-value: 8.91e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKavgSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVA-FYGFASlEEPIMVVMEL 257
Cdd:cd05622  79 KVIGRGAFGEVQLVRHK---STRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQlFYAFQD-DRYLYMVMEY 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKyLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLEKA 337
Cdd:cd05622 155 MPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTA 233
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17542550 338 --PIRWLAPESLKS----GMFNEKTDVWSYGVFLTELMArcEHDPLYPKSL 382
Cdd:cd05622 234 vgTPDYISPEVLKSqggdGYYGRECDWWSVGVFLYEMLV--GDTPFYADSL 282
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
176-379 1.05e-12

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 69.37  E-value: 1.05e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 176 NLdKKLGCGAFGEVFKGqYKAVGSTNppieVAVKRI------LGNAKRKQiqefcNEAQIMTVLQHENIV----AFYGFA 245
Cdd:cd07850   4 NL-KPIGSGAQGIVCAA-YDTVTGQN----VAIKKLsrpfqnVTHAKRAY-----RELVLMKLVNHKNIIgllnVFTPQK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 246 SLEE--PIMVVMELVTGgDLRKYLQTTQNIPKLQILWFAMnvASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS 323
Cdd:cd07850  73 SLEEfqDVYLVMELMDA-NLCQVIQMDLDHERMSYLLYQM--LCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLA 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17542550 324 -LQGTE------VTTKnlekapiRWLAPESLkSGM-FNEKTDVWSYGVFLTElMARceHDPLYP 379
Cdd:cd07850 150 rTAGTSfmmtpyVVTR-------YYRAPEVI-LGMgYKENVDIWSVGCIMGE-MIR--GTVLFP 202
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
177-369 1.11e-12

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: 69.18  E-value: 1.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQimTVLQHENIVAF-----YGFASlEEPI 251
Cdd:cd05614   4 LLKVLGTGAYGKVFLVRKVSGHDANKLYAMKVLRKAALVQKAKTVEHTRTER--NVLEHVRQSPFlvtlhYAFQT-DAKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 MVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSlqgTEVTT 331
Cdd:cd05614  81 HLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLS---KEFLT 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 17542550 332 KNLEK-----APIRWLAPESLKS-GMFNEKTDVWSYGVFLTELM 369
Cdd:cd05614 158 EEKERtysfcGTIEYMAPEIIRGkSGHGKAVDWWSLGILMFELL 201
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
177-378 1.16e-12

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: 68.70  E-value: 1.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKavGSTNPPievAVKRILGNAKRKQIQefcNEAQIMTVLQHENIVAFYGFASLEEPIMVVME 256
Cdd:cd14085   7 IESELGRGATSVVYRCRQK--GTQKPY---AVKKLKKTVDKKIVR---TEIGVLLRLSHPNIIKLKEIFETPTEISLVLE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDL------RKYLQTTQNIPKL-QILwfamnvaSGMRHLSSKGIIHRDLAARNCLVT---QDLKAKISDFGLS-LQ 325
Cdd:cd14085  79 LVTGGELfdriveKGYYSERDAADAVkQIL-------EAVAYLHENGIVHRDLKPENLLYAtpaPDAPLKIADFGLSkIV 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17542550 326 GTEVTTKNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMarCEHDPLY 378
Cdd:cd14085 152 DQQVTMKTVCGTP-GYCAPEILRGCAYGPEVDMWSVGVITYILL--CGFEPFY 201
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
179-409 1.17e-12

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: 68.24  E-value: 1.17e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRI--LGNAKRKQIQEFC------------NEAQIMTVLQHENIVAFYGF 244
Cdd:cd14077   7 KTIGAGSMGKVKLAKHIRTGE-----KCAIKIIprASNAGLKKEREKRlekeisrdirtiREAALSSLLNHPHICRLRDF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 245 ASLEEPIMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSL 324
Cdd:cd14077  82 LRTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLSN 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 325 QGTEVTTKNLEKAPIRWLAPESLKSGMF-NEKTDVWSYGVFLTELMARC-----EHDPLYPKSLKDAK----AWILTE-- 392
Cdd:cd14077 162 LYDPRRLLRTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKvpfddENMPALHAKIKKGKveypSYLSSEck 241
                       250
                ....*....|....*..
gi 17542550 393 ERPHKMENGDPKELMVL 409
Cdd:cd14077 242 SLISRMLVVDPKKRATL 258
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
179-422 1.33e-12

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: 68.01  E-value: 1.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVfkgqYKAVGSTNppIEVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHE-NIVAFYGFASLEEP--IMVV 254
Cdd:cd14131   7 KQLGKGGSSKV----YKVLNPKK--KIYALKRVdLEGADEQTLQSYKNEIELLKKLKGSdRIIQLYDYEVTDEDdyLYMV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELvTGGDLRKYLQT--TQNIPklqiLWFAMNVASGM----RHLSSKGIIHRDLAARNCLVTQDlKAKISDFGLSLQGTE 328
Cdd:cd14131  81 MEC-GEIDLATILKKkrPKPID----PNFIRYYWKQMleavHTIHEEGIVHSDLKPANFLLVKG-RLKLIDFGIAKAIQN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 329 VTT---KNLEKAPIRWLAPESLKSGMFNE----------KTDVWSYGVFLTELMARceHDPL--YPKSLKDAKAwILTEE 393
Cdd:cd14131 155 DTTsivRDSQVGTLNYMSPEAIKDTSASGegkpkskigrPSDVWSLGCILYQMVYG--KTPFqhITNPIAKLQA-IIDPN 231
                       250       260       270
                ....*....|....*....|....*....|.
gi 17542550 394 rpHKMENGD--PKELMVLIDACCERNPNERL 422
Cdd:cd14131 232 --HEIEFPDipNPDLIDVMKRCLQRDPKKRP 260
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
234-435 1.39e-12

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: 67.90  E-value: 1.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 234 QHENIVAFYG------FASLEEP-IMVVMELVTGgDLRKYLQTTQNIP-KLQIlwfAMNVASGMRHLSSKGIIHRDLAAR 305
Cdd:cd13975  56 KHERIVSLHGsvidysYGGGSSIaVLLIMERLHR-DLYTGIKAGLSLEeRLQI---ALDVVEGIRFLHSQGLVHRDIKLK 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 306 NCLVTQDLKAKISDFGLS-----LQGTEVTTknlekaPIRwLAPEsLKSGMFNEKTDVWSYGVFLTELMARCEHDPL-YP 379
Cdd:cd13975 132 NVLLDKKNRAKITDLGFCkpeamMSGSIVGT------PIH-MAPE-LFSGKYDNSVDVYAFGILFWYLCAGHVKLPEaFE 203
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17542550 380 KSLKDAKAWILTEE--RPHKMENGDpKELMVLIDACCERNPNERLNFNTVKRQITDIY 435
Cdd:cd13975 204 QCASKDHLWNNVRKgvRPERLPVFD-EECWNLMEACWSGDPSQRPLLGIVQPKLQGIM 260
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
179-368 1.49e-12

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: 68.85  E-value: 1.49e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNA--KRKQIQEFCNEAQIMTVLQHENIV-AFYGFASlEEPIMVVM 255
Cdd:cd05573   7 KVIGRGAFGEVWLVRDKDTGQV-----YAMKILRKSDmlKREQIAHVRAERDILADADSPWIVrLHYAFQD-EDHLYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS------------ 323
Cdd:cd05573  81 EYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCtkmnksgdresy 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17542550 324 -LQGTEVTTKNLEKAPIRWL-----------------APESLKSGMFNEKTDVWSYGVFLTEL 368
Cdd:cd05573 161 lNDSVNTLFQDNVLARRRPHkqrrvraysavgtpdyiAPEVLRGTGYGPECDWWSLGVILYEM 223
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
177-422 1.57e-12

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: 68.10  E-value: 1.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFkgQYKAVGSTNPPIEVAVKrILGNA----KRKQIQEFCNEAQimtVLQHENIVAF-----YGFASl 247
Cdd:cd05613   4 LLKVLGTGAYGKVF--LVRKVSGHDAGKLYAMK-VLKKAtivqKAKTAEHTRTERQ---VLEHIRQSPFlvtlhYAFQT- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 248 EEPIMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSlqgT 327
Cdd:cd05613  77 DTKLHLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLS---K 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 328 EVTTKNLEKA-----PIRWLAPESLKSG--MFNEKTDVWSYGVFLTELMARCEhdPLYPKSLKDAKAWIltEERPHKMEN 400
Cdd:cd05613 154 EFLLDENERAysfcgTIEYMAPEIVRGGdsGHDKAVDWWSLGVLMYELLTGAS--PFTVDGEKNSQAEI--SRRILKSEP 229
                       250       260
                ....*....|....*....|....*.
gi 17542550 401 GDPKELMVLIDACCER----NPNERL 422
Cdd:cd05613 230 PYPQEMSALAKDIIQRllmkDPKKRL 255
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
179-365 1.94e-12

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: 67.36  E-value: 1.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVfKGQYKAVGSTnppiEVAVKrILGNAK--RKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVME 256
Cdd:cd14075   8 GELGSGNFSQV-KLGIHQLTKE----KVAIK-ILDKTKldQKTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQNIPKL--QILwFAmNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNL 334
Cdd:cd14075  82 YASGGELYTKISTEGKLSESeaKPL-FA-QIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKRGETLNT 159
                       170       180       190
                ....*....|....*....|....*....|..
gi 17542550 335 EKAPIRWLAPESLK-SGMFNEKTDVWSYGVFL 365
Cdd:cd14075 160 FCGSPPYAAPELFKdEHYIGIYVDIWALGVLL 191
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
179-393 2.13e-12

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


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 68.15  E-value: 2.13e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKrILgnaKRKQIQEFCNEAQIMT---VLQ---HENIVAF-YGFASlEEPI 251
Cdd:cd05571   1 KVLGKGTFGKVILCREKATGEL-----YAIK-IL---KKEVIIAKDEVAHTLTenrVLQntrHPFLTSLkYSFQT-NDRL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 MVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTE--V 329
Cdd:cd05571  71 CFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISygA 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17542550 330 TTKNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMarCEHDPLYPKSLKDAKAWILTEE 393
Cdd:cd05571 151 TTKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMM--CGRLPFYNRDHEVLFELILMEE 211
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
230-442 2.66e-12

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: 67.05  E-value: 2.66e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 230 MTVLQHENIVAFYGFASLEEPIMVVMELVTGGDLRKYLQTtQNIP-----KLQILwfaMNVASGMRHLSSKGIIHRDLAA 304
Cdd:cd14043  50 LRELRHENVNLFLGLFVDCGILAIVSEHCSRGSLEDLLRN-DDMKldwmfKSSLL---LDLIKGMRYLHHRGIVHGRLKS 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 305 RNCLVTQDLKAKISDFGLS--LQGTEVTTKNLEKAPIRWLAPESLKSGMFNEKT----DVWSYGVFLTELMARCEhdply 378
Cdd:cd14043 126 RNCVVDGRFVLKITDYGYNeiLEAQNLPLPEPAPEELLWTAPELLRDPRLERRGtfpgDVFSFAIIMQEVIVRGA----- 200
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17542550 379 PKSLKDAKAWILTEE--------RPHKMENGDPKELMVLIDACCERNPNERLNFNTVKRQITDIymealNKG 442
Cdd:cd14043 201 PYCMLGLSPEEIIEKvrsppplcRPSVSMDQAPLECIQLMKQCWSEAPERRPTFDQIFDQFKSI-----NKG 267
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
179-424 3.28e-12

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: 67.65  E-value: 3.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKavGSTNPpieVAVKRILGNA--KRKQIQEFCNEAQIMTVLQHENIVAFYgfASLEEP--IMVV 254
Cdd:cd05574   7 KLLGKGDVGRVYLVRLK--GTGKL---FAMKVLDKEEmiKRNKVKRVLTEREILATLDHPFLPTLY--ASFQTSthLCFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTTQN--IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTT- 331
Cdd:cd05574  80 MDYCPGGELFRLLQKQPGkrLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKQSSVTPPp 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 332 -----------KNLEKAPIR------------------WLAPESLKSGMFNEKTDVWSYGVFLTELMARCEhdPLYPKSL 382
Cdd:cd05574 160 vrkslrkgsrrSSVKSIEKEtfvaepsarsnsfvgteeYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTT--PFKGSNR 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 17542550 383 KDAKAWILTEERPHKMENGDPKELMVLIDACCERNPNERLNF 424
Cdd:cd05574 238 DETFSNILKKELTFPESPPVSSEAKDLIRKLLVKDPSKRLGS 279
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
179-422 3.42e-12

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: 67.43  E-value: 3.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVF---------KGQYKAvgstnppIEVAVKRILGNAKRKQIQefcNEAQIMTVLQHENIVAF-YGFASlE 248
Cdd:cd05582   1 KVLGQGSFGKVFlvrkitgpdAGTLYA-------MKVLKKATLKVRDRVRTK---MERDILADVNHPFIVKLhYAFQT-E 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 249 EPIMVVMELVTGGDL-----RKYLQTTQNIPklqilWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS 323
Cdd:cd05582  70 GKLYLILDFLRGGDLftrlsKEVMFTEEDVK-----FYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLS 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 324 LQGTEVTTKNLE-KAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMArcEHDPLYPKSLKDAKAWILteerphKMENGD 402
Cdd:cd05582 145 KESIDHEKKAYSfCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT--GSLPFQGKDRKETMTMIL------KAKLGM 216
                       250       260
                ....*....|....*....|....
gi 17542550 403 PK----ELMVLIDACCERNPNERL 422
Cdd:cd05582 217 PQflspEAQSLLRALFKRNPANRL 240
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
176-368 3.43e-12

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


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 67.32  E-value: 3.43e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 176 NLDKKLGCGAFGEVFKGQYKAVGSTNppiEVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:cd08216   1 ELLYEIGKCFKGGGVVHLAKHKPTNT---LVAVKKInLESDSKEDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYVV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQT--TQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSL----QGTE 328
Cdd:cd08216  78 TPLMAYGSCRDLLKThfPEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYsmvkHGKR 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17542550 329 VT---------TKNLEkapirWLAPESLKSGM--FNEKTDVWSYGVFLTEL 368
Cdd:cd08216 158 QRvvhdfpkssEKNLP-----WLSPEVLQQNLlgYNEKSDIYSVGITACEL 203
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
179-422 3.89e-12

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


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 66.48  E-value: 3.89e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGST--NPPIEVAVKRILGNAKRKQIQefcNEAQIMTVLQ-HENIVA-FYGFASlEEPIMVV 254
Cdd:cd14019   7 EKIGEGTFSSVYKAEDKLHDLYdrNKGRLVALKHIYPTSSPSRIL---NELECLERLGgSNNVSGlITAFRN-EDQVVAV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTtqnIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDL-KAKISDFGLSlQGTEvtTKN 333
Cdd:cd14019  83 LPYIEHDDFRDFYRK---MSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETgKGVLVDFGLA-QREE--DRP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 334 LEKAP------IRwlAPESL-KSGMFNEKTDVWSYGVFLTELMARCeHDPLYPKSLKDAKAWILTeerphkmENGDPkEL 406
Cdd:cd14019 157 EQRAPragtrgFR--APEVLfKCPHQTTAIDIWSAGVILLSILSGR-FPFFFSSDDIDALAEIAT-------IFGSD-EA 225
                       250
                ....*....|....*.
gi 17542550 407 MVLIDACCERNPNERL 422
Cdd:cd14019 226 YDLLDKLLELDPSKRI 241
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
173-379 4.00e-12

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: 66.91  E-value: 4.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 173 STINLdKKLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIM 252
Cdd:cd07870   1 SYLNL-EKLGEGSYATVYKGISRINGQL-----VALKVISMKTEEGVPFTAIREASLLKGLKHANIVLLHDIIHTKETLT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGgDLRKYL-QTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS-LQGTEVT 330
Cdd:cd07870  75 FVFEYMHT-DLAQYMiQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLArAKSIPSQ 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17542550 331 TKNLEKAPIRWLAPESL-KSGMFNEKTDVWSYGVFLTELMarcEHDPLYP 379
Cdd:cd07870 154 TYSSEVVTLWYRPPDVLlGATDYSSALDIWGAGCIFIEML---QGQPAFP 200
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
179-371 4.57e-12

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: 66.67  E-value: 4.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMEL 257
Cdd:cd07861   6 EKIGEGTYGVVYKGRNKKTGQI-----VAMKKIrLESEEEGVPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGgDLRKYLQTT---QNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ-GTEVTTKN 333
Cdd:cd07861  81 LSM-DLKKYLDSLpkgKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAfGIPVRVYT 159
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 17542550 334 LEKAPIRWLAPESL-KSGMFNEKTDVWSYGVFLTELMAR 371
Cdd:cd07861 160 HEVVTLWYRAPEVLlGSPRYSTPVDIWSIGTIFAEMATK 198
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
179-379 4.70e-12

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 67.76  E-value: 4.70e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGeVFKGQYKAVGSTNppieVAVKRI------LGNAKRKQiqefcNEAQIMTVLQHENIVA----FYGFASLE 248
Cdd:cd07875  30 KPIGSGAQG-IVCAAYDAILERN----VAIKKLsrpfqnQTHAKRAY-----RELVLMKCVNHKNIIGllnvFTPQKSLE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 249 E--PIMVVMELVTGgDLRKYLQTTQNIPKLQILWFAMnvASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQG 326
Cdd:cd07875 100 EfqDVYIVMELMDA-NLCQVIQMELDHERMSYLLYQM--LCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTA 176
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17542550 327 TEVTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMArceHDPLYP 379
Cdd:cd07875 177 GTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIK---GGVLFP 226
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
179-379 4.81e-12

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 67.42  E-value: 4.81e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGeVFKGQYKAVGSTNppieVAVKRI------LGNAKRKQiqefcNEAQIMTVLQHENIVA----FYGFASLE 248
Cdd:cd07874  23 KPIGSGAQG-IVCAAYDAVLDRN----VAIKKLsrpfqnQTHAKRAY-----RELVLMKCVNHKNIISllnvFTPQKSLE 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 249 E--PIMVVMELVTGgDLRKYLQTTQNIPKLQILWFAMnvASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQG 326
Cdd:cd07874  93 EfqDVYLVMELMDA-NLCQVIQMELDHERMSYLLYQM--LCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTA 169
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17542550 327 TEVTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMarcEHDPLYP 379
Cdd:cd07874 170 GTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMV---RHKILFP 219
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
179-379 6.33e-12

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 66.38  E-value: 6.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMEL 257
Cdd:PLN00009   8 EKIGEGTYGVVYKARDRVTNET-----IALKKIrLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVFEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  258 VTGgDLRKYLQTTQNIPKLQ--ILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKA-KISDFGLSLQ-GTEVTTKN 333
Cdd:PLN00009  83 LDL-DLKKHMDSSPDFAKNPrlIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNAlKLADFGLARAfGIPVRTFT 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 17542550  334 LEKAPIRWLAPES-LKSGMFNEKTDVWSYGVFLTELMarcEHDPLYP 379
Cdd:PLN00009 162 HEVVTLWYRAPEIlLGSRHYSTPVDIWSVGCIFAEMV---NQKPLFP 205
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
176-372 6.45e-12

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: 65.97  E-value: 6.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 176 NLDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVM 255
Cdd:cd14105   8 DIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASRRGVSREDIEREVSILRQVLHPNIITLHDVFENKTDVVLIL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNC-LVTQDL---KAKISDFGLSLQ---GTE 328
Cdd:cd14105  88 ELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENImLLDKNVpipRIKLIDFGLAHKiedGNE 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 17542550 329 VttKNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMARC 372
Cdd:cd14105 168 F--KNIFGTP-EFVAPEIVNYEPLGLEADMWSIGVITYILLSGA 208
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
179-363 6.58e-12

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: 65.82  E-value: 6.58e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd14184   7 KVIGDGNFAVVKECVERSTGK-----EFALKIIDKAKCCGKEHLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVMELV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLV------TQDLkaKISDFGLS--LQGTEVT 330
Cdd:cd14184  82 KGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypdgTKSL--KLGDFGLAtvVEGPLYT 159
                       170       180       190
                ....*....|....*....|....*....|...
gi 17542550 331 TKNlekAPIrWLAPESLKSGMFNEKTDVWSYGV 363
Cdd:cd14184 160 VCG---TPT-YVAPEIIAETGYGLKVDIWAAGV 188
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
179-369 6.63e-12

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 66.90  E-value: 6.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRILGN------AKRKQiqefcNEAQIMTVLQHENIVAFYGFASLEEPI- 251
Cdd:cd07880  21 KQVGSGAYGTVCSALDRRTGA-----KVAIKKLYRPfqselfAKRAY-----RELRLLKHMKHENVIGLLDVFTPDLSLd 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 -----MVVMELVtGGDLRKyLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQG 326
Cdd:cd07880  91 rfhdfYLVMPFM-GTDLGK-LMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQT 168
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17542550 327 -TEVTTKNLekapIRWL-APESLKSGM-FNEKTDVWSYGVFLTELM 369
Cdd:cd07880 169 dSEMTGYVV----TRWYrAPEVILNWMhYTQTVDIWSVGCIMAEML 210
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
179-369 6.69e-12

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 66.85  E-value: 6.69e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRIlgnAKRKQIQEFCNEA----QIMTVLQHENIVA-------------F 241
Cdd:cd07879  21 KQVGSGAYGSVCSAIDKRTGE-----KVAIKKL---SRPFQSEIFAKRAyrelTLLKHMQHENVIGlldvftsavsgdeF 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 242 YGFaSLEEPIMVVmelvtggDLRKYLQTTQNIPKLQILWFAMnvASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFG 321
Cdd:cd07879  93 QDF-YLVMPYMQT-------DLQKIMGHPLSEDKVQYLVYQM--LCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFG 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17542550 322 LS------LQGTEVTtknlekapiRWL-APESLKSGM-FNEKTDVWSYGVFLTELM 369
Cdd:cd07879 163 LArhadaeMTGYVVT---------RWYrAPEVILNWMhYNQTVDIWSVGCIMAEML 209
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
181-402 6.83e-12

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: 66.29  E-value: 6.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKgqykaVGSTNPPIEV-AVKRI----LGNAKRKQIQEfcnEAQIMTVLQ---HENIVAFYGFASLEEPIM 252
Cdd:cd14052   8 IGSGEFSQVYK-----VSERVPTGKVyAVKKLkpnyAGAKDRLRRLE---EVSILRELTldgHDNIVQLIDSWEYHGHLY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYLQTTQNIPKL------QILwfaMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSlqg 326
Cdd:cd14052  80 IQTELCENGSLDVFLSELGLLGRLdefrvwKIL---VELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMA--- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 327 tevTT----KNLEKAPIR-WLAPESLKSGMFNEKTDVWSYGVFLTELMARCEhdplypksLKD-AKAWilteerpHKMEN 400
Cdd:cd14052 154 ---TVwpliRGIEREGDReYIAPEILSEHMYDKPADIFSLGLILLEAAANVV--------LPDnGDAW-------QKLRS 215

                ..
gi 17542550 401 GD 402
Cdd:cd14052 216 GD 217
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
175-379 7.48e-12

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 66.71  E-value: 7.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  175 INLDKKLGCGAFGEVFKGQYKAVGStnppiEVAVKRI------LGNAKRKQIQEFCN-------EAQIMTVLQHENIVAF 241
Cdd:PTZ00024  11 IQKGAHLGEGTYGKVEKAYDTLTGK-----IVAIKKVkiieisNDVTKDRQLVGMCGihfttlrELKIMNEIKHENIMGL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  242 YGFASLEEPIMVVMELVTGgDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFG 321
Cdd:PTZ00024  86 VDVYVEGDFINLVMDIMAS-DLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFG 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17542550  322 LS-----------LQGTEVTTKNLEKAP----IRWLAPESL-KSGMFNEKTDVWSYGVFLTELMARcehDPLYP 379
Cdd:PTZ00024 165 LArrygyppysdtLSKDETMQRREEMTSkvvtLWYRAPELLmGAEKYHFAVDMWSVGCIFAELLTG---KPLFP 235
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
184-379 8.77e-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: 66.09  E-value: 8.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 184 GAFGEVFKGQYKAVGSTnppieVAVKRIlgnaK-RKQIQEF----CNEAQIMTVLQHENIVafygfaSLEE--------P 250
Cdd:cd07843  16 GTYGVVYRARDKKTGEI-----VALKKL----KmEKEKEGFpitsLREINILLKLQHPNIV------TVKEvvvgsnldK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMELVTGgDLRKYLQT-----TQNIPK---LQILwfamnvaSGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGL 322
Cdd:cd07843  81 IYMVMEYVEH-DLKSLMETmkqpfLQSEVKclmLQLL-------SGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGL 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17542550 323 SLQGTEVTTKNLEKAPIRWL-APESL-KSGMFNEKTDVWSYGVFLTELMARcehDPLYP 379
Cdd:cd07843 153 AREYGSPLKPYTQLVVTLWYrAPELLlGAKEYSTAIDMWSVGCIFAELLTK---KPLFP 208
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
180-368 9.82e-12

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: 65.66  E-value: 9.82e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRkqiQEF----CNEAQIMTVLQHENIVafygfaSLEEpiMVVM 255
Cdd:cd07840   6 QIGEGTYGQVYKARNKKTGEL-----VALKKIRMENEK---EGFpitaIREIKLLQKLDHPNVV------RLKE--IVTS 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGG-------------DLRKYLQTTQN---IPKL-----QILwfamnvaSGMRHLSSKGIIHRDLAARNCLVTQDLK 314
Cdd:cd07840  70 KGSAKYkgsiymvfeymdhDLTGLLDNPEVkftESQIkcymkQLL-------EGLQYLHSNGILHRDIKGSNILINNDGV 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17542550 315 AKISDFGLSlqgtevTTKNLEKAPI-------RWLAPESLKSGMFNEKT--DVWSYGVFLTEL 368
Cdd:cd07840 143 LKLADFGLA------RPYTKENNADytnrvitLWYRPPELLLGATRYGPevDMWSVGCILAEL 199
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
194-421 9.87e-12

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 67.35  E-value: 9.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  194 YKAVGSTNPPIEVAVKRILGNAKRkQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTGGDLRKYLQT--TQ 271
Cdd:PTZ00267  84 FVATRGSDPKEKVVAKFVMLNDER-QAAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKQrlKE 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  272 NIP----KLQILWFAMNVAsgMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLEKA----PIrWLA 343
Cdd:PTZ00267 163 HLPfqeyEVGLLFYQIVLA--LDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSLDVASSfcgtPY-YLA 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  344 PESLKSGMFNEKTDVWSYGVFLTELMARceHDPLYPKSLKDAKAWILteerphkMENGDP------KELMVLIDACCERN 417
Cdd:PTZ00267 240 PELWERKRYSKKADMWSLGVILYELLTL--HRPFKGPSQREIMQQVL-------YGKYDPfpcpvsSGMKALLDPLLSKN 310

                 ....
gi 17542550  418 PNER 421
Cdd:PTZ00267 311 PALR 314
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
179-433 1.00e-11

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: 65.78  E-value: 1.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKrKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEP-----IMV 253
Cdd:cd13986   6 RLLGEGGFSFVYLVEDLSTGRL-----YALKKILCHSK-EDVKEAMREIENYRLFNHPNILRLLDSQIVKEAggkkeVYL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQN----IPKLQILWFAMNVASGMRHL---SSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQG 326
Cdd:cd13986  80 LLPYYKRGSLQDEIERRLVkgtfFPEDRILHIFLGICRGLKAMhepELVPYAHRDIKPGNVLLSEDDEPILMDLGSMNPA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 327 T-EVTTKNL---------EKAPIRWLAPE--SLKSG-MFNEKTDVWSYGVFLTELM-ARCEHDPLYPK--SLKDAkawIL 390
Cdd:cd13986 160 RiEIEGRREalalqdwaaEHCTMPYRAPElfDVKSHcTIDEKTDIWSLGCTLYALMyGESPFERIFQKgdSLALA---VL 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 17542550 391 TEERPHKMENGDPKELMVLIDACCERNPNERLNFNTVKRQITD 433
Cdd:cd13986 237 SGNYSFPDNSRYSEELHQLVKSMLVVNPAERPSIDDLLSRVHD 279
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
179-428 1.03e-11

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: 65.59  E-value: 1.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVK-RILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASleEPIMVVMEL 257
Cdd:cd14025   2 EKVGSGGFGQVYKVRHKHWKT-----WLAIKcPPSLHVDDSERMELLEEAKKMEMAKFRHILPVYGICS--EPVGLVMEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLqTTQNIP---KLQILWfamNVASGMR--HLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTK 332
Cdd:cd14025  75 METGSLEKLL-ASEPLPwelRFRIIH---ETAVGMNflHCMKPPLLHLDLKPANILLDAHYHVKISDFGLAKWNGLSHSH 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 333 NLEKAPIR----WLAPESL--KSGMFNEKTDVWSYGVFLTELMAR----CEHDPLYPKSLKDAKAW-----ILTEERPHK 397
Cdd:cd14025 151 DLSRDGLRgtiaYLPPERFkeKNRCPDTKHDVYSFAIVIWGILTQkkpfAGENNILHIMVKVVKGHrpslsPIPRQRPSE 230
                       250       260       270
                ....*....|....*....|....*....|.
gi 17542550 398 MENgdpkeLMVLIDACCERNPNERLNFNTVK 428
Cdd:cd14025 231 CQQ-----MICLMKRCWDQDPRKRPTFQDIT 256
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
179-406 1.14e-11

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


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 66.59  E-value: 1.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNA--KRKQIQEFCNEAQIMTVLQHENIVA-FYGFASLEEpIMVVM 255
Cdd:cd05600  17 TQVGQGGYGSVFLARKKDTGEI-----CALKIMKKKVlfKLNEVNHVLTERDILTTTNSPWLVKlLYAFQDPEN-VYLAM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQG--------T 327
Cdd:cd05600  91 EYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASGTlspkkiesM 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 328 EVTTKNLEKAPIR------------------------------WLAPESLKSGMFNEKTDVWSYGVFLTELMarCEHDPL 377
Cdd:cd05600 171 KIRLEEVKNTAFLeltakerrniyramrkedqnyansvvgspdYMAPEVLRGEGYDLTVDYWSLGCILFECL--VGFPPF 248
                       250       260       270
                ....*....|....*....|....*....|...
gi 17542550 378 YPKSLKDA----KAWILTEERPHKMENGDPKEL 406
Cdd:cd05600 249 SGSTPNETwanlYHWKKTLQRPVYTDPDLEFNL 281
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
235-370 1.15e-11

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: 66.21  E-value: 1.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 235 HENIVAFYGFASLEEPIMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLK 314
Cdd:cd05618  80 HPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGH 159
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17542550 315 AKISDFGLSLQGTEV--TTKNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd05618 160 IKLTDYGMCKEGLRPgdTTSTFCGTP-NYIAPEILRGEDYGFSVDWWALGVLMFEMMA 216
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
181-368 1.42e-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: 65.14  E-value: 1.42e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTnppieVAVKRI--LGNAKRKQ---IQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVM 255
Cdd:cd06630   8 LGTGAFSSCYQARDVKTGTL-----MAVKQVsfCRNSSSEQeevVEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGD----LRKYLQTTQNIpklqILWFAMNVASGMRHLSSKGIIHRDLAARNCLVT---QDLKakISDFGLSLQGTE 328
Cdd:cd06630  83 EWMAGGSvaslLSKYGAFSENV----IINYTLQILRGLAYLHDNQIIHRDLKGANLLVDstgQRLR--IADFGAAARLAS 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17542550 329 VTTKNLE-----KAPIRWLAPESLKSGMFNEKTDVWSYGVFLTEL 368
Cdd:cd06630 157 KGTGAGEfqgqlLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEM 201
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
175-371 1.53e-11

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 65.92  E-value: 1.53e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 175 INLDKKLGCGAFGEVFkgqykAVGSTNPPIEVAVKRI------LGNAKRkqiqeFCNEAQIMTVLQHENIVAFY-----G 243
Cdd:cd07853   2 VEPDRPIGYGAFGVVW-----SVTDPRDGKRVALKKMpnvfqnLVSCKR-----VFRELKMLCFFKHDNVLSALdilqpP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 244 FASLEEPIMVVMELVTGgDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGL- 322
Cdd:cd07853  72 HIDPFEEIYVVTELMQS-DLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLa 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17542550 323 -------SLQGT-EVTTKnlekapiRWLAPESLK-SGMFNEKTDVWSYGVFLTELMAR 371
Cdd:cd07853 151 rveepdeSKHMTqEVVTQ-------YYRAPEILMgSRHYTSAVDIWSVGCIFAELLGR 201
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
179-369 1.60e-11

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 65.82  E-value: 1.60e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGstnppIEVAVKRIL------GNAKRKQiqefcNEAQIMTVLQHENIVA----FYGFASLE 248
Cdd:cd07876  27 KPIGSGAQGIVCAAFDTVLG-----INVAVKKLSrpfqnqTHAKRAY-----RELVLLKCVNHKNIISllnvFTPQKSLE 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 249 E--PIMVVMELVTGgDLRKYLQTTQNIPKLQILWFAMnvASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSlqg 326
Cdd:cd07876  97 EfqDVYLVMELMDA-NLCQVIHMELDHERMSYLLYQM--LCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLA--- 170
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 17542550 327 tEVTTKNLEKAPI----RWLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd07876 171 -RTACTNFMMTPYvvtrYYRAPEVILGMGYKENVDIWSVGCIMGELV 216
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
217-365 1.81e-11

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: 64.99  E-value: 1.81e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 217 RKQIQEFCNEAQIMTVLQHENIVAFygFASLEEP----IMVVMELVTGGDLRKyLQTTQNIPKLQILWFAMNVASGMRHL 292
Cdd:cd14199  66 RGPIERVYQEIAILKKLDHPNVVKL--VEVLDDPsedhLYMVFELVKQGPVME-VPTLKPLSEDQARFYFQDLIKGIEYL 142
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17542550 293 SSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEVTTKNLEKAPIrWLAPESLKS--GMFNEKT-DVWSYGVFL 365
Cdd:cd14199 143 HYQKIIHRDVKPSNLLVGEDGHIKIADFGVSneFEGSDALLTNTVGTPA-FMAPETLSEtrKIFSGKAlDVWAMGVTL 219
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
176-365 1.89e-11

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: 64.34  E-value: 1.89e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 176 NLDKKLGCGAFGEVFKGQYKAVGStnppiEVAVKRI----LGNAKRKQIQEfcnEAQIMTVLQHENIVAFYGFASLEEPI 251
Cdd:cd14071   3 DIERTIGKGNFAVVKLARHRITKT-----EVAIKIIdksqLDEENLKKIYR---EVQIMKMLNHPHIIKLYQVMETKDML 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 MVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS--LQGTEV 329
Cdd:cd14071  75 YLVTEYASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSnfFKPGEL 154
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 17542550 330 TTKNLEKAPirWLAPESLKSGMFN-EKTDVWSYGVFL 365
Cdd:cd14071 155 LKTWCGSPP--YAAPEVFEGKEYEgPQLDIWSLGVVL 189
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
205-363 2.49e-11

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: 64.25  E-value: 2.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 205 EVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMN 284
Cdd:cd14183  33 EYALKIINKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMELVKGGDLFDAITSTNKYTERDASGMLYN 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 285 VASGMRHLSSKGIIHRDLAARNCLVTQDLKA----KISDFGLS--LQGTEVTTKNLEKapirWLAPESLKSGMFNEKTDV 358
Cdd:cd14183 113 LASAIKYLHSLNIVHRDIKPENLLVYEHQDGskslKLGDFGLAtvVDGPLYTVCGTPT----YVAPEIIAETGYGLKVDI 188

                ....*
gi 17542550 359 WSYGV 363
Cdd:cd14183 189 WAAGV 193
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
254-370 3.36e-11

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: 64.75  E-value: 3.36e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEV--TT 331
Cdd:cd05588  74 VIEFVNGGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPgdTT 153
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 17542550 332 KNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd05588 154 STFCGTP-NYIAPEILRGEDYGFSVDWWALGVLMFEMLA 191
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
177-323 4.32e-11

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: 63.63  E-value: 4.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGStnppiEVAVKRILGNAKRKQIQefcNEAQIMTVLQ-HENIVAFYGFASLEEPIMVVM 255
Cdd:cd14016   4 LVKKIGSGSFGEVYLGIDLKTGE-----EVAIKIEKKDSKHPQLE---YEAKVYKLLQgGPGIPRLYWFGQEGDYNVMVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVtgG----DLRKY------LQTtqnipklqILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAK---ISDFGL 322
Cdd:cd14016  76 DLL--GpsleDLFNKcgrkfsLKT--------VLMLADQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNkvyLIDFGL 145

                .
gi 17542550 323 S 323
Cdd:cd14016 146 A 146
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
178-363 4.57e-11

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


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 63.30  E-value: 4.57e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 178 DKKLGCGAFGEVFKGQYKAVGstnppievavKRILgnAKRKQIQEF-CNEAQIMTVLQHENIVAFYGFASLEE-PIMVVM 255
Cdd:cd14109   9 EEDEKRAAQGAPFHVTERSTG----------RNFL--AQLRYGDPFlMREVDIHNSLDHPNIVQMHDAYDDEKlAVTVID 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRK--YLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVtQDLKAKISDFGLSLQGTEVTTKN 333
Cdd:cd14109  77 NLASTIELVRdnLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILL-QDDKLKLADFGQSRRLLRGKLTT 155
                       170       180       190
                ....*....|....*....|....*....|
gi 17542550 334 LEKAPIRWLAPESLKSGMFNEKTDVWSYGV 363
Cdd:cd14109 156 LIYGSPEFVSPEIVNSYPVTLATDMWSVGV 185
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
172-368 4.63e-11

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: 63.46  E-value: 4.63e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 172 HSTINLDKKLGCGAFGEVFkgqykAVGSTNPPIEVAVKRILGNAKrKQIQEFCNEAQIMTVLQ-HENIVAFYGFASLEEP 250
Cdd:cd14037   2 SHHVTIEKYLAEGGFAHVY-----LVKTSNGGNRAALKRVYVNDE-HDLNVCKREIEIMKRLSgHKNIVGYIDSSANRSG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 -----IMVVMELVTGGDLRKYLQTT-----QNIPKLQILWFAMNVASGMRHLSSKgIIHRDLAARNCLVTQDLKAKISDF 320
Cdd:cd14037  76 ngvyeVLLLMEYCKGGGVIDLMNQRlqtglTESEILKIFCDVCEAVAAMHYLKPP-LIHRDLKVENVLISDSGNYKLCDF 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17542550 321 G---------LSLQGTEVTTKNLEK---APIRwlAPE--SLKSG-MFNEKTDVWSYGVFLTEL 368
Cdd:cd14037 155 GsattkilppQTKQGVTYVEEDIKKyttLQYR--APEmiDLYRGkPITEKSDIWALGCLLYKL 215
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
181-379 4.91e-11

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: 63.86  E-value: 4.91e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQEFC-NEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVT 259
Cdd:cd07848   9 VGEGAYGVVLKCRHKETKEI-----VAIKKFKDSEENEEVKETTlRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 260 GGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNL-EKAP 338
Cdd:cd07848  84 KNMLELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSNANYtEYVA 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 17542550 339 IRWL-APESLKSGMFNEKTDVWSYGVFLTELmarCEHDPLYP 379
Cdd:cd07848 164 TRWYrSPELLLGAPYGKAVDMWSVGCILGEL---SDGQPLFP 202
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
180-371 4.99e-11

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: 63.93  E-value: 4.99e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGSTnppieVAVKRIL-GNAKRKQIQEFCNEAQIMTVLQHENIVAFY--------GFASLEEP 250
Cdd:cd07865  19 KIGQGTFGEVFKARHRKTGQI-----VALKKVLmENEKEGFPITALREIKILQLLKHENVVNLIeicrtkatPYNRYKGS 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMELVTGgDLRKYLQTTQNIPKLQILWFAMN-VASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGL----SLQ 325
Cdd:cd07865  94 IYLVFEFCEH-DLAGLLSNKNVKFTLSEIKKVMKmLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLarafSLA 172
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17542550 326 GTEVTTKNLEKAPIRWLAPESLKSG--MFNEKTDVWSYGVFLTELMAR 371
Cdd:cd07865 173 KNSQPNRYTNRVVTLWYRPPELLLGerDYGPPIDMWGAGCIMAEMWTR 220
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
181-372 6.76e-11

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


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 63.51  E-value: 6.76e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAvgsTNppIEVAVKrILGNAKRKQIQEFcneAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd14175   9 IGVGSYSVCKRCVHKA---TN--MEYAVK-VIDKSKRDPSEEI---EILLRYGQHPNIITLKDVYDDGKHVYLVTELMRG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDL----KAKISDFGLSLQ--------GTE 328
Cdd:cd14175  80 GELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESgnpeSLRICDFGFAKQlraengllMTP 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 17542550 329 VTTKNlekapirWLAPESLKSGMFNEKTDVWSYGVFLTELMARC 372
Cdd:cd14175 160 CYTAN-------FVAPEVLKRQGYDEGCDIWSLGILLYTMLAGY 196
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
179-440 8.09e-11

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: 63.50  E-value: 8.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILGNAKRKQIQEFCNeaQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd05602  13 KVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSERN--VLLKNVKHPFLVGLHFSFQTTDKLYFVLDYI 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTE--VTTKNLEK 336
Cdd:cd05602  91 NGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEpnGTTSTFCG 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 337 APiRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEhdPLYPKSLKDAKAWILTeeRPHKMENGDPKELMVLIDACCER 416
Cdd:cd05602 171 TP-EYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLP--PFYSRNTAEMYDNILN--KPLQLKPNITNSARHLLEGLLQK 245
                       250       260
                ....*....|....*....|....
gi 17542550 417 NPNERLNFntvkrqiTDIYMEALN 440
Cdd:cd05602 246 DRTKRLGA-------KDDFTEIKN 262
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
176-376 1.13e-10

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


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 62.05  E-value: 1.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 176 NLDKKLGCGAFG------EVFKGQykavgstnppiEVAVKRI----LGNAKRKQIQEfcnEAQIMTVLQHENIVAFYGFA 245
Cdd:cd14074   6 DLEETLGRGHFAvvklarHVFTGE-----------KVAVKVIdktkLDDVSKAHLFQ---EVRCMKLVQHPNVVRLYEVI 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 246 SLEEPIMVVMELVTGGDLRKYLQTTQN-IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLK-AKISDFGLS 323
Cdd:cd14074  72 DTQTKLYLILELGDGGDMYDYIMKHENgLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQGlVKLTDFGFS 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17542550 324 ---LQGTEVTTKNLEKApirWLAPESLKSGMFNE-KTDVWSYGVFLteLMARCEHDP 376
Cdd:cd14074 152 nkfQPGEKLETSCGSLA---YSAPEILLGDEYDApAVDIWSLGVIL--YMLVCGQPP 203
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
181-369 1.19e-10

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: 63.09  E-value: 1.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTnppieVAVK-----RILGnakRKQIQEFCNEAQIMTVL---QHENIVAFYGFASLEEPIM 252
Cdd:cd05589   7 LGRGHFGKVLLAEYKPTGEL-----FAIKalkkgDIIA---RDEVESLMCEKRIFETVnsaRHPFLVNLFACFQTPEHVC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGGDLRKYLQttQNI-PKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVT- 330
Cdd:cd05589  79 FVMEYAAGGDLMMHIH--EDVfSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGd 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 17542550 331 -TKNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd05589 157 rTSTFCGTP-EFLAPEVLTDTSYTRAVDWWGLGVLIYEML 195
pknD PRK13184
serine/threonine-protein kinase PknD;
179-369 1.31e-10

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 64.41  E-value: 1.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRIlgnakRKQIQE-------FCNEAQIMTVLQHENIVAFYGFASLEEPI 251
Cdd:PRK13184   8 RLIGKGGMGEVYLAYDPVCSR-----RVALKKI-----REDLSEnpllkkrFLREAKIAADLIHPGIVPVYSICSDGDPV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  252 MVVMELVTGGDLRKYLQTT---QNIPK-----------LQILwfaMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKI 317
Cdd:PRK13184  78 YYTMPYIEGYTLKSLLKSVwqkESLSKelaektsvgafLSIF---HKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVI 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17542550  318 SDFGLSLqgtevtTKNLE-------KAPIR------------------WLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:PRK13184 155 LDWGAAI------FKKLEeedlldiDVDERnicyssmtipgkivgtpdYMAPERLLGVPASESTDIYALGVILYQML 225
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
179-370 1.39e-10

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 62.19  E-value: 1.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKrilgnAKRKQIQEfcNEAQIMTVLQHENIVAFY-GFASLEEPIMVvMEL 257
Cdd:cd14104   6 EELGRGQFGIVHRCVETSSKKTYMAKFVKVK-----GADQVLVK--KEISILNIARHRNILRLHeSFESHEELVMI-FEF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTQ-NIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARN--CLVTQDLKAKISDFGLSLQGTEVTTKNL 334
Cdd:cd14104  78 ISGVDIFERITTARfELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENiiYCTRRGSYIKIIEFGQSRQLKPGDKFRL 157
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17542550 335 EKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd14104 158 QYTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLS 193
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
179-429 1.43e-10

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


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 62.72  E-value: 1.43e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQiqefcNEAQ-IMT---VL----QHENIVAF-YGFASLEE 249
Cdd:cd05575   1 KVIGKGSFGKVLLARHKAEGKL-----YAVKVLQKKAILKR-----NEVKhIMAernVLlknvKHPFLVGLhYSFQTKDK 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 250 pIMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEV 329
Cdd:cd05575  71 -LYFVLDYVNGGELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEP 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 330 --TTKNLEKAPiRWLAPESLKSGMFNEKTDVWSYGVFLTELMarCEHDPLYPKSLKDAKAWILteERPHKMENGDPKELM 407
Cdd:cd05575 150 sdTTSTFCGTP-EYLAPEVLRKQPYDRTVDWWCLGAVLYEML--YGLPPFYSRDTAEMYDNIL--HKPLRLRTNVSPSAR 224
                       250       260
                ....*....|....*....|....*.
gi 17542550 408 VLIDACCERNPNERL----NFNTVKR 429
Cdd:cd05575 225 DLLEGLLQKDRTKRLgsgnDFLEIKN 250
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
179-364 1.63e-10

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: 61.83  E-value: 1.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFY-GFASLEEPIMvVMEL 257
Cdd:cd14114   8 EELGTGAFGVVHRCTERATGN------NFAAKFIMTPHESDKETVRKEIQIMNQLHHPKLINLHdAFEDDNEMVL-ILEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTTQN-IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARN--CLVTQDLKAKISDFGLSL-----QGTEV 329
Cdd:cd14114  81 LSGGELFERIAAEHYkMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENimCTTKRSNEVKLIDFGLAThldpkESVKV 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 17542550 330 TTKNLEKApirwlAPESLKSGMFNEKTDVWSYGVF 364
Cdd:cd14114 161 TTGTAEFA-----APEIVEREPVGFYTDMWAVGVL 190
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
179-372 2.03e-10

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: 61.98  E-value: 2.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVgstnppiEVAVKRILGNAKRKQIQEfcNEAQIMTVLQHENIVAFY-----GFASLEEpIMV 253
Cdd:cd14220   1 RQIGKGRYGEVWMGKWRGE-------KVAVKVFFTTEEASWFRE--TEIYQTVLMRHENILGFIaadikGTGSWTQ-LYL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTqNIPKLQILWFAMNVASGMRHLSSK--------GIIHRDLAARNCLVTQDLKAKISDFGLSLQ 325
Cdd:cd14220  71 ITDYHENGSLYDFLKCT-TLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGTCCIADLGLAVK 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17542550 326 GTEVTTK-----NLEKAPIRWLAP----ESLKSGMFNE--KTDVWSYGVFLTELMARC 372
Cdd:cd14220 150 FNSDTNEvdvplNTRVGTKRYMAPevldESLNKNHFQAyiMADIYSFGLIIWEMARRC 207
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
184-372 2.05e-10

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: 61.98  E-value: 2.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 184 GAFGEVFKGQYkavgsTNPPIEVAVKRIlgnakrKQIQEFCNEAQIMTV--LQHENIVAFYGFASLEEPIMVVMELVTG- 260
Cdd:cd14141   6 GRFGCVWKAQL-----LNEYVAVKIFPI------QDKLSWQNEYEIYSLpgMKHENILQFIGAEKRGTNLDVDLWLITAf 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 ---GDLRKYLQTTQnIPKLQILWFAMNVASGMRHLSSK----------GIIHRDLAARNCLVTQDLKAKISDFGLSLQ-- 325
Cdd:cd14141  75 hekGSLTDYLKANV-VSWNELCHIAQTMARGLAYLHEDipglkdghkpAIAHRDIKSKNVLLKNNLTACIADFGLALKfe 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17542550 326 -GTEVTTKNLEKAPIRWLAPESLKSGM-FNE----KTDVWSYGVFLTELMARC 372
Cdd:cd14141 154 aGKSAGDTHGQVGTRRYMAPEVLEGAInFQRdaflRIDMYAMGLVLWELASRC 206
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
184-434 2.30e-10

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: 61.58  E-value: 2.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 184 GAFGEVFKGQYkavgsTNPPIEVAVKRIlgnakrKQIQEFCNEAQIMTV--LQHENIVAFYGF----ASLEEPIMVVMEL 257
Cdd:cd14140   6 GRFGCVWKAQL-----MNEYVAVKIFPI------QDKQSWQSEREIFSTpgMKHENLLQFIAAekrgSNLEMELWLITAF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VTGGDLRKYLQTtqNIpklqILW-----FAMNVASGMRHLS-----SKG------IIHRDLAARNCLVTQDLKAKISDFG 321
Cdd:cd14140  75 HDKGSLTDYLKG--NI----VSWnelchIAETMARGLSYLHedvprCKGeghkpaIAHRDFKSKNVLLKNDLTAVLADFG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 322 LSLQ---GTEVTTKNLEKAPIRWLAPESLKSGM-FNE----KTDVWSYGVFLTELMARCE------HDPLYP-------- 379
Cdd:cd14140 149 LAVRfepGKPPGDTHGQVGTRRYMAPEVLEGAInFQRdsflRIDMYAMGLVLWELVSRCKaadgpvDEYMLPfeeeigqh 228
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 380 KSLKDAKAWILTEE-RP----HKMENGDPKELMVLIDACCERNPNERLNFNTVKRQITDI 434
Cdd:cd14140 229 PSLEDLQEVVVHKKmRPvfkdHWLKHPGLAQLCVTIEECWDHDAEARLSAGCVEERISQI 288
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
181-422 2.36e-10

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: 61.99  E-value: 2.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTNPPIEVAVKRIlgnaKRKQIQEFCNEAQIMTVLQHENIVAF-----YGFASLEEpIMVVM 255
Cdd:cd14223   8 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRI----KMKQGETLALNERIMLSLVSTGDCPFivcmsYAFHTPDK-LSFIL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEvTTKNLE 335
Cdd:cd14223  83 DLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSK-KKPHAS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 336 KAPIRWLAPESLKSGM-FNEKTDVWSYGVFLTELMArcEHDPLYPKSLKDAKAW-ILTEERPHKMENGDPKELMVLIDAC 413
Cdd:cd14223 162 VGTHGYMAPEVLQKGVaYDSSADWFSLGCMLFKLLR--GHSPFRQHKTKDKHEIdRMTLTMAVELPDSFSPELRSLLEGL 239

                ....*....
gi 17542550 414 CERNPNERL 422
Cdd:cd14223 240 LQRDVNRRL 248
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
172-422 2.50e-10

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: 62.00  E-value: 2.50e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 172 HSTIN---LDKKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRIlgnaKRKQIQEFCNEAQIMTVLQHENIVAF-----YG 243
Cdd:cd05633   1 HLTMNdfsVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRI----KMKQGETLALNERIMLSLVSTGDCPFivcmtYA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 244 FASLEEpIMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS 323
Cdd:cd05633  77 FHTPDK-LCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 324 LQGTEvTTKNLEKAPIRWLAPESLKSGM-FNEKTDVWSYGVFLTELMArcEHDPLYPKSLKDAK-----AWILTEERPHK 397
Cdd:cd05633 156 CDFSK-KKPHASVGTHGYMAPEVLQKGTaYDSSADWFSLGCMLFKLLR--GHSPFRQHKTKDKHeidrmTLTVNVELPDS 232
                       250       260
                ....*....|....*....|....*
gi 17542550 398 MEngdpKELMVLIDACCERNPNERL 422
Cdd:cd05633 233 FS----PELKSLLEGLLQRDVSKRL 253
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
181-425 2.67e-10

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: 61.62  E-value: 2.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQEFCNEAQIMtVLQHE--NIVAFYGFASLEEPIMVVMELV 258
Cdd:cd06618  23 IGSGTCGQVYKMRHKKTGHV-----MAVKQMRRSGNKEENKRILMDLDVV-LKSHDcpYIVKCYGYFITDSDVFICMELM 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 tGGDLRKYLQTTQN-IPKLQILWFAMNVASGMRHLSSK-GIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLEK 336
Cdd:cd06618  97 -STCLDKLLKRIQGpIPEDILGKMTVSIVKALHYLKEKhGVIHRDVKPSNILLDESGNVKLCDFGISGRLVDSKAKTRSA 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 337 APIRWLAPESL---KSGMFNEKTDVWSYGVFLTELMArcehdPLYPKSLKDAKAWILT---EERPHKMENGDPKELMV-- 408
Cdd:cd06618 176 GCAAYMAPERIdppDNPKYDIRADVWSLGISLVELAT-----GQFPYRNCKTEFEVLTkilNEEPPSLPPNEGFSPDFcs 250
                       250
                ....*....|....*..
gi 17542550 409 LIDACCERNPNERLNFN 425
Cdd:cd06618 251 FVDLCLTKDHRYRPKYR 267
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
176-371 2.89e-10

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: 61.56  E-value: 2.89e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 176 NLDKKLGCGAFGEVFKGQYKAVGStnppiEVAVKRILGNAKRK--QIQEFcNEAQIMTVLQHENIVA----FYGFASLEE 249
Cdd:cd07866  11 EILGKLGEGTFGEVYKARQIKTGR-----VVALKKILMHNEKDgfPITAL-REIKILKKLKHPNVVPlidmAVERPDKSK 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 250 PIMVVMELVT---GGDLRKYLQTTQ-NIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS-- 323
Cdd:cd07866  85 RKRGSVYMVTpymDHDLSGLLENPSvKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLArp 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17542550 324 ---------LQGTEVTTKNLEKAPIRWLAPESLKSGMFNEKT--DVWSYGVFLTELMAR 371
Cdd:cd07866 165 ydgpppnpkGGGGGGTRKYTNLVVTRWYRPPELLLGERRYTTavDIWGIGCVFAEMFTR 223
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
179-369 3.09e-10

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 61.63  E-value: 3.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd07869  11 EKLGEGSYATVYKGKSKVNGKL-----VALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEYV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGgDLRKYL-QTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLEKA 337
Cdd:cd07869  86 HT-DLCQYMdKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTYSNEV 164
                       170       180       190
                ....*....|....*....|....*....|....
gi 17542550 338 PIRWLAPES--LKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd07869 165 VTLWYRPPDvlLGSTEYSTCLDMWGVGCIFVEMI 198
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
180-378 3.69e-10

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: 61.20  E-value: 3.69e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGSTNppieVAVKRILGNAKRK-----QIQEFCNEAQIMTvLQHENIVAFYGFASL-----EE 249
Cdd:cd07862   8 EIGEGAYGKVFKARDLKNGGRF----VALKRVRVQTGEEgmplsTIREVAVLRHLET-FEHPNVVRLFDVCTVsrtdrET 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 250 PIMVVMELVTGgDLRKYLQTTQN--IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGT 327
Cdd:cd07862  83 KLTLVFEHVDQ-DLTTYLDKVPEpgVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIYS 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17542550 328 EVTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARcehDPLY 378
Cdd:cd07862 162 FQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRR---KPLF 209
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
181-378 4.34e-10

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


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 60.89  E-value: 4.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGStnppiEVAVKRI---LGNAKRKQIqefcNEAQIMTVLQ-HENIVAFYGFASLEEPIMVVME 256
Cdd:cd14090  10 LGEGAYASVQTCINLYTGK-----EYAVKIIekhPGHSRSRVF----REVETLHQCQgHPNILQLIEYFEDDERFYLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLK---AKISDFGL-------SLQG 326
Cdd:cd14090  81 KMRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKvspVKICDFDLgsgiklsSTSM 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 327 TEVTTKNLEkAPI---RWLAPE-----SLKSGMFNEKTDVWSYGVFLTELMarCEHDPLY 378
Cdd:cd14090 161 TPVTTPELL-TPVgsaEYMAPEvvdafVGEALSYDKRCDLWSLGVILYIML--CGYPPFY 217
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
181-369 4.63e-10

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


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 60.36  E-value: 4.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGStnppiEVAVKRIlgNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd14115   1 IGRGRFSIVKKCLHKATRK-----DVAVKFV--SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDL---KAKISDFGLSLQGTEVTTKNLEKA 337
Cdd:cd14115  74 GRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDAVQISGHRHVHHLLG 153
                       170       180       190
                ....*....|....*....|....*....|..
gi 17542550 338 PIRWLAPESLKSGMFNEKTDVWSYGVfLTELM 369
Cdd:cd14115 154 NPEFAAPEVIQGTPVSLATDIWSIGV-LTYVM 184
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
180-378 5.64e-10

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


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 60.36  E-value: 5.64e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFK------GQYKAVGSTNPPIE---VAVKRILGNAKRKQIQEFcneaqimtvlQHENIVAFYGF-ASL-- 247
Cdd:cd07863   7 EIGVGAYGTVYKardphsGHFVALKSVRVQTNedgLPLSTVREVALLKRLEAF----------DHPNIVRLMDVcATSrt 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 248 --EEPIMVVMELVTGgDLRKYLQTTQ--NIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS 323
Cdd:cd07863  77 drETKVTLVFEHVDQ-DLRTYLDKVPppGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLA 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17542550 324 lqgtEVTTKNLEKAPI---RWL-APESLKSGMFNEKTDVWSYGVFLTELMARcehDPLY 378
Cdd:cd07863 156 ----RIYSCQMALTPVvvtLWYrAPEVLLQSTYATPVDMWSVGCIFAEMFRR---KPLF 207
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
178-370 5.84e-10

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


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 60.43  E-value: 5.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 178 DKKLGCGAFGEVfkgqyKAVGSTNPPIEVAVKRILGNAKRKQIQEFcneAQIMTVLQ---HENIVAFYGFASLEEPIMVV 254
Cdd:cd14174   7 DELLGEGAYAKV-----QGCVSLQNGKEYAVKIIEKNAGHSRSRVF---REVETLYQcqgNKNILELIEFFEDDTRFYLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLK---AKISDF----GLSLQG- 326
Cdd:cd14174  79 FEKLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKvspVKICDFdlgsGVKLNSa 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17542550 327 -TEVTTKNLEK--APIRWLAPESL-----KSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd14174 159 cTPITTPELTTpcGSAEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLS 210
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
184-424 6.93e-10

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: 60.32  E-value: 6.93e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 184 GAFGEVFKGQYkavgsTNPPIEVAVKRI-----LGNAKRKQIqefCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd14026   8 GAFGTVSRARH-----ADWRVTVAIKCLkldspVGDSERNCL---LKEAEILHKARFSYILPILGICNEPEFLGIVTEYM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQNIP------KLQILWfamNVASGMRHLS--SKGIIHRDLAARNCLVTQDLKAKISDFGL------SL 324
Cdd:cd14026  80 TNGSLNELLHEKDIYPdvawplRLRILY---EIALGVNYLHnmSPPLLHHDLKTQNILLDGEFHVKIADFGLskwrqlSI 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 325 QGTEVTTKNLEKAPIRWLAPESLKSGMFNE---KTDVWSYGVFLTELMARCE--HDPLYPKSLKDAkawILTEERPHKME 399
Cdd:cd14026 157 SQSRSSKSAPEGGTIIYMPPEEYEPSQKRRasvKHDIYSYAIIMWEVLSRKIpfEEVTNPLQIMYS---VSQGHRPDTGE 233
                       250       260       270
                ....*....|....*....|....*....|.
gi 17542550 400 NGDP-----KELMV-LIDACCERNPNERLNF 424
Cdd:cd14026 234 DSLPvdiphRATLInLIESGWAQNPDERPSF 264
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
171-372 7.12e-10

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: 60.45  E-value: 7.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 171 IHSTINLDKKLGCGAFGEVFKGQYKAVgstnppiEVAVKRILGNAKRKQIQEfcNEAQIMTVLQHENIVAFY-----GFA 245
Cdd:cd14219   3 IAKQIQMVKQIGKGRYGEVWMGKWRGE-------KVAVKVFFTTEEASWFRE--TEIYQTVLMRHENILGFIaadikGTG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 246 SLEEpIMVVMELVTGGDLRKYLQTTqNIPKLQILWFAMNVASGMRHLSSK--------GIIHRDLAARNCLVTQDLKAKI 317
Cdd:cd14219  74 SWTQ-LYLITDYHENGSLYDYLKST-TLDTKAMLKLAYSSVSGLCHLHTEifstqgkpAIAHRDLKSKNILVKKNGTCCI 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17542550 318 SDFGLSLQGTEVTTK-----NLEKAPIRWLAP----ESLKSGMFNE--KTDVWSYGVFLTELMARC 372
Cdd:cd14219 152 ADLGLAVKFISDTNEvdippNTRVGTKRYMPPevldESLNRNHFQSyiMADMYSFGLILWEVARRC 217
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
179-421 7.16e-10

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 62.06  E-value: 7.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550   179 KKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRIlgnaKRKQIQEFCNEAQIMTVLQHENIVAFYG--FASLEEPIMVVME 256
Cdd:PTZ00266   19 KKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGL----KEREKSQLVIEVNVMRELKHKNIVRYIDrfLNKANQKLYILME 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550   257 LVTGGDLRKYLQTTQNI--------------PKLQILWFAMNVASGMrhlSSKGIIHRDLAARNCLVTQDLK-------- 314
Cdd:PTZ00266   95 FCDAGDLSRNIQKCYKMfgkieehaivditrQLLHALAYCHNLKDGP---NGERVLHRDLKPQNIFLSTGIRhigkitaq 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550   315 ---------AKISDFGLSLQ-GTEVTTKNLEKAPIRWlAPESL--KSGMFNEKTDVWSYGVFLTELmarCEHDPLYPKSL 382
Cdd:PTZ00266  172 annlngrpiAKIGDFGLSKNiGIESMAHSCVGTPYYW-SPELLlhETKSYDDKSDMWALGCIIYEL---CSGKTPFHKAN 247
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 17542550   383 KDAKAWILTEERPHKMENGDPKELMVLIDACCERNPNER 421
Cdd:PTZ00266  248 NFSQLISELKRGPDLPIKGKSKELNILIKNLLNLSAKER 286
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
172-369 7.27e-10

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


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 60.46  E-value: 7.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 172 HSTIN----LDKKLGCGAFGEVFKG------QYKAVgstnpPIEVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAF 241
Cdd:cd14040   1 HPTLNerylLLHLLGRGGFSEVYKAfdlyeqRYAAV-----KIHQLNKSWRDEKKENYHKHACREYRIHKELDHPRIVKL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 242 YGFASLE-EPIMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSS--KGIIHRDLAARNCLVTQDL---KA 315
Cdd:cd14040  76 YDYFSLDtDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLVDGTacgEI 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17542550 316 KISDFGLS---------LQGTEVTTKNlekAPIRW-LAPESLKSG----MFNEKTDVWSYGVFLTELM 369
Cdd:cd14040 156 KITDFGLSkimdddsygVDGMDLTSQG---AGTYWyLPPECFVVGkeppKISNKVDVWSVGVIFFQCL 220
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
179-382 8.36e-10

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


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 60.47  E-value: 8.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKRI--LGNAKRKQIQEFCNEAQIMTVLQHENIVA-FYGFASlEEPIMVVM 255
Cdd:cd05596  32 KVIGRGAFGEVQLVRHKSTKKV-----YAMKLLskFEMIKRSDSAFFWEERDIMAHANSEWIVQlHYAFQD-DKYLYMVM 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRKyLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ---------G 326
Cdd:cd05596 106 DYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCMKmdkdglvrsD 184
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 327 TEVTTKNlekapirWLAPESLKS----GMFNEKTDVWSYGVFLTELMarCEHDPLYPKSL 382
Cdd:cd05596 185 TAVGTPD-------YISPEVLKSqggdGVYGRECDWWSVGVFLYEML--VGDTPFYADSL 235
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
181-378 8.40e-10

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


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 59.62  E-value: 8.40e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGStnppiEVAVKRILGNAKRKQIQEFCNEA----QIMTVLQ-HENIvaFYGfaslEEPIMVVM 255
Cdd:cd14172  12 LGLGVNGKVLECFHRRTGQ-----KCALKLLYDSPKARREVEHHWRAsggpHIVHILDvYENM--HHG----KRCLLIIM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRKYLQT--TQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVT---QDLKAKISDFGLSlqgTEVT 330
Cdd:cd14172  81 ECMEGGELFSRIQErgDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTskeKDAVLKLTDFGFA---KETT 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17542550 331 TKNLEKAPIR---WLAPESLKSGMFNEKTDVWSYGVFLTELMarCEHDPLY 378
Cdd:cd14172 158 VQNALQTPCYtpyYVAPEVLGPEKYDKSCDMWSLGVIMYILL--CGFPPFY 206
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
177-370 8.64e-10

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: 60.03  E-value: 8.64e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKLGCGAFGEVFKGQYKAVGStnppiEVAVKrILGNAKRKQIQEFcneAQIMTVLQHENIVAFYGFASLEEPIMVVME 256
Cdd:cd14178   7 IKEDIGIGSYSVCKRCVHKATST-----EYAVK-IIDKSKRDPSEEI---EILLRYGQHPNIITLKDVYDDGKFVYLVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDL----KAKISDFGLSLQ------- 325
Cdd:cd14178  78 LMRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESgnpeSIRICDFGFAKQlraengl 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17542550 326 -GTEVTTKNlekapirWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd14178 158 lMTPCYTAN-------FVAPEVLKRQGYDAACDIWSLGILLYTMLA 196
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
205-370 1.00e-09

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: 59.60  E-value: 1.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 205 EVAVKRILGNAKR---KQIQEF----CNEAQIMT-VLQHENIVAFYGFASLEEPIMVVMELVTGGDLRKYLQTTQNIPKL 276
Cdd:cd14181  37 EFAVKIIEVTAERlspEQLEEVrsstLKEIHILRqVSGHPSIITLIDSYESSTFIFLVFDLMRRGELFDYLTEKVTLSEK 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 277 QILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQ-GTEVTTKNLEKAPiRWLAPESLKSGM---- 351
Cdd:cd14181 117 ETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHlEPGEKLRELCGTP-GYLAPEILKCSMdeth 195
                       170       180
                ....*....|....*....|.
gi 17542550 352 --FNEKTDVWSYGVFLTELMA 370
Cdd:cd14181 196 pgYGKEVDLWACGVILFTLLA 216
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
180-379 1.23e-09

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: 59.69  E-value: 1.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQ-EFCNEAQIMTVLQHENIVAFYGFA---SLEEpIMVVM 255
Cdd:cd07845  14 RIGEGTYGIVYRARDTTSGEI-----VALKKVRMDNERDGIPiSSLREITLLLNLRHPNIVELKEVVvgkHLDS-IFLVM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGgDLRKYLQTTQN-IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNL 334
Cdd:cd07845  88 EYCEQ-DLASLLDNMPTpFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTYGLPAKPMT 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17542550 335 EKAPIRWL-APESLkSGMFNEKT--DVWSYGVFLTELMArceHDPLYP 379
Cdd:cd07845 167 PKVVTLWYrAPELL-LGCTTYTTaiDMWAVGCILAELLA---HKPLLP 210
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
216-380 1.44e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 60.01  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  216 KRKQIQEFCNEAQIMTVLQHENIVAFYG-FASLEEPIMVVMELVTggDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSS 294
Cdd:PHA03212 123 KAGQRGGTATEAHILRAINHPSIIQLKGtFTYNKFTCLILPRYKT--DLYCYLAAKRNIAICDILAIERSVLRAIQYLHE 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  295 KGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLE--KAPIRWLAPESLKSGMFNEKTDVWSYGVFLTElMARC 372
Cdd:PHA03212 201 NRIIHRDIKAENIFINHPGDVCLGDFGAACFPVDINANKYYgwAGTIATNAPELLARDPYGPAVDIWSAGIVLFE-MATC 279

                 ....*...
gi 17542550  373 eHDPLYPK 380
Cdd:PHA03212 280 -HDSLFEK 286
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
172-369 1.60e-09

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: 59.30  E-value: 1.60e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 172 HSTIN----LDKKLGCGAFGEVfkgqYKAVGSTNPP-IEVAVKRILGNAKRKQIQEF----CNEAQIMTVLQHENIVAFY 242
Cdd:cd14041   1 HPTLNdrylLLHLLGRGGFSEV----YKAFDLTEQRyVAVKIHQLNKNWRDEKKENYhkhaCREYRIHKELDHPRIVKLY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 243 GFASLE-EPIMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSS--KGIIHRDLAARNCLVTQDL---KAK 316
Cdd:cd14041  77 DYFSLDtDSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEikPPIIHYDLKPGNILLVNGTacgEIK 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17542550 317 ISDFGLS----------LQGTEVTTKNlekAPIRW-LAPESLKSG----MFNEKTDVWSYGVFLTELM 369
Cdd:cd14041 157 ITDFGLSkimdddsynsVDGMELTSQG---AGTYWyLPPECFVVGkeppKISNKVDVWSVGVIFYQCL 221
SH2 cd00173
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ...
72-151 1.76e-09

Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they bind pTyr-containing polypeptide ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. They are present in a wide array of proteins including: adaptor proteins (Nck1, Crk, Grb2), scaffolds (Slp76, Shc, Dapp1), kinases (Src, Syk, Fps, Tec), phosphatases (Shp-1, Shp-2), transcription factors (STAT1), Ras signaling molecules (Ras-Gap), ubiquitination factors (c-Cbl), cytoskeleton regulators (Tensin), signal regulators (SAP), and phospholipid second messengers (PLCgamma), amongst others.


Pssm-ID: 198173 [Multi-domain]  Cd Length: 79  Bit Score: 54.38  E-value: 1.76e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  72 YHGVLFGSEAEKLLT--WDRAYLVRRAITKPNKFlCISVNWK-KKIFHYQLDFNEDGWCCKKLyekfptmPNRRFLHIRQ 148
Cdd:cd00173   3 FHGSISREEAERLLRgkPDGTFLVRESSSEPGDY-VLSVRSGdGKVKHYLIERNEGGYYLLGG-------SGRTFPSLPE 74

                ...
gi 17542550 149 LLE 151
Cdd:cd00173  75 LVE 77
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
179-379 2.01e-09

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


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 59.10  E-value: 2.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFK------GQYkavgstnppieVAVKrILGNAKRKQIQEfCNEAQIMTVLQH------ENIVAFYGFAS 246
Cdd:cd14210  19 SVLGKGSFGQVVKcldhktGQL-----------VAIK-IIRNKKRFHQQA-LVEVKILKHLNDndpddkHNIVRYKDSFI 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 247 LEEPIMVVMELVtGGDLRKYLQTT--QNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKA--KISDFGL 322
Cdd:cd14210  86 FRGHLCIVFELL-SINLYELLKSNnfQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKSsiKVIDFGS 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17542550 323 SLQGTEVTTKNLEKAPIRwlAPESLKSGMFNEKTDVWSYGVFLTELMArceHDPLYP 379
Cdd:cd14210 165 SCFEGEKVYTYIQSRFYR--APEVILGLPYDTAIDMWSLGCILAELYT---GYPLFP 216
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
179-362 2.45e-09

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: 58.96  E-value: 2.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFkgQYKAVGSTNPPIEVAVKrILGNAK----RKQIQEFCNEAQIMTVLQHENIVAF-YGFASlEEPIMV 253
Cdd:cd05584   2 KVLGKGGYGKVF--QVRKTTGSDKGKIFAMK-VLKKASivrnQKDTAHTKAERNILEAVKHPFIVDLhYAFQT-GGKLYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGL---SLQGTEVT 330
Cdd:cd05584  78 ILEYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLckeSIHDGTVT 157
                       170       180       190
                ....*....|....*....|....*....|..
gi 17542550 331 tkNLEKAPIRWLAPESLKSGMFNEKTDVWSYG 362
Cdd:cd05584 158 --HTFCGTIEYMAPEILTRSGHGKAVDWWSLG 187
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
181-370 3.17e-09

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


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 58.34  E-value: 3.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGStnppiEVAVKRIlgnAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTG 260
Cdd:cd14180  14 LGEGSFSVCRKCRHRQSGQ-----EYAVKII---SRRMEANTQREVAALRLCQSHPNIVALHEVLHDQYHTYLVMELLRG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 261 GDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKA---KISDFG---LSLQGTEVTtknl 334
Cdd:cd14180  86 GELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDGavlKVIDFGfarLRPQGSRPL---- 161
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 17542550 335 eKAP---IRWLAPESLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd14180 162 -QTPcftLQYAAPELFSNQGYDESCDLWSLGVILYTMLS 199
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
235-370 3.23e-09

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


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 58.11  E-value: 3.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 235 HENIVAFYGFASLEEPIMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLV---TQ 311
Cdd:cd14173  59 HRNVLELIEFFEEEDKFYLVFEKMRGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCehpNQ 138
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17542550 312 DLKAKISDF----GLSLQG--TEVTTKNLEK--APIRWLAPE-----SLKSGMFNEKTDVWSYGVFLTELMA 370
Cdd:cd14173 139 VSPVKICDFdlgsGIKLNSdcSPISTPELLTpcGSAEYMAPEvveafNEEASIYDKRCDLWSLGVILYIMLS 210
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
242-425 3.39e-09

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: 58.35  E-value: 3.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 242 YGFASlEEPIMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFG 321
Cdd:cd05585  61 FSFQS-PEKLYLVLAFINGGELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFG 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 322 L-SLQGTEVTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTELMARCEhdPLYPKSLKDAKAWILTEerPHKMEN 400
Cdd:cd05585 140 LcKLNMKDDDKTNTFCGTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLP--PFYDENTNEMYRKILQE--PLRFPD 215
                       170       180
                ....*....|....*....|....*
gi 17542550 401 GDPKELMVLIDACCERNPNERLNFN 425
Cdd:cd05585 216 GFDRDAKDLLIGLLNRDPTKRLGYN 240
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
176-363 3.57e-09

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 57.60  E-value: 3.57e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 176 NLDKKLGCGAFGEVFKGQYKAVGstnppIEVAVKRILGNAKRKQIQEfcNEAQIMTVLQHENIVAFYGFASLEEPIMVVM 255
Cdd:cd14108   5 DIHKEIGRGAFSYLRRVKEKSSD-----LSFAAKFIPVRAKKKTSAR--RELALLAELDHKSIVRFHDAFEKRRVVIIVT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRKYLQTTqNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLV--TQDLKAKISDFGLSLQGTEVTTKN 333
Cdd:cd14108  78 ELCHEELLERITKRP-TVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMadQKTDQVRICDFGNAQELTPNEPQY 156
                       170       180       190
                ....*....|....*....|....*....|
gi 17542550 334 LEKAPIRWLAPESLKSGMFNEKTDVWSYGV 363
Cdd:cd14108 157 CKYGTPEFVAPEIVNQSPVSKVTDIWPVGV 186
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
172-381 3.89e-09

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


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 57.59  E-value: 3.89e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 172 HSTINLDKKLGCGAFGEVFKGQYKAVGstnppIEVAVKRI-LGNAKRKQIQEfcnEAQIMTVLQHENIVAFYGFASLEEP 250
Cdd:cd14107   1 HSVYEVKEEIGRGTFGFVKRVTHKGNG-----ECCAAKFIpLRSSTRARAFQ---ERDILARLSHRRLTCLLDQFETRKT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVT----QDLKakISDFGLSLQG 326
Cdd:cd14107  73 LILILELCSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVsptrEDIK--ICDFGFAQEI 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17542550 327 TEVTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGVfLTELMARCeHDPLYPKS 381
Cdd:cd14107 151 TPSEHQFSKYGSPEFVAPEIVHQEPVSAATDIWALGV-IAYLSLTC-HSPFAGEN 203
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
181-422 4.45e-09

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: 57.83  E-value: 4.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTNPPIEVAVKRIlgnaKRKQIQEFCNEAQIMTVLQHEN-----IVAF-YGFASLEEpIMVV 254
Cdd:cd05606   2 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRI----KMKQGETLALNERIMLSLVSTGgdcpfIVCMtYAFQTPDK-LCFI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQgtevTTKNL 334
Cdd:cd05606  77 LDLMNGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACD----FSKKK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 335 EKAPI---RWLAPESLKSGM-FNEKTDVWSYGVFLTELMArcEHDPLYPKSLKDaKAWI--LTEERPHKMENGDPKELMV 408
Cdd:cd05606 153 PHASVgthGYMAPEVLQKGVaYDSSADWFSLGCMLYKLLK--GHSPFRQHKTKD-KHEIdrMTLTMNVELPDSFSPELKS 229
                       250
                ....*....|....
gi 17542550 409 LIDACCERNPNERL 422
Cdd:cd05606 230 LLEGLLQRDVSKRL 243
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
176-391 5.31e-09

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


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 57.30  E-value: 5.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 176 NLDKKLGCGAFGEVFKGQYKAVGSTnppieVAVKRI-LGNAKRKQIQ-EFCNEAQimtvLQHENIVAFYGFASLEEPIMV 253
Cdd:cd14665   3 ELVKDIGSGNFGVARLMRDKQTKEL-----VAVKYIeRGEKIDENVQrEIINHRS----LRHPNIVRFKEVILTPTHLAI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLV--TQDLKAKISDFGLSLQGTEVTT 331
Cdd:cd14665  74 VMEYAAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLdgSPAPRLKICDFGYSKSSVLHSQ 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17542550 332 KNLEKAPIRWLAPESLKSGMFNEK-TDVWSYGVFLTELM--ARCEHDPLYPKSLKDAKAWILT 391
Cdd:cd14665 154 PKSTVGTPAYIAPEVLLKKEYDGKiADVWSCGVTLYVMLvgAYPFEDPEEPRNFRKTIQRILS 216
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
180-379 5.36e-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: 57.38  E-value: 5.36e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQEFC-NEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd07847   8 KIGEGSYGVVFKCRNRETGQI-----VAIKKFVESEDDPVIKKIAlREIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEYC 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFG----LSLQGTEVTtknl 334
Cdd:cd07847  83 DHTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGfariLTGPGDDYT---- 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 17542550 335 EKAPIRWL-APESLKSGM-FNEKTDVWSYGVFLTELMARCehdPLYP 379
Cdd:cd07847 159 DYVATRWYrAPELLVGDTqYGPPVDVWAIGCVFAELLTGQ---PLWP 202
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
181-369 7.52e-09

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 58.12  E-value: 7.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  181 LGCGAFGEVfkgqYKAVgSTNPPIEVAVKRILGNAKRKQiqefcNEAQIMTVLQHENIV---AFY---GFASLEEPIM-- 252
Cdd:PTZ00036  74 IGNGSFGVV----YEAI-CIDTSEKVAIKKVLQDPQYKN-----RELLIMKNLNHINIIflkDYYyteCFKKNEKNIFln 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  253 VVMELV---TGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLV---TQDLkaKISDFGlslqg 326
Cdd:PTZ00036 144 VVMEFIpqtVHKYMKHYARNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIdpnTHTL--KLCDFG----- 216
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17542550  327 tevTTKNL--EKAPIRWL------APE-SLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:PTZ00036 217 ---SAKNLlaGQRSVSYIcsrfyrAPElMLGATNYTTHIDLWSLGCIIAEMI 265
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
179-379 8.06e-09

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 57.15  E-value: 8.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKRilgnaKRKQIQE------FCNEAQIMTVLQHEN-IVAFYGFASLEEPI 251
Cdd:cd07837   7 EKIGEGTYGKVYKARDKNTGKL-----VALKK-----TRLEMEEegvpstALREVSLLQMLSQSIyIVRLLDVEHVEENG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 252 MVVMELV---TGGDLRKYLQTTQN-----IPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKA-KISDFGL 322
Cdd:cd07837  77 KPLLYLVfeyLDTDLKKFIDSYGRgphnpLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLlKIADLGL 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17542550 323 SLQGT-EVTTKNLEKAPIRWLAPES-LKSGMFNEKTDVWSYGVFLTELMARcehDPLYP 379
Cdd:cd07837 157 GRAFTiPIKSYTHEIVTLWYRAPEVlLGSTHYSTPVDMWSVGCIFAEMSRK---QPLFP 212
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
177-390 8.13e-09

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 56.75  E-value: 8.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 177 LDKKlGCGAFGEVFKGQYKAVGSTNPpievaVKRILGNAKRKQ--IQEFcneaQIMTVLQHENIVAFYGFASLEEPIMVV 254
Cdd:cd14111   8 LDEK-ARGRFGVIRRCRENATGKNFP-----AKIVPYQAEEKQgvLQEY----EILKSLHHERIMALHEAYITPRYLVLI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFG-------LSLQGT 327
Cdd:cd14111  78 AEFCSGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGsaqsfnpLSLRQL 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17542550 328 EVTTKNLEkapirWLAPESLKSGMFNEKTDVWSYGVfLTELMARCEHdPLYPKSLKDAKAWIL 390
Cdd:cd14111 158 GRRTGTLE-----YMAPEMVKGEPVGPPADIWSIGV-LTYIMLSGRS-PFEDQDPQETEAKIL 213
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
191-379 9.07e-09

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 57.10  E-value: 9.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 191 KGQYKAVGS---TNPPIEVAVKRI------LGNAKRkqiqeFCNEAQIMTVLQHENIVAFYGFASLEEP-----IMVVME 256
Cdd:cd07859  10 KGSYGVVCSaidTHTGEKVAIKKIndvfehVSDATR-----ILREIKLLRLLRHPDIVEIKHIMLPPSRrefkdIYVVFE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVtGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGL---SLQGTEVTTKN 333
Cdd:cd07859  85 LM-ESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLarvAFNDTPTAIFW 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17542550 334 LEKAPIRWL-APEsLKSGMFNEKT---DVWSYGVFLTELMArceHDPLYP 379
Cdd:cd07859 164 TDYVATRWYrAPE-LCGSFFSKYTpaiDIWSIGCIFAEVLT---GKPLFP 209
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
173-381 1.08e-08

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 56.62  E-value: 1.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 173 STINLDKkLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIM 252
Cdd:cd07844   1 TYKKLDK-LGEGSYATVYKGRSKLTGQL-----VALKEIRLEHEEGAPFTAIREASLLKDLKHANIVTLHDIIHTKKTLT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 253 VVMELVTGgDLRKYLQTTQNIPKLQ-ILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSlQGTEVTT 331
Cdd:cd07844  75 LVFEYLDT-DLKQYMDDCGGGLSMHnVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLA-RAKSVPS 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17542550 332 KNLEKAPIR-WLAPES--LKSGMFNEKTDVWSYGVFLTELMArceHDPLYPKS 381
Cdd:cd07844 153 KTYSNEVVTlWYRPPDvlLGSTEYSTSLDMWGVGCIFYEMAT---GRPLFPGS 202
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
179-379 1.09e-08

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: 56.80  E-value: 1.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKRI---LGNAKRKQ--------IQEFCNeaqimtvlqHENIVafygfasl 247
Cdd:cd07852  13 KKLGKGAYGIVWKAIDKKTGEV-----VALKKIfdaFRNATDAQrtfreimfLQELND---------HPNII-------- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 248 eePIMVVMELVTGGDLR---KYLQTT----------QNIPKLQILWFAMNVasgMRHLSSKGIIHRDLAARNCLVTQDLK 314
Cdd:cd07852  71 --KLLNVIRAENDKDIYlvfEYMETDlhaviranilEDIHKQYIMYQLLKA---LKYLHSGGVIHRDLKPSNILLNSDCR 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17542550 315 AKISDFGL--SLQGTEVTTKNlekaPI-------RWL-APESL-KSGMFNEKTDVWSYGVFLTELMARcehDPLYP 379
Cdd:cd07852 146 VKLADFGLarSLSQLEEDDEN----PVltdyvatRWYrAPEILlGSTRYTKGVDMWSVGCILGEMLLG---KPLFP 214
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
179-378 1.10e-08

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


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 56.14  E-value: 1.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRILGNAKRKqiqefcNEAQI-MTVLQHENIV--------AFYGFASLee 249
Cdd:cd14089   7 QVLGLGINGKVLECFHKKTGE-----KFALKVLRDNPKAR------REVELhWRASGCPHIVriidvyenTYQGRKCL-- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 250 piMVVMELVTGGDLRKYLQTTQNIP-----KLQILwfaMNVASGMRHLSSKGIIHRDLAARNCLVTQ---DLKAKISDFG 321
Cdd:cd14089  74 --LVVMECMEGGELFSRIQERADSAftereAAEIM---RQIGSAVAHLHSMNIAHRDLKPENLLYSSkgpNAILKLTDFG 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 322 LSlqgTEVTTKNLEKAPI---RWLAPESLKSGMFNEKTDVWSYGVFLTELMarCEHDPLY 378
Cdd:cd14089 149 FA---KETTTKKSLQTPCytpYYVAPEVLGPEKYDKSCDMWSLGVIMYILL--CGYPPFY 203
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
131-394 1.12e-08

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: 57.33  E-value: 1.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 131 LYEKFPTMPNRRFLHIRQLLEaWpqATPFlipTPRGSNVLIH-STINLDKKLGCGAFGEVfkgqykAVGSTNPPIEVAVK 209
Cdd:cd05624  35 LYTECSHSPLRRDKYVSEFLE-W--AKPF---TQLVKEMQLHrDDFEIIKVIGRGAFGEV------AVVKMKNTERIYAM 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 210 RILGN---AKRKQIQEFCNEAQIMTVLQHENIVAF-YGFASlEEPIMVVMELVTGGDLRKYLQTTQN-IPKLQILWFAMN 284
Cdd:cd05624 103 KILNKwemLKRAETACFREERNVLVNGDCQWITTLhYAFQD-ENYLYLVMDYYVGGDLLTLLSKFEDkLPEDMARFYIGE 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 285 VASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTT--KNLEKAPIRWLAPESLKS-----GMFNEKTD 357
Cdd:cd05624 182 MVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCLKMNDDGTvqSSVAVGTPDYISPEILQAmedgmGKYGPECD 261
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 17542550 358 VWSYGVFLTELMArcEHDPLYPKSLKDAKAWILT-EER 394
Cdd:cd05624 262 WWSLGVCMYEMLY--GETPFYAESLVETYGKIMNhEER 297
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
181-371 1.40e-08

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: 56.35  E-value: 1.40e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTnppieVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFY----------GFASLEE 249
Cdd:cd07864  15 IGEGTYGQVYKAKDKDTGEL-----VALKKVrLDNEKEGFPITAIREIKILRQLNHRSVVNLKeivtdkqdalDFKKDKG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 250 PIMVVMELVTGgDLRKYLQTTQ-NIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS-LQGT 327
Cdd:cd07864  90 AFYLVFEYMDH-DLMGLLESGLvHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLArLYNS 168
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17542550 328 EVTTKNLEKAPIRWLAPESLKSG--MFNEKTDVWSYGVFLTELMAR 371
Cdd:cd07864 169 EESRPYTNKVITLWYRPPELLLGeeRYGPAIDVWSCGCILGELFTK 214
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
179-323 1.49e-08

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: 56.81  E-value: 1.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGqYKAVGSTNPPIEVAVKRILGNakRKQIQEFCNEAQIMTVLQHENIVA-FYGFASLEEpIMVVMEL 257
Cdd:cd05610  10 KPISRGAFGKVYLG-RKKNNSKLYAVKVVKKADMIN--KNMVHQVQAERDALALSKSPFIVHlYYSLQSANN-VYLVMEY 85
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17542550 258 VTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS 323
Cdd:cd05610  86 LIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLS 151
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
180-379 1.57e-08

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: 55.89  E-value: 1.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGSTnppieVAVKRILGNAKRKQIQEFC-NEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd07846   8 LVGEGSYGMVMKCRHKETGQI-----VAIKKFLESEDDKMVKKIAmREIKMLKQLRHENLVNLIEVFRRKKRWYLVFEFV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TG---GDLRKYLQTTQNIPKLQILWfamNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLS---LQGTEVTTk 332
Cdd:cd07846  83 DHtvlDDLEKYPNGLDESRVRKYLF---QILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFArtlAAPGEVYT- 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17542550 333 nlEKAPIRWL-APESL-KSGMFNEKTDVWSYGVFLTELMArceHDPLYP 379
Cdd:cd07846 159 --DYVATRWYrAPELLvGDTKYGKAVDVWAVGCLVTEMLT---GEPLFP 202
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
181-381 1.62e-08

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 56.30  E-value: 1.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTnppieVAVKrILGN--AKRKQIQefcNEAQIMTVLQHE-----NIVAFYGFASLEEPIMV 253
Cdd:cd14211   7 LGRGTFGQVVKCWKRGTNEI-----VAIK-ILKNhpSYARQGQ---IEVSILSRLSQEnadefNFVRAYECFQHKNHTCL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGgDLRKYLQTT--QNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCL----VTQDLKAKISDFG-LSLQG 326
Cdd:cd14211  78 VFEMLEQ-NLYDFLKQNkfSPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMlvdpVRQPYRVKVIDFGsASHVS 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17542550 327 TEVTTKNLEKAPIRwlAPESLKSGMFNEKTDVWSYGVFLTELMARCehdPLYPKS 381
Cdd:cd14211 157 KAVCSTYLQSRYYR--APEIILGLPFCEAIDMWSLGCVIAELFLGW---PLYPGS 206
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
180-369 1.71e-08

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: 55.75  E-value: 1.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 180 KLGCGAFGEVFKGQYKAVGSTnppieVAVKRIlgNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVT 259
Cdd:cd14113  14 ELGRGRFSVVKKCDQRGTKRA-----VATKFV--NKKLMKRDQVTHELGVLQSLQHPQLVGLLDTFETPTSYILVLEMAD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 260 GGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKA---KISDFGLSLQ-GTEVTTKNLE 335
Cdd:cd14113  87 QGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSKptiKLADFGDAVQlNTTYYIHQLL 166
                       170       180       190
                ....*....|....*....|....*....|....
gi 17542550 336 KAPiRWLAPESLKSGMFNEKTDVWSYGVfLTELM 369
Cdd:cd14113 167 GSP-EFAAPEIILGNPVSLTSDLWSIGV-LTYVL 198
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
226-365 1.74e-08

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


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 55.83  E-value: 1.74e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 226 EAQIMTVLQHENIVAFygFASLEEP----IMVVMELVTGGDLRKyLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRD 301
Cdd:cd14118  64 EIAILKKLDHPNVVKL--VEVLDDPnednLYMVFELVDKGAVME-VPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRD 140
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17542550 302 LAARNCLVTQDLKAKISDFGLS--LQGTEVTTKNLEKAPIrWLAPESLKSG--MFNEK-TDVWSYGVFL 365
Cdd:cd14118 141 IKPSNLLLGDDGHVKIADFGVSneFEGDDALLSSTAGTPA-FMAPEALSESrkKFSGKaLDIWAMGVTL 208
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
181-383 1.88e-08

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 56.19  E-value: 1.88e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAvgsTNppiEVAVKRILGN----AKRKQIqefcnEAQIMTVLQHEN------IVAFYGFASLEEP 250
Cdd:cd14229   8 LGRGTFGQVVKCWKRG---TN---EIVAVKILKNhpsyARQGQI-----EVGILARLSNENadefnfVRAYECFQHRNHT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMELVTggDLRKYLQTTQNIP-KLQILW-FAMNVASGMRHLSSKGIIHRDLAARNCL----VTQDLKAKISDFG-LS 323
Cdd:cd14229  77 CLVFEMLEQ--NLYDFLKQNKFSPlPLKVIRpILQQVATALKKLKSLGLIHADLKPENIMlvdpVRQPYRVKVIDFGsAS 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 324 LQGTEVTTKNLEKAPIRwlAPESLKSGMFNEKTDVWSYGVFLTELMARCehdPLYPKSLK 383
Cdd:cd14229 155 HVSKTVCSTYLQSRYYR--APEIILGLPFCEAIDMWSLGCVIAELFLGW---PLYPGALE 209
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
205-370 2.10e-08

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: 55.69  E-value: 2.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 205 EVAVKRI----LGNAKRKQIQEFCN----EAQIM-TVLQHENIVAFYGFASLEEPIMVVMELVTGGDLRKYLQTTQNIPK 275
Cdd:cd14182  30 EYAVKIIditgGGSFSPEEVQELREatlkEIDILrKVSGHPNIIQLKDTYETNTFFFLVFDLMKKGELFDYLTEKVTLSE 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 276 LQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTTKNLEKAPIRWLAPESLKSGM---- 351
Cdd:cd14182 110 KETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLDPGEKLREVCGTPGYLAPEIIECSMddnh 189
                       170       180
                ....*....|....*....|.
gi 17542550 352 --FNEKTDVWSYGVFLTELMA 370
Cdd:cd14182 190 pgYGKEVDMWSTGVIMYTLLA 210
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
226-384 2.54e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 56.04  E-value: 2.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  226 EAQIMTVLQHENIVAFYG-FASLEEPIMVVMELVTggDLRKYL-QTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLA 303
Cdd:PHA03209 107 EAMLLQNVNHPSVIRMKDtLVSGAITCMVLPHYSS--DLYTYLtKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVK 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550  304 ARNCLVTQDLKAKISDFG-----------LSLQGTEVTTknlekapirwlAPESLKSGMFNEKTDVWSYGVFLTELMArc 372
Cdd:PHA03209 185 TENIFINDVDQVCIGDLGaaqfpvvapafLGLAGTVETN-----------APEVLARDKYNSKADIWSAGIVLFEMLA-- 251
                        170
                 ....*....|..
gi 17542550  373 ehdplYPKSLKD 384
Cdd:PHA03209 252 -----YPSTIFE 258
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
179-370 3.17e-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: 3.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTnppieVAVKrILGNA---KRKQIQEFCNEAQIMTVLQHENIVA-FYGFASlEEPIMVV 254
Cdd:cd05599   7 KVIGRGAFGEVRLVRKKDTGHV-----YAMK-KLRKSemlEKEQVAHVRAERDILAEADNPWVVKlYYSFQD-EENLYLI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGD----LRKYLQTTQNIPKLQILWFAMNVASGMRHlsskGIIHRDLAARNCLVTQDLKAKISDFGLSlqgtevt 330
Cdd:cd05599  80 MEFLPGGDmmtlLMKKDTLTEEETRFYIAETVLAIESIHKL----GYIHRDIKPDNLLLDARGHIKLSDFGLC------- 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17542550 331 tKNLEKAPIR--------WLAPES-LKSGmFNEKTDVWSYGVFLTELMA 370
Cdd:cd05599 149 -TGLKKSHLAystvgtpdYIAPEVfLQKG-YGKECDWWSLGVIMYEMLI 195
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
131-394 4.13e-08

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


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 55.41  E-value: 4.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 131 LYEKFPTMPNRRFLHIRQLLEaWpqATPFlipTPRGSNVLIH-STINLDKKLGCGAFGEVfkgqykAVGSTNPPIEVAVK 209
Cdd:cd05623  35 LYDECSNSPLRREKNILEYLE-W--AKPF---TSKVKQMRLHkEDFEILKVIGRGAFGEV------AVVKLKNADKVFAM 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 210 RILGN---AKRKQIQEFCNEAQIMTVLQHENIVAF-YGFASlEEPIMVVMELVTGGDLRKYLQTTQN-IPKLQILWFAMN 284
Cdd:cd05623 103 KILNKwemLKRAETACFREERDVLVNGDSQWITTLhYAFQD-DNNLYLVMDYYVGGDLLTLLSKFEDrLPEDMARFYLAE 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 285 VASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQGTEVTT--KNLEKAPIRWLAPESLKS-----GMFNEKTD 357
Cdd:cd05623 182 MVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMEDGTvqSSVAVGTPDYISPEILQAmedgkGKYGPECD 261
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 17542550 358 VWSYGVFLTELMArcEHDPLYPKSLKDAKAWILT-EER 394
Cdd:cd05623 262 WWSLGVCMYEMLY--GETPFYAESLVETYGKIMNhKER 297
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
160-369 6.08e-08

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


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 54.64  E-value: 6.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 160 LIPTPRGSNVLIHSTINLDKKLGCGAFGEVFKGQYKAVGstnppIEVAVKrILGNAKRKQIQEFcneAQIMTVLQHENIV 239
Cdd:cd14176   6 IVQQLHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATN-----MEFAVK-IIDKSKRDPTEEI---EILLRYGQHPNII 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 240 AFYGFASLEEPIMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDL----KA 315
Cdd:cd14176  77 TLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSI 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17542550 316 KISDFGLSLQgteVTTKN-LEKAPI---RWLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd14176 157 RICDFGFAKQ---LRAENgLLMTPCytaNFVAPEVLERQGYDAACDIWSLGVLLYTML 211
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
179-369 6.78e-08

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 54.63  E-value: 6.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILgnaKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd05626   7 KTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVL---NRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDYI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 259 TGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSL------------QG 326
Cdd:cd05626  84 PGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTgfrwthnskyyqKG 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17542550 327 TEVTTKNLEKAPI------------------------------------RWLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd05626 164 SHIRQDSMEPSDLwddvsncrcgdrlktleqratkqhqrclahslvgtpNYIAPEVLLRKGYTQLCDWWSVGVILFEML 242
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
186-384 8.87e-08

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 53.49  E-value: 8.87e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 186 FGEVFKGQYKAVGSTNppievAVKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTGGDLRK 265
Cdd:cd14088  14 FCEIFRAKDKTTGKLY-----TCKKFLKRDGRKVRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLELATGREVFD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 266 YL--------QTTQNIPKlqilwfamNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAK---ISDFGLSLQGTevttkNL 334
Cdd:cd14088  89 WIldqgyyseRDTSNVIR--------QVLEAVAYLHSLKIVHRNLKLENLVYYNRLKNSkivISDFHLAKLEN-----GL 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17542550 335 EKAPI---RWLAPESLKSGMFNEKTDVWSYGVFLTELMArcEHDPLYPKSLKD 384
Cdd:cd14088 156 IKEPCgtpEYLAPEVVGRQRYGRPVDCWAIGVIMYILLS--GNPPFYDEAEED 206
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
204-370 1.15e-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: 53.48  E-value: 1.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 204 IEVAVKrILGNAKRKQIQEFcneAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTGGDLRKYLQTTQNIPKLQILWFAM 283
Cdd:cd14177  30 MEFAVK-IIDKSKRDPSEEI---EILMRYGQHPNIITLKDVYDDGRYVYLVTELMKGGELLDRILRQKFFSEREASAVLY 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 284 NVASGMRHLSSKGIIHRDLAARNCLVTQDLKA----KISDFGLS--LQG------TEVTTKNlekapirWLAPESLKSGM 351
Cdd:cd14177 106 TITKTVDYLHCQGVVHRDLKPSNILYMDDSANadsiRICDFGFAkqLRGenglllTPCYTAN-------FVAPEVLMRQG 178
                       170
                ....*....|....*....
gi 17542550 352 FNEKTDVWSYGVFLTELMA 370
Cdd:cd14177 179 YDAACDIWSLGVLLYTMLA 197
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
251-378 1.49e-07

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


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 53.11  E-value: 1.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 251 IMVVMELVTGGDLRKYLQT--TQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQ---DLKAKISDFGLSlq 325
Cdd:cd14170  74 LLIVMECLDGGELFSRIQDrgDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFA-- 151
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17542550 326 gTEVTTKNLEKAPIR---WLAPESLKSGMFNEKTDVWSYGVFLTELMarCEHDPLY 378
Cdd:cd14170 152 -KETTSHNSLTTPCYtpyYVAPEVLGPEKYDKSCDMWSLGVIMYILL--CGYPPFY 204
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
226-365 1.91e-07

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: 52.64  E-value: 1.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 226 EAQIMTVLQHENIVAFygFASLEEP----IMVVMELVTGGDLRKyLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRD 301
Cdd:cd14200  73 EIAILKKLDHVNIVKL--IEVLDDPaednLYMVFDLLRKGPVME-VPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRD 149
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17542550 302 LAARNCLVTQDLKAKISDFGLSLQ--GTEVTTKNLEKAPIrWLAPESL---KSGMFNEKTDVWSYGVFL 365
Cdd:cd14200 150 IKPSNLLLGDDGHVKIADFGVSNQfeGNDALLSSTAGTPA-FMAPETLsdsGQSFSGKALDVWAMGVTL 217
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
179-369 2.45e-07

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: 52.35  E-value: 2.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGStnppiEVAVKRIlgnAKRKQIQEFCNE-----AQIMTVLQHENIVAFYGFASLEEPIMV 253
Cdd:cd14106  14 TPLGRGKFAVVRKCIHKETGK-----EYAAKFL---RKRRRGQDCRNEilheiAVLELCKDCPRVVNLHEVYETRSELIL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 254 VMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKA---KISDFGLS--LQgte 328
Cdd:cd14106  86 ILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPLgdiKLCDFGISrvIG--- 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17542550 329 vttknlEKAPIR-------WLAPESLKSGMFNEKTDVWSYGVfLTELM 369
Cdd:cd14106 163 ------EGEEIReilgtpdYVAPEILSYEPISLATDMWSIGV-LTYVL 203
SH2_Fps_family cd10361
Src homology 2 (SH2) domain found in feline sarcoma, Fujinami poultry sarcoma, and fes-related ...
66-139 2.94e-07

Src homology 2 (SH2) domain found in feline sarcoma, Fujinami poultry sarcoma, and fes-related (Fes/Fps/Fer) proteins; The Fps family consists of members Fps/Fes and Fer/Flk/Tyk3. They are cytoplasmic protein-tyrosine kinases implicated in signaling downstream from cytokines, growth factors and immune receptors. Fes/Fps/Fer contains three coiled-coil regions, an SH2 (Src-homology-2) and a TK (tyrosine kinase catalytic) domain signature. Members here include: Fps/Fes, Fer, Kin-31, and In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198224  Cd Length: 90  Bit Score: 48.29  E-value: 2.94e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17542550  66 LINLHVYHGVLFGSEAEKLLTWDRAYLVRRAITKP--NKFLCISVNWKKKIFHYQLDFNEDGWC-CKKlyEKFPTMP 139
Cdd:cd10361   3 LENEPYYHGLLPREDAEELLKNDGDFLVRKTEPKGggKRKLVLSVRWDGKIRHFVINRDDGGKYyIEG--KSFKSIS 77
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
187-371 3.61e-07

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: 51.72  E-value: 3.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 187 GEVFKGQYKAVgstnppiEVAVKRI-LGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTGGDLRK 265
Cdd:cd14057   9 GELWKGRWQGN-------DIVAKILkVRDVTTRISRDFNEEYPRLRIFSHPNVLPVLGACNSPPNLVVISQYMPYGSLYN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 266 YL--QTTQNIPKLQILWFAMNVASGMRHLSS-KGIIHR-DLAARNCLVTQDLKAKIS--DFGLSLQgtevtTKNLEKAPI 339
Cdd:cd14057  82 VLheGTGVVVDQSQAVKFALDIARGMAFLHTlEPLIPRhHLNSKHVMIDEDMTARINmaDVKFSFQ-----EPGKMYNPA 156
                       170       180       190
                ....*....|....*....|....*....|....*
gi 17542550 340 rWLAPESLK---SGMFNEKTDVWSYGVFLTELMAR 371
Cdd:cd14057 157 -WMAPEALQkkpEDINRRSADMWSFAILLWELVTR 190
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
179-338 5.41e-07

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 51.10  E-value: 5.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKgqykaVGSTNPPIEVAVKRilgNAKRKQIQEFCNEAQIMTVLQHENIVA-FYGFASLEEPIMVVMEL 257
Cdd:cd14017   6 KKIGGGGFGEIYK-----VRDVVDGEEVAMKV---ESKSQPKQVLKMEVAVLKKLQGKPHFCrLIGCGRTERYNYIVMTL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 258 VtG---GDLRKyLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLV----TQDLKAKISDFGLSLQGTEVt 330
Cdd:cd14017  78 L-GpnlAELRR-SQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIgrgpSDERTVYILDFGLARQYTNK- 154

                ....*...
gi 17542550 331 TKNLEKAP 338
Cdd:cd14017 155 DGEVERPP 162
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
179-369 6.32e-07

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: 51.55  E-value: 6.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTNppievAVK--RILGNAKRKQIQEFCNEAQIMTVLQHENIVA-FYGFASlEEPIMVVM 255
Cdd:cd05598   7 KTIGVGAFGEVSLVRKKDTNALY-----AMKtlRKKDVLKRNQVAHVKAERDILAEADNEWVVKlYYSFQD-KENLYFVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 256 ELVTGGDLRKYLQTT----QNIPKLQILWFAMNVASgmrhLSSKGIIHRDLAARNCLVTQDLKAKISDFGL--------- 322
Cdd:cd05598  81 DYIPGGDLMSLLIKKgifeEDLARFYIAELVCAIES----VHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthd 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17542550 323 -------SLQGTevttknlekaPiRWLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd05598 157 skyylahSLVGT----------P-NYIAPEVLLRTGYTQLCDWWSVGVILYEML 199
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
184-453 6.37e-07

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: 50.99  E-value: 6.37e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 184 GAFGEVFKGQykavgSTNPPIEVA-VKRILGNAKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTGGD 262
Cdd:cd14157   4 GTFADIYKGY-----RHGKQYVIKrLKETECESPKSTERFFQTEVQICFRCCHPNILPLLGFCVESDCHCLIYPYMPNGS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 263 LRKYLQT---TQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSL-------QGTEVTTK 332
Cdd:cd14157  79 LQDRLQQqggSHPLPWEQRLSISLGLLKAVQHLHNFGILHGNIKSSNVLLDGNLLPKLGHSGLRLcpvdkksVYTMMKTK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 333 NLeKAPIRWLAPESLKSGMFNEKTDVWSYGVFLTEL---MARCEHDPlYPKSLKDakawILTEERPHKMENGDPKelmvl 409
Cdd:cd14157 159 VL-QISLAYLPEDFVRHGQLTEKVDIFSCGVVLAEIltgIKAMDEFR-SPVYLKD----LLLEEIQRAKEGSQSK----- 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 17542550 410 idaccERNPNerlnfNTVKRQITDIYMEAlnkgpQDGRKPENSA 453
Cdd:cd14157 228 -----HKSPE-----SLAAKEICSKYLDK-----RAGLLPENVA 256
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
181-378 7.41e-07

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: 51.42  E-value: 7.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 181 LGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILgnaKRKQIQEFCNEAQIM--TVLQHENIVAFYGFaSLEEP--IMVVME 256
Cdd:cd05586   1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIV---AKKEVAHTIGERNILvrTALDESPFIVGLKF-SFQTPtdLYLVTD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 257 LVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGLSLQG-TEVTTKNLE 335
Cdd:cd05586  77 YMSGGELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADlTDNKTTNTF 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 17542550 336 KAPIRWLAPES-LKSGMFNEKTDVWSYGVFLTELMarCEHDPLY 378
Cdd:cd05586 157 CGTTEYLAPEVlLDEKGYTKMVDFWSLGVLVFEMC--CGWSPFY 198
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
216-363 7.79e-07

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: 50.69  E-value: 7.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 216 KRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSK 295
Cdd:cd14110  39 KPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSR 118
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 296 GIIHRDLAARNCLVTQDLKAKISDFG--LSLQGTEVTTKNLEKAPIRWLAPESLKSGMFNEKTDVWSYGV 363
Cdd:cd14110 119 RILHLDLRSENMIITEKNLLKIVDLGnaQPFNQGKVLMTDKKGDYVETMAPELLEGQGAGPQTDIWAIGV 188
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
176-371 1.07e-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: 50.63  E-value: 1.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 176 NLDKKLGCGAFGEVFKGQYKAVGStnppiEVAVKRILGNAKRK---QIQEFCNEAQIMTvlQHENIVAF----------- 241
Cdd:cd13977   3 SLIREVGRGSYGVVYEAVVRRTGA-----RVAVKKIRCNAPENvelALREFWALSSIQR--QHPNVIQLeecvlqrdgla 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 242 ------YGFASLEEPIM-------------------VVMELVTGGDLRKYLQTTQNIPKLQILwFAMNVASGMRHLSSKG 296
Cdd:cd13977  76 qrmshgSSKSDLYLLLVetslkgercfdprsacylwFVMEFCDGGDMNEYLLSRRPDRQTNTS-FMLQLSSALAFLHRNQ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 297 IIHRDLAARNCLVTQDLKA---KISDFGLSLQGTEVTTKNLEKAPIR------------WLAPEsLKSGMFNEKTDVWSY 361
Cdd:cd13977 155 IVHRDLKPDNILISHKRGEpilKVADFGLSKVCSGSGLNPEEPANVNkhflssacgsdfYMAPE-VWEGHYTAKADIFAL 233
                       250
                ....*....|
gi 17542550 362 GVFLTELMAR 371
Cdd:cd13977 234 GIIIWAMVER 243
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
233-383 1.79e-06

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


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 49.38  E-value: 1.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 233 LQHENIVAFYGFASLEEPIMVVMELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLV--T 310
Cdd:cd14662  53 LRHPNIIRFKEVVLTPTHLAIVMEYAAGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLdgS 132
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17542550 311 QDLKAKISDFGLSLQGT-EVTTKNLEKAPIrWLAPESLKSGMFNEK-TDVWSYGVFLTELM--ARCEHDPLYPKSLK 383
Cdd:cd14662 133 PAPRLKICDFGYSKSSVlHSQPKSTVGTPA-YIAPEVLSRKEYDGKvADVWSCGVTLYVMLvgAYPFEDPDDPKNFR 208
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
179-415 2.21e-06

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: 50.04  E-value: 2.21e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGstnppiEVAVKRILGNA---KRKQIQEFCNEAQIMTVLQHENIVA-FYGFASlEEPIMVV 254
Cdd:cd05628   7 KVIGRGAFGEVRLVQKKDTG------HVYAMKILRKAdmlEKEQVGHIRAERDILVEADSLWVVKmFYSFQD-KLNLYLI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGL------------ 322
Cdd:cd05628  80 MEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLctglkkahrtef 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 323 ------------------SLQGTEVTTKNLEKAPIR------WLAPESLKSGMFNEKTDVWSYGVFLTELM----ARCEH 374
Cdd:cd05628 160 yrnlnhslpsdftfqnmnSKRKAETWKRNRRQLAFStvgtpdYIAPEVFMQTGYNKLCDWWSLGVIMYEMLigypPFCSE 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 17542550 375 DP--LYPKSLKDAKAWILTEERPHKMENGDpkelmVLIDACCE 415
Cdd:cd05628 240 TPqeTYKKVMNWKETLIFPPEVPISEKAKD-----LILRFCCE 277
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
179-322 2.57e-06

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 49.66  E-value: 2.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGSTNPPIEVAVKRILgnaKRKQIQEFCNEAQIMTVLQHENIVAFYGFASLEEPIMVVMELV 258
Cdd:cd05625   7 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVL---LRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYI 83
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17542550 259 TGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGL 322
Cdd:cd05625  84 PGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGL 147
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
171-363 2.88e-06

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


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 49.15  E-value: 2.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 171 IHSTINLDKK-LGCGAFGEVFKGQYKAVGStnppiEVAVKRIlgnAKRKQIQEfCnEAQIM---TVLQ----HENIVAFY 242
Cdd:cd14198   5 FNNFYILTSKeLGRGKFAVVRQCISKSTGQ-----EYAAKFL---KKRRRGQD-C-RAEILheiAVLElaksNPRVVNLH 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 243 GFASLEEPIMVVMELVTGGDLRKYL--QTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQ-----DLKa 315
Cdd:cd14198  75 EVYETTSEIILILEYAAGGEIFNLCvpDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSiyplgDIK- 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17542550 316 kISDFGLSLQ-GTEVTTKNLEKAPiRWLAPESLKSGMFNEKTDVWSYGV 363
Cdd:cd14198 154 -IVDFGMSRKiGHACELREIMGTP-EYLAPEILNYDPITTATDMWNIGV 200
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
179-369 2.91e-06

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: 49.67  E-value: 2.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 179 KKLGCGAFGEVFKGQYKAVGstnppiEVAVKRILGNA---KRKQIQEFCNEAQIMTVLQHENIVA-FYGFASlEEPIMVV 254
Cdd:cd05627   8 KVIGRGAFGEVRLVQKKDTG------HIYAMKILRKAdmlEKEQVAHIRAERDILVEADGAWVVKmFYSFQD-KRNLYLI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542550 255 MELVTGGDLRKYLQTTQNIPKLQILWFAMNVASGMRHLSSKGIIHRDLAARNCLVTQDLKAKISDFGL------------ 322
Cdd:cd05627  81 MEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLctglkkahrtef 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17542550 323 ------------------SLQGTEVTTKNLEKAPIR------WLAPESLKSGMFNEKTDVWSYGVFLTELM 369
Cdd:cd05627 161 yrnlthnppsdfsfqnmnSKRKAETWKKNRRQLAYStvgtpdYIAPEVFMQTGYNKLCDWWSLGVIMYEML 231
 
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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