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Conserved domains on  [gi|223461072|gb|AAI38795|]
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Receptor tyrosine kinase-like orphan receptor 1 [Mus musculus]

Protein Classification

inactive tyrosine-protein kinase transmembrane receptor ROR1( domain architecture ID 12077559)

inactive tyrosine-protein kinase transmembrane receptor ROR1 maybe a receptor for ligand WNT5A which activate downstream NFkB signaling pathway and may result in the inhibition of WNT3A-mediated signaling; has very low kinase activity in vitro

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
467-749 0e+00

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: 623.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGHLYLPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQ 546
Cdd:cd05090    1 ELPLSAVRFMEELGECAFGKIYKGHLYLPGMDHAQLVAIKTLKDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 547 PVCMLFEYMNQGDLHEFLIMRSPHSDVGCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQ 626
Cdd:cd05090   81 PVCMLFEFMNQGDLHEFLIMRSPHSDVGCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 627 LHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVR 706
Cdd:cd05090  161 LHVKISDLGLSREIYSSDYYRVQNKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVR 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 223461072 707 KRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRLRSW 749
Cdd:cd05090  241 KRQLLPCSEDCPPRMYSLMTECWQEIPSRRPRFKDIHARLRSW 283
CRD_TK_ROR1 cd07467
Cysteine-rich domain of tyrosine kinase-like orphan receptor 1; The cysteine-rich domain (CRD) ...
166-307 5.37e-108

Cysteine-rich domain of tyrosine kinase-like orphan receptor 1; The cysteine-rich domain (CRD) is an essential part of the tyrosine kinase-like orphan receptor 1 (Ror1), a conserved family of tyrosine kinases that function in various processes, including neuronal and skeletal development, cell polarity, and cell movement. Ror proteins are receptors of Wnt proteins, which are key players in a number of fundamental cellular processes in embryogenesis and postnatal development. In different cellular contexts, Ror proteins can either activate or repress transcription of Wnt target genes, and can modulate Wnt signaling by sequestering Wnt ligands. In addition, a number of Wnt-independent functions have been proposed for both Ror1 and Ror2.


:

Pssm-ID: 143576  Cd Length: 142  Bit Score: 329.69  E-value: 5.37e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 166 EDGFCQPYRGIACARFIGNRTVYMESLHMQGEIENQITAAFTMIGTSSHLSDKCSQFAIPSLCHYAFPYCDETSSVPKPR 245
Cdd:cd07467    1 EDGFCQPYRGIACARFIGNRTIYMESLHMQGEIENQITAAFTMIGTSSHLSDKCSQFAIPSLCHYAFPYCDETSGMPKPR 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223461072 246 DLCRDECEVLENVLCQTEYIFARSNPMILMRLKLPNCEDLPQPESPEAANCIRIGIPMADPI 307
Cdd:cd07467   81 DLCRDECEILENVLCQTEYIFARSNPMILMRLKLPNCEDLAQPDSPEAANCIRIGIPMADPI 142
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
311-393 3.88e-42

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


:

Pssm-ID: 214527  Cd Length: 83  Bit Score: 148.31  E-value: 3.88e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072   311 HKCYNSTGVDYRGTVSVTKSGRQCQPWNSQYPHTHSFTALRFPELNGGHSYCRNPGNQKEAPWCFTLDENFKSDLCDIPA 390
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80

                   ...
gi 223461072   391 CDS 393
Cdd:smart00130  81 CEE 83
I-set pfam07679
Immunoglobulin I-set domain;
63-148 1.80e-19

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 83.85  E-value: 1.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072   63 PMNNITTSLGQTAELHCKVSGNPPPSIRWFKNDAPvVQEPRRISFRATNYGSRLRIRNLDTTDTGYFQCVATNGKKVVST 142
Cdd:pfam07679   6 KPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQP-LRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEA 84

                  ....*.
gi 223461072  143 TGVLFV 148
Cdd:pfam07679  85 SAELTV 90
 
Name Accession Description Interval E-value
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
467-749 0e+00

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: 623.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGHLYLPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQ 546
Cdd:cd05090    1 ELPLSAVRFMEELGECAFGKIYKGHLYLPGMDHAQLVAIKTLKDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 547 PVCMLFEYMNQGDLHEFLIMRSPHSDVGCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQ 626
Cdd:cd05090   81 PVCMLFEFMNQGDLHEFLIMRSPHSDVGCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 627 LHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVR 706
Cdd:cd05090  161 LHVKISDLGLSREIYSSDYYRVQNKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVR 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 223461072 707 KRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRLRSW 749
Cdd:cd05090  241 KRQLLPCSEDCPPRMYSLMTECWQEIPSRRPRFKDIHARLRSW 283
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
473-746 2.35e-134

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: 403.03  E-value: 2.35e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  473 VRFMEELGECTFGKIYKGHLYLPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLF 552
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEGENTKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  553 EYMNQGDLHEFLIMRsphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKIS 632
Cdd:pfam07714  81 EYMPGGDLLDFLRKH----------------KRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKIS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  633 DLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLP 712
Cdd:pfam07714 145 DFGLSRDIYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLP 224
                         250       260       270
                  ....*....|....*....|....*....|....
gi 223461072  713 CSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:pfam07714 225 QPENCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
473-746 8.42e-131

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 393.82  E-value: 8.42e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072   473 VRFMEELGECTFGKIYKGHLYLPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLF 552
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKGKGGKKKVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072   553 EYMNQGDLHEFLIMRSPHsdvgcssdedgtvkssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKIS 632
Cdd:smart00219  81 EYMEGGDLLSYLRKNRPK----------------LSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKIS 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072   633 DLGLSREIYSADYYRVQSKSsLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLP 712
Cdd:smart00219 145 DFGLSRDLYDDDYYRKRGGK-LPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGYRLP 223
                          250       260       270
                   ....*....|....*....|....*....|....
gi 223461072   713 CSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:smart00219 224 QPPNCPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
CRD_TK_ROR1 cd07467
Cysteine-rich domain of tyrosine kinase-like orphan receptor 1; The cysteine-rich domain (CRD) ...
166-307 5.37e-108

Cysteine-rich domain of tyrosine kinase-like orphan receptor 1; The cysteine-rich domain (CRD) is an essential part of the tyrosine kinase-like orphan receptor 1 (Ror1), a conserved family of tyrosine kinases that function in various processes, including neuronal and skeletal development, cell polarity, and cell movement. Ror proteins are receptors of Wnt proteins, which are key players in a number of fundamental cellular processes in embryogenesis and postnatal development. In different cellular contexts, Ror proteins can either activate or repress transcription of Wnt target genes, and can modulate Wnt signaling by sequestering Wnt ligands. In addition, a number of Wnt-independent functions have been proposed for both Ror1 and Ror2.


Pssm-ID: 143576  Cd Length: 142  Bit Score: 329.69  E-value: 5.37e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 166 EDGFCQPYRGIACARFIGNRTVYMESLHMQGEIENQITAAFTMIGTSSHLSDKCSQFAIPSLCHYAFPYCDETSSVPKPR 245
Cdd:cd07467    1 EDGFCQPYRGIACARFIGNRTIYMESLHMQGEIENQITAAFTMIGTSSHLSDKCSQFAIPSLCHYAFPYCDETSGMPKPR 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223461072 246 DLCRDECEVLENVLCQTEYIFARSNPMILMRLKLPNCEDLPQPESPEAANCIRIGIPMADPI 307
Cdd:cd07467   81 DLCRDECEILENVLCQTEYIFARSNPMILMRLKLPNCEDLAQPDSPEAANCIRIGIPMADPI 142
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
311-393 3.88e-42

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


Pssm-ID: 214527  Cd Length: 83  Bit Score: 148.31  E-value: 3.88e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072   311 HKCYNSTGVDYRGTVSVTKSGRQCQPWNSQYPHTHSFTALRFPELNGGHSYCRNPGNQKEAPWCFTLDENFKSDLCDIPA 390
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80

                   ...
gi 223461072   391 CDS 393
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
310-392 2.26e-40

Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.


Pssm-ID: 238056  Cd Length: 83  Bit Score: 143.29  E-value: 2.26e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 310 NHKCYNSTGVDYRGTVSVTKSGRQCQPWNSQYPHTHSFTALRFPELNGGHSYCRNPGNQKEAPWCFTLDENFKSDLCDIP 389
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIP 80

                 ...
gi 223461072 390 ACD 392
Cdd:cd00108   81 RCE 83
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
477-720 2.01e-29

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 123.20  E-value: 2.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHlylpgmDHA--QLVAIKTLK-DYNNPQQWTE-FQQEASLMAELHHPNIVCLLGAVTQEQPVCMLF 552
Cdd:COG0515   13 RLLGRGGMGVVYLAR------DLRlgRPVALKVLRpELAADPEARErFRREARALARLNHPNIVRVYDVGEEDGRPYLVM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 EYMNQGDLHEFLIMRSPhsdvgcssdedgtvkssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKIS 632
Cdd:COG0515   87 EYVEGESLADLLRRRGP-----------------LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 633 DLGLSREIYSADyyrvQSKSSLPI---RWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRKRQ 709
Cdd:COG0515  150 DFGIARALGGAT----LTQTGTVVgtpGYMAPEQARGEPVDPRSDVYSLGVTLYELLT-GRPPFDGDSPAELLRAHLREP 224
                        250
                 ....*....|....
gi 223461072 710 LLPCSE---DCPPR 720
Cdd:COG0515  225 PPPPSElrpDLPPA 238
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
313-391 4.69e-27

Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.


Pssm-ID: 395005  Cd Length: 79  Bit Score: 105.08  E-value: 4.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  313 CYNSTGVDYRGTVSVTKSGRQCQPWNSQYPHTHSF-TALRFPELNGGHSYCRNPGNQkEAPWCFTLDENFKSDLCDIPAC 391
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGD-ERPWCYTTDPRVRWEYCDIPRC 79
I-set pfam07679
Immunoglobulin I-set domain;
63-148 1.80e-19

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 83.85  E-value: 1.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072   63 PMNNITTSLGQTAELHCKVSGNPPPSIRWFKNDAPvVQEPRRISFRATNYGSRLRIRNLDTTDTGYFQCVATNGKKVVST 142
Cdd:pfam07679   6 KPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQP-LRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEA 84

                  ....*.
gi 223461072  143 TGVLFV 148
Cdd:pfam07679  85 SAELTV 90
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
479-687 4.23e-19

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 89.82  E-value: 4.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQWTEFQQ-------------EASLMAELHHPNIVCLLGAVTQE 545
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTG----KIVAIKKVKIIEISNDVTKDRQlvgmcgihfttlrELKIMNEIKHENIMGLVDVYVEG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 546 QPVCMLFEYMnQGDLHEFL--IMRSPHSDVGCssdedgtvkssldhgdflhIAIQIAAGMEYLSSHFFVHKDLAARNILI 623
Cdd:PTZ00024  93 DFINLVMDIM-ASDLKKVVdrKIRLTESQVKC-------------------ILLQILNGLNVLHKWYFMHRDLSPANIFI 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223461072 624 GEQLHVKISDLGLSREIYSADYYRVQSKSSLPIR-----------WM-PPEAIM-YGKFSSDSDIWSFGVVLWEIFS 687
Cdd:PTZ00024 153 NSKGICKIADFGLARRYGYPPYSDTLSKDETMQRreemtskvvtlWYrAPELLMgAEKYHFAVDMWSVGCIFAELLT 229
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
66-148 5.71e-19

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 82.17  E-value: 5.71e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072    66 NITTSLGQTAELHCKVSGNPPPSIRWFKNDAPVVQEPRRISFRATNYGSRLRIRNLDTTDTGYFQCVATNGKKVVSTTGV 145
Cdd:smart00410   3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                   ...
gi 223461072   146 LFV 148
Cdd:smart00410  83 LTV 85
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
170-288 2.23e-17

Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This domain of unknown function has been independently identified by several groups. The domain contains 10 conserved cysteines.


Pssm-ID: 460190  Cd Length: 116  Bit Score: 78.76  E-value: 2.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  170 CQPYRGIACARFIGNRTVYMESLHMQGEIENQITAAFTMIGTSSHLSD-KCSQFAIPSLCHYAFPYCDETSSVPKPRDLC 248
Cdd:pfam01392   1 CEPITLPMCLGLGYNATVFPNLLGHQTQEEAELSLAYLVLSEFEPLVDlSCSPSLRLFLCSLYFPPCTLGPSPKPVCPPC 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 223461072  249 RDECEVLENvLCQTEYIFARSNPMILMRLklpNCEDLPQP 288
Cdd:pfam01392  81 RSLCEEVRY-GCEPLLEEAKFGFSWPEFL---DCDSLPAD 116
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
60-143 3.54e-17

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 77.43  E-value: 3.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  60 LDEPMNNITTSLGQTAELHCKVSGNPPPSIRWFKNDAPVVQEPRRISFRAtnygSRLRIRNLDTTDTGYFQCVATN--GK 137
Cdd:cd20978    4 IQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVED----GTLTIINVQPEDTGYYGCVATNeiGD 79

                 ....*.
gi 223461072 138 KVVSTT 143
Cdd:cd20978   80 IYTETL 85
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
503-684 9.39e-12

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 68.67  E-value: 9.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 503 VAIKTLK-DYNNPQQWTE-FQQEASLMAELHHPNIVcllgAVT---QEQPV---CMlfEYMNQGDLHEFLIMRSPhsdvg 574
Cdd:NF033483  35 VAVKVLRpDLARDPEFVArFRREAQSAASLSHPNIV----SVYdvgEDGGIpyiVM--EYVDGRTLKDYIREHGP----- 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 575 cssdedgtvkssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSRE------------IYS 642
Cdd:NF033483 104 ------------LSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARAlssttmtqtnsvLGT 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 223461072 643 ADYyrvqsksslpirwMPPEAIMYGKFSSDSDIWSFGVVLWE 684
Cdd:NF033483 172 VHY-------------LSPEQARGGTVDARSDIYSLGIVLYE 200
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
498-719 2.28e-07

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 54.85  E-value: 2.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072   498 DHAQLVAIKTLKD--YNNPQQWTEFQQEASLMAELHHPNIVCLL-GAVTQEQPVCMLFEYMNQGDLHEFLIMRSPhsdvg 574
Cdd:TIGR03903    1 MTGHEVAIKLLRTdaPEEEHQRARFRRETALCARLYHPNIVALLdSGEAPPGLLFAVFEYVPGRTLREVLAADGA----- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072   575 cssdedgtvkssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILI---GEQLHVKISDLGLS------REIYSADY 645
Cdd:TIGR03903   76 ------------LPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVsqtGVRPHAKVLDFGIGtllpgvRDADVATL 143
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223461072   646 YRVQSKSSLPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEmvrkRQLLPCSEDCPP 719
Cdd:TIGR03903  144 TRTTEVLGTP-TYCAPEQLRGEPVTPNSDLYAWGLIFLECLT-GQRVVQGASVAEILY----QQLSPVDVSLPP 211
 
Name Accession Description Interval E-value
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
467-749 0e+00

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: 623.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGHLYLPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQ 546
Cdd:cd05090    1 ELPLSAVRFMEELGECAFGKIYKGHLYLPGMDHAQLVAIKTLKDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 547 PVCMLFEYMNQGDLHEFLIMRSPHSDVGCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQ 626
Cdd:cd05090   81 PVCMLFEFMNQGDLHEFLIMRSPHSDVGCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 627 LHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVR 706
Cdd:cd05090  161 LHVKISDLGLSREIYSSDYYRVQNKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVR 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 223461072 707 KRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRLRSW 749
Cdd:cd05090  241 KRQLLPCSEDCPPRMYSLMTECWQEIPSRRPRFKDIHARLRSW 283
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
467-749 0e+00

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: 583.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGHLYLPG-MDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQE 545
Cdd:cd05048    1 EIPLSAVRFLEELGEGAFGKVYKGELLGPSsEESAISVAIKTLKENASPKTQQDFRREAELMSDLQHPNIVCLLGVCTKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 546 QPVCMLFEYMNQGDLHEFLIMRSPHSDVGCSSDeDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGE 625
Cdd:cd05048   81 QPQCMLFEYMAHGDLHEFLVRHSPHSDVGVSSD-DDGTASSLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLVGD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 626 QLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMV 705
Cdd:cd05048  160 GLTVKISDFGLSRDIYSSDYYRVQSKSLLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSYGLQPYYGYSNQEVIEMI 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 223461072 706 RKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRLRSW 749
Cdd:cd05048  240 RSRQLLPCPEDCPARVYSLMVECWHEIPSRRPRFKEIHTRLRTW 283
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
466-749 1.27e-160

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: 471.81  E-value: 1.27e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 466 KELPLSAVRFMEELGECTFGKIYKGHLY--LPGmDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVT 543
Cdd:cd05091    1 KEINLSAVRFMEELGEDRFGKVYKGHLFgtAPG-EQTQAVAIKTLKDKAEGPLREEFRHEAMLRSRLQHPNIVCLLGVVT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 544 QEQPVCMLFEYMNQGDLHEFLIMRSPHSDVGcSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILI 623
Cdd:cd05091   80 KEQPMSMIFSYCSHGDLHEFLVMRSPHSDVG-STDDDKTVKSTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 624 GEQLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIE 703
Cdd:cd05091  159 FDKLNVKISDLGLFREVYAADYYKLMGNSLLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSYGLQPYCGYSNQDVIE 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 223461072 704 MVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRLRSW 749
Cdd:cd05091  239 MIRNRQVLPCPDDCPAWVYTLMLECWNEFPSRRPRFKDIHSRLRTW 284
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
473-746 2.35e-134

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: 403.03  E-value: 2.35e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  473 VRFMEELGECTFGKIYKGHLYLPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLF 552
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEGENTKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  553 EYMNQGDLHEFLIMRsphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKIS 632
Cdd:pfam07714  81 EYMPGGDLLDFLRKH----------------KRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKIS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  633 DLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLP 712
Cdd:pfam07714 145 DFGLSRDIYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLP 224
                         250       260       270
                  ....*....|....*....|....*....|....
gi 223461072  713 CSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:pfam07714 225 QPENCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
473-746 8.42e-131

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 393.82  E-value: 8.42e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072   473 VRFMEELGECTFGKIYKGHLYLPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLF 552
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKGKGGKKKVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072   553 EYMNQGDLHEFLIMRSPHsdvgcssdedgtvkssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKIS 632
Cdd:smart00219  81 EYMEGGDLLSYLRKNRPK----------------LSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKIS 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072   633 DLGLSREIYSADYYRVQSKSsLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLP 712
Cdd:smart00219 145 DFGLSRDLYDDDYYRKRGGK-LPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGYRLP 223
                          250       260       270
                   ....*....|....*....|....*....|....
gi 223461072   713 CSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:smart00219 224 QPPNCPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
473-746 8.62e-131

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: 393.84  E-value: 8.62e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072   473 VRFMEELGECTFGKIYKGHLYLPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLF 552
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGKGDGKEVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072   553 EYMNQGDLHEFLIMRSPHSdvgcssdedgtvkssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKIS 632
Cdd:smart00221  81 EYMPGGDLLDYLRKNRPKE---------------LSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKIS 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072   633 DLGLSREIYSADYYRVQSKSsLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLP 712
Cdd:smart00221 146 DFGLSRDLYDDDYYKVKGGK-LPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGYRLP 224
                          250       260       270
                   ....*....|....*....|....*....|....
gi 223461072   713 CSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:smart00221 225 KPPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
477-747 4.32e-125

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: 379.19  E-value: 4.32e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLYLPGmDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMN 556
Cdd:cd00192    1 KKLGEGAFGEVYKGKLKGGD-GKTVDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLIMRSPHSDVgcssdedgTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGL 636
Cdd:cd00192   80 GGDLLDFLRKSRPVFPS--------PEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 637 SREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPCSED 716
Cdd:cd00192  152 SRDIYDDDYYRKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPGLSNEEVLEYLRKGYRLPKPEN 231
                        250       260       270
                 ....*....|....*....|....*....|.
gi 223461072 717 CPPRMYSLMTECWNEIPSRRPRFKDIHVRLR 747
Cdd:cd00192  232 CPDELYELMLSCWQLDPEDRPTFSELVERLE 262
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
467-747 1.28e-108

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: 336.75  E-value: 1.28e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGHLY--LPGMDhAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQ 544
Cdd:cd05049    1 HIKRDTIVLKRELGEGAFGKVFLGECYnlEPEQD-KMLVAVKTLKDASSPDARKDFEREAELLTNLQHENIVKFYGVCTE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 545 EQPVCMLFEYMNQGDLHEFLIMRSPHSDVGCSSDEDgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIG 624
Cdd:cd05049   80 GDPLLMVFEYMEHGDLNKFLRSHGPDAAFLASEDSA---PGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 625 EQLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEM 704
Cdd:cd05049  157 TNLVVKIGDFGMSRDIYSTDYYRVGGHTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWFQLSNTEVIEC 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 223461072 705 VRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRLR 747
Cdd:cd05049  237 ITQGRLLQRPRTCPSEVYAVMLGCWKREPQQRLNIKDIHKRLQ 279
CRD_TK_ROR1 cd07467
Cysteine-rich domain of tyrosine kinase-like orphan receptor 1; The cysteine-rich domain (CRD) ...
166-307 5.37e-108

Cysteine-rich domain of tyrosine kinase-like orphan receptor 1; The cysteine-rich domain (CRD) is an essential part of the tyrosine kinase-like orphan receptor 1 (Ror1), a conserved family of tyrosine kinases that function in various processes, including neuronal and skeletal development, cell polarity, and cell movement. Ror proteins are receptors of Wnt proteins, which are key players in a number of fundamental cellular processes in embryogenesis and postnatal development. In different cellular contexts, Ror proteins can either activate or repress transcription of Wnt target genes, and can modulate Wnt signaling by sequestering Wnt ligands. In addition, a number of Wnt-independent functions have been proposed for both Ror1 and Ror2.


Pssm-ID: 143576  Cd Length: 142  Bit Score: 329.69  E-value: 5.37e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 166 EDGFCQPYRGIACARFIGNRTVYMESLHMQGEIENQITAAFTMIGTSSHLSDKCSQFAIPSLCHYAFPYCDETSSVPKPR 245
Cdd:cd07467    1 EDGFCQPYRGIACARFIGNRTIYMESLHMQGEIENQITAAFTMIGTSSHLSDKCSQFAIPSLCHYAFPYCDETSGMPKPR 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223461072 246 DLCRDECEVLENVLCQTEYIFARSNPMILMRLKLPNCEDLPQPESPEAANCIRIGIPMADPI 307
Cdd:cd07467   81 DLCRDECEILENVLCQTEYIFARSNPMILMRLKLPNCEDLAQPDSPEAANCIRIGIPMADPI 142
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
467-747 4.01e-103

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: 322.55  E-value: 4.01e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGHL--YLPGMDHAqLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQ 544
Cdd:cd05050    1 EYPRNNIEYVRDIGQGAFGRVFQARApgLLPYEPFT-MVAVKMLKEEASADMQADFQREAALMAEFDHPNIVKLLGVCAV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 545 EQPVCMLFEYMNQGDLHEFLIMRSPHSDVGCSSDEDGTVKSSLDHGDF-----LHIAIQIAAGMEYLSSHFFVHKDLAAR 619
Cdd:cd05050   80 GKPMCLLFEYMAYGDLNEFLRHRSPRAQCSLSHSTSSARKCGLNPLPLscteqLCIAKQVAAGMAYLSERKFVHRDLATR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 620 NILIGEQLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQ 699
Cdd:cd05050  160 NCLVGENMVVKIADFGLSRNIYSADYYKASENDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGMQPYYGMAHE 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 223461072 700 EVIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRLR 747
Cdd:cd05050  240 EVIYYVRDGNVLSCPDNCPLELYNLMRLCWSKLPSDRPSFASINRILQ 287
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
467-746 7.34e-91

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: 290.39  E-value: 7.34e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFG------------KIYKGHLYLPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPN 534
Cdd:cd05051    1 EFPREKLEFVEKLGEGQFGevhlceanglsdLTSDDFIGNDNKDEPVLVAVKMLRPDASKNAREDFLKEVKIMSQLKDPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 535 IVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSPHSDVGCSSDedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHK 614
Cdd:cd05051   81 IVRLLGVCTRDEPLCMIVEYMENGDLNQFLQKHEAETQGASATN-----SKTLSYGTLLYMATQIASGMKYLESLNFVHR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 615 DLAARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFG-LQPY 693
Cdd:cd05051  156 DLATRNCLVGPNYTIKIADFGMSRNLYSGDYYRIEGRAVLPIRWMAWESILLGKFTTKSDVWAFGVTLWEILTLCkEQPY 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 694 YGFSNQEVIEMV-------RKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd05051  236 EHLTDEQVIENAgeffrddGMEVYLSRPPNCPKEIYELMLECWRRDEEDRPTFREIHLFL 295
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
478-748 1.09e-90

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: 289.56  E-value: 1.09e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 478 ELGECTFGKIYKGHLY--LPGMDHAqLVAIKTLKDYN-NPQQwtEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd05092   12 ELGEGAFGKVFLAECHnlLPEQDKM-LVAVKALKEATeSARQ--DFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQGDLHEFLimRSPHSDVGCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd05092   89 MRHGDLNRFL--RSHGPDAKILDGGEGQAPGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 635 GLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPCS 714
Cdd:cd05092  167 GMSRDIYSTDYYRVGGRTMLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTYGKQPWYQLSNTEAIECITQGRELERP 246
                        250       260       270
                 ....*....|....*....|....*....|....
gi 223461072 715 EDCPPRMYSLMTECWNEIPSRRPRFKDIHVRLRS 748
Cdd:cd05092  247 RTCPPEVYAIMQGCWQREPQQRHSIKDIHSRLQA 280
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
467-748 1.04e-88

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: 283.85  E-value: 1.04e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGHLYLPGMDHAQL-VAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQE 545
Cdd:cd05032    2 ELPREKITLIRELGQGSFGMVYEGLAKGVVKGEPETrVAIKTVNENASMRERIEFLNEASVMKEFNCHHVVRLLGVVSTG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 546 QPVCMLFEYMNQGDLHEFLimRSPHSDvgcssDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGE 625
Cdd:cd05032   82 QPTLVVMELMAKGDLKSYL--RSRRPE-----AENNPGLGPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 626 QLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMV 705
Cdd:cd05032  155 DLTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLAEQPYQGLSNEEVLKFV 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 223461072 706 RKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRLRS 748
Cdd:cd05032  235 IDGGHLDLPENCPDKLLELMRMCWQYNPKMRPTFLEIVSSLKD 277
CRD_TK_ROR2 cd07468
Cysteine-rich domain of tyrosine kinase-like orphan receptor 2; The cysteine-rich domain (CRD) ...
166-303 6.91e-86

Cysteine-rich domain of tyrosine kinase-like orphan receptor 2; The cysteine-rich domain (CRD) is an essential part of the tyrosine kinase-like orphan receptor (Ror2), a conserved family of tyrosine kinases that function in various processes, including neuronal and skeletal development, cell polarity, and cell movement. Ror proteins are receptors of Wnt proteins, which are key players in a number of fundamental cellular processes in embryogenesis and postnatal development. In different cellular contexts, Ror proteins can either activate or repress transcription of Wnt target genes, and can modulate Wnt signaling by sequestering Wnt ligands. In addition, a number of Wnt-independent functions have been proposed for both Ror1 and Ror2.


Pssm-ID: 143577  Cd Length: 140  Bit Score: 271.12  E-value: 6.91e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 166 EDGFCQPYRGIACARFIGNRTVYMESLHMQGEIENQITAAFTMIGTSSHLSDKCSQFAIPSLCHYAFPYCDETSSVPKPR 245
Cdd:cd07468    1 KDGFCQPYRGIACARFIGNRTIYVDSLQMQGEIENRITAAFTMIGTSTHLSDQCSQFAIPSFCHFVFPLCDDRSRTPKPR 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 223461072 246 DLCRDECEVLENVLCQTEYIFARSNPMILMRLKLPNCEDLPQPESPEAANCIRIGIPM 303
Cdd:cd07468   81 ELCRDECEVLENDLCRQEYNIARSNPLILMQLQLPKCEELPLPESPEAANCMRIGIPV 138
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
468-746 1.32e-81

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: 264.62  E-value: 1.32e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 468 LPLSAVRFMEELGECTFGKIYKGHLYLPGMDHAqLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQP 547
Cdd:cd05033    1 IDASYVTIEKVIGGGEFGEVCSGSLKLPGKKEI-DVAIKTLKSGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 548 VCMLFEYMNQGDLHEFLimrsphsdvgcsSDEDGTVKSsldhGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQL 627
Cdd:cd05033   80 VMIVTEYMENGSLDKFL------------RENDGKFTV----TQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 628 HVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRK 707
Cdd:cd05033  144 VCKVSDFGLSRRLEDSEATYTTKGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSYGERPYWDMSNQDVIKAVED 223
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 223461072 708 RQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd05033  224 GYRLPPPMDCPSALYQLMLDCWQKDRNERPTFSQIVSTL 262
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
466-746 4.78e-81

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: 263.48  E-value: 4.78e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 466 KELPLSAVRFMEELGECTFGKIYKGHLYLPGMDHAQL-VAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQ 544
Cdd:cd05036    1 KEVPRKNLTLIRALGQGAFGEVYEGTVSGMPGDPSPLqVAVKTLPELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 545 EQPVCMLFEYMNQGDLHEFLIMRSPHSdvgcssdedgTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILI- 623
Cdd:cd05036   81 RLPRFILLELMAGGDLKSFLRENRPRP----------EQPSSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLt 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 624 --GEQLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEV 701
Cdd:cd05036  151 ckGPGRVAKIGDFGMARDIYRADYYRKGGKAMLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSLGYMPYPGKSNQEV 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 223461072 702 IEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd05036  231 MEFVTSGGRMDPPKNCPGPVYRIMTQCWQHIPEDRPNFSTILERL 275
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
477-747 1.14e-80

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: 261.90  E-value: 1.14e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGhLYLPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGaVTQEQPVCMLFEYMN 556
Cdd:cd05060    1 KELGHGNFGSVRKG-VYLMKSGKEVEVAVKTLKQEHEKAGKKEFLREASVMAQLDHPCIVRLIG-VCKGEPLMLVMELAP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLIMRSPHSDVgcssdedgtvkssldhgDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGL 636
Cdd:cd05060   79 LGPLLKYLKKRREIPVS-----------------DLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGM 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 637 SREI-YSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPCSE 715
Cdd:cd05060  142 SRALgAGSDYYRATTAGRWPLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSYGAKPYGEMKGPEVIAMLESGERLPRPE 221
                        250       260       270
                 ....*....|....*....|....*....|..
gi 223461072 716 DCPPRMYSLMTECWNEIPSRRPRFKDIHVRLR 747
Cdd:cd05060  222 ECPQEIYSIMLSCWKYRPEDRPTFSELESTFR 253
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
478-748 5.75e-78

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: 255.74  E-value: 5.75e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 478 ELGECTFGKIYKGHLYLPGMDHAQ-LVAIKTLKDYNNPQQwTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMN 556
Cdd:cd05093   12 ELGEGAFGKVFLAECYNLCPEQDKiLVAVKTLKDASDNAR-KDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLIMRSPHSDVGCssdeDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGL 636
Cdd:cd05093   91 HGDLNKFLRAHGPDAVLMA----EGNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 637 SREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPCSED 716
Cdd:cd05093  167 SRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRT 246
                        250       260       270
                 ....*....|....*....|....*....|..
gi 223461072 717 CPPRMYSLMTECWNEIPSRRPRFKDIHVRLRS 748
Cdd:cd05093  247 CPKEVYDLMLGCWQREPHMRLNIKEIHSLLQN 278
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
467-748 3.70e-76

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: 251.07  E-value: 3.70e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIY------------KGHLYLPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPN 534
Cdd:cd05095    1 EFPRKLLTFKEKLGEGQFGEVHlceaegmekfmdKDFALEVSENQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 535 IVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSPHSDVGCSSDedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHK 614
Cdd:cd05095   81 IIRLLAVCITDDPLCMITEYMENGDLNQFLSRQQPEGQLALPSN-----ALTVSYSDLRFMAAQIASGMKYLSSLNFVHR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 615 DLAARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGL-QPY 693
Cdd:cd05095  156 DLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETLTFCReQPY 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223461072 694 YGFSNQEVIEMV------RKRQL-LPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRLRS 748
Cdd:cd05095  236 SQLSDEQVIENTgeffrdQGRQTyLPQPALCPDSVYKLMLSCWRRDTKDRPSFQEIHTLLQE 297
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
478-743 3.73e-75

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: 248.00  E-value: 3.73e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 478 ELGECTFGKIYKGHLY-LPGMDHAQLVAIKTLKDYNNPQQwTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMN 556
Cdd:cd05094   12 ELGEGAFGKVFLAECYnLSPTKDKMLVAVKTLKDPTLAAR-KDFQREAELLTNLQHDHIVKFYGVCGDGDPLIMVFEYMK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLIMRSPHSDVgCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGL 636
Cdd:cd05094   91 HGDLNKFLRAHGPDAMI-LVDGQPRQAKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIGDFGM 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 637 SREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPCSED 716
Cdd:cd05094  170 SRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQGRVLERPRV 249
                        250       260
                 ....*....|....*....|....*..
gi 223461072 717 CPPRMYSLMTECWNEIPSRRPRFKDIH 743
Cdd:cd05094  250 CPKEVYDIMLGCWQREPQQRLNIKEIY 276
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
467-748 5.83e-75

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: 246.49  E-value: 5.83e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGhLYLpgmdhAQLVAIKTLKDYNNPQQwtEFQQEASLMAELHHPNIVCLLGAVTQEQ 546
Cdd:cd05039    2 AINKKDLKLGELIGKGEFGDVMLG-DYR-----GQKVAVKCLKDDSTAAQ--AFLAEASVMTTLRHPNLVQLLGVVLEGN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 547 PVCMLFEYMNQGDLHEFLIMRSphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQ 626
Cdd:cd05039   74 GLYIVTEYMAKGSLVDYLRSRG---------------RAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSED 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 627 LHVKISDLGLSREIYSAdyyrvQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVR 706
Cdd:cd05039  139 NVAKVSDFGLAKEASSN-----QDGGKLPIKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPHVE 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 223461072 707 KRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRLRS 748
Cdd:cd05039  214 KGYRMEAPEGCPPEVYKVMKNCWELDPAKRPTFKQLREKLEH 255
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
467-748 3.76e-74

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: 245.66  E-value: 3.76e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIY----KGHLYLPGM------DHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIV 536
Cdd:cd05097    1 EFPRQQLRLKEKLGEGQFGEVHlceaEGLAEFLGEgapefdGQPVLVAVKMLRADVTKTARNDFLKEIKIMSRLKNPNII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 537 CLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSPHSDVGCSSDedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDL 616
Cdd:cd05097   81 RLLGVCVSDDPLCMITEYMENGDLNQFLSQREIESTFTHANN-----IPSVSIANLLYMAVQIASGMKYLASLNFVHRDL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 617 AARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSF-GLQPYYG 695
Cdd:cd05097  156 ATRNCLVGNHYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMAWESILLGKFTTASDVWAFGVTLWEMFTLcKEQPYSL 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 696 FSNQEVIEMV------RKRQL-LPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRLRS 748
Cdd:cd05097  236 LSDEQVIENTgeffrnQGRQIyLSQTPLCPSPVFKLMMRCWSRDIKDRPTFNKIHHFLRE 295
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
467-743 4.69e-74

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: 245.61  E-value: 4.69e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIykgHLY-------LPGMD--------HAQLVAIKTLKDYNNPQQWTEFQQEASLMAELH 531
Cdd:cd05096    1 KFPRGHLLFKEKLGEGQFGEV---HLCevvnpqdLPTLQfpfnvrkgRPLLVAVKILRPDANKNARNDFLKEVKILSRLK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 532 HPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSPHSDVGCSSDEDGTVKS--SLDHGDFLHIAIQIAAGMEYLSSH 609
Cdd:cd05096   78 DPNIIRLLGVCVDEDPLCMITEYMENGDLNQFLSSHHLDDKEENGNDAVPPAHClpAISYSSLLHVALQIASGMKYLSSL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 610 FFVHKDLAARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSF- 688
Cdd:cd05096  158 NFVHRDLATRNCLVGENLTIKIADFGMSRNLYAGDYYRIQGRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWEILMLc 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223461072 689 GLQPYYGFSNQEVIEMV------RKRQL-LPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIH 743
Cdd:cd05096  238 KEQPYGELTDEQVIENAgeffrdQGRQVyLFRPPPCPQGLYELMLQCWSRDCRERPSFSDIH 299
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
479-742 6.34e-74

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: 243.86  E-value: 6.34e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKG---HLYLPGMDHAQlVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYM 555
Cdd:cd05044    3 LGSGAFGEVFEGtakDILGDGSGETK-VAVKTLRKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILELM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQGDLHEFLIMRSPHSDVGCSsdedgtvkssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLH----VKI 631
Cdd:cd05044   82 EGGDLLSYLRAARPTAFTPPL----------LTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKDYrervVKI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 632 SDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLL 711
Cdd:cd05044  152 GDFGLARDIYKNDYYRKEGEGLLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEILTLGQQPYPARNNLEVLHFVRAGGRL 231
                        250       260       270
                 ....*....|....*....|....*....|.
gi 223461072 712 PCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05044  232 DQPDNCPDDLYELMLRCWSTDPEERPSFARI 262
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
468-742 2.51e-73

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: 242.76  E-value: 2.51e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 468 LPLSAVRFMEELGECTFGKIYKGhlYLPGMDHA---QLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQ 544
Cdd:cd05046    2 FPRSNLQEITTLGRGEFGEVFLA--KAKGIEEEggeTLVLVKALQKTKDENLQSEFRRELDMFRKLSHKNVVRLLGLCRE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 545 EQPVCMLFEYMNQGDLHEFLIMrsphsdvgcSSDEDGTVKSS-LDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILI 623
Cdd:cd05046   80 AEPHYMILEYTDLGDLKQFLRA---------TKSKDEKLKPPpLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 624 GEQLHVKISDLGLSREIYSADYYRVQsKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIE 703
Cdd:cd05046  151 SSQREVKVSLLSLSKDVYNSEYYKLR-NALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTQGELPFYGLSDEEVLN 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 223461072 704 MVRKRQL-LPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05046  230 RLQAGKLeLPVPEGCPSRLYKLMTRCWAVNPKDRPSFSEL 269
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
467-746 6.83e-73

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: 241.17  E-value: 6.83e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGhLYLPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTqEQ 546
Cdd:cd05056    2 EIQREDITLGRCIGEGQFGDVYQG-VYMSPENEKIAVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVIT-EN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 547 PVCMLFEYMNQGDLHEFLIMRsphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQ 626
Cdd:cd05056   80 PVWIVMELAPLGELRSYLQVN----------------KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 627 LHVKISDLGLSREIYSADYYRVqSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVR 706
Cdd:cd05056  144 DCVKLGDFGLSRYMEDESYYKA-SKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMLGVKPFQGVKNNDVIGRIE 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 223461072 707 KRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd05056  223 NGERLPMPPNCPPTLYSLMTKCWAYDPSKRPRFTELKAQL 262
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
477-746 1.01e-72

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: 239.88  E-value: 1.01e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGhLYLPGMDhaqlVAIKTLKdynnPQQWT--EFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd05034    1 KKLGAGQFGEVWMG-VWNGTTK----VAVKTLK----PGTMSpeAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTEL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQGDLHEFLimrsphsdvgcsSDEDGtvkSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd05034   72 MSKGSLLDYL------------RTGEG---RALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADF 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 635 GLSREIySADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPCS 714
Cdd:cd05034  137 GLARLI-EDDEYTAREGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTYGRVPYPGMTNREVLEQVERGYRMPKP 215
                        250       260       270
                 ....*....|....*....|....*....|..
gi 223461072 715 EDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd05034  216 PGCPDELYDIMLQCWKKEPEERPTFEYLQSFL 247
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
477-743 2.27e-72

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: 239.27  E-value: 2.27e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLYLPGMDhaqlVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMN 556
Cdd:cd05041    1 EKIGRGNFGDVYRGVLKPDNTE----VAVKTCRETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLimRSPhsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGL 636
Cdd:cd05041   77 GGSLLTFL--RKK--------------GARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGM 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 637 SREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPCSED 716
Cdd:cd05041  141 SREEEDGEYTVSDGLKQIPIKWTAPEALNYGRYTSESDVWSFGILLWEIFSLGATPYPGMSNQQTREQIESGYRMPAPEL 220
                        250       260
                 ....*....|....*....|....*..
gi 223461072 717 CPPRMYSLMTECWNEIPSRRPRFKDIH 743
Cdd:cd05041  221 CPEAVYRLMLQCWAYDPENRPSFSEIY 247
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
467-746 2.81e-72

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: 239.62  E-value: 2.81e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGhLYlpgmDHAQLVAIKTLK-DYNNPQqwtEFQQEASLMAELHHPNIVCLLGAVTQE 545
Cdd:cd05068    4 EIDRKSLKLLRKLGSGQFGEVWEG-LW----NNTTPVAVKTLKpGTMDPE---DFLREAQIMKKLRHPKLIQLYAVCTLE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 546 QPVCMLFEYMNQGDLHEFLimrspHSDvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGE 625
Cdd:cd05068   76 EPIYIITELMKHGSLLEYL-----QGK-----------GRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGE 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 626 QLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMV 705
Cdd:cd05068  140 NNICKVADFGLARVIKVEDEYEAREGAKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTYGRIPYPGMTNAEVLQQV 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 223461072 706 RKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd05068  220 ERGYRMPCPPNCPPQLYDIMLECWKADPMERPTFETLQWKL 260
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
467-742 4.75e-71

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: 236.93  E-value: 4.75e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGHLY--LPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAEL-HHPNIVCLLGAVT 543
Cdd:cd05053    8 ELPRDRLTLGKPLGEGAFGQVVKAEAVglDNKPNEVVTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNIINLLGACT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 544 QEQPVCMLFEYMNQGDLHEFLIMRSPHSDVgCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILI 623
Cdd:cd05053   88 QDGPLYVVVEYASKGNLREFLRARRPPGEE-ASPDDPRVPEEQLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVLV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 624 GEQLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIE 703
Cdd:cd05053  167 TEDNVMKIADFGLARDIHHIDYYRKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFK 246
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 223461072 704 MVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05053  247 LLKEGHRMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQL 285
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
479-746 3.01e-69

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: 231.16  E-value: 3.01e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLylpgMDHAQLVAIKTLKDYNNPQQwtEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQG 558
Cdd:cd05052   14 LGGGQYGEVYEGVW----KKYNLTVAVKTLKEDTMEVE--EFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 559 DLHEFLimRSPHsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSR 638
Cdd:cd05052   88 NLLDYL--RECN-------------REELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 639 eIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPCSEDCP 718
Cdd:cd05052  153 -LMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKGYRMERPEGCP 231
                        250       260
                 ....*....|....*....|....*...
gi 223461072 719 PRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd05052  232 PKVYELMRACWQWNPSDRPSFAEIHQAL 259
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
470-742 4.07e-68

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: 228.22  E-value: 4.07e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 470 LSAVRFMEELGECTFGKIYKGHLYLPGmDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVC 549
Cdd:cd05065    3 VSCVKIEEVIGAGEFGEVCRGRLKLPG-KREIFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 550 MLFEYMNQGDLHEFLimrsphsdvgcssdedgtvksSLDHGDFLHIAI-----QIAAGMEYLSSHFFVHKDLAARNILIG 624
Cdd:cd05065   82 IITEFMENGALDSFL---------------------RQNDGQFTVIQLvgmlrGIAAGMKYLSEMNYVHRDLAARNILVN 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 625 EQLHVKISDLGLSR---EIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEV 701
Cdd:cd05065  141 SNLVCKVSDFGLSRfleDDTSDPTYTSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDV 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 223461072 702 IEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05065  221 INAIEQDYRLPPPMDCPTALHQLMLDCWQKDRNLRPKFGQI 261
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
467-746 4.40e-68

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: 227.70  E-value: 4.40e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGhLYLpgmDHAQlVAIKTLKDYNNPQQwTEFQQEASLMAELHHPNIVCLLGAVTQEQ 546
Cdd:cd05148    2 ERPREEFTLERKLGSGYFGEVWEG-LWK---NRVR-VAIKILKSDDLLKQ-QDFQKEVQALKRLRHKHLISLFAVCSVGE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 547 PVCMLFEYMNQGDLHEFLimRSPhsdvgcssdeDGtvkSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQ 626
Cdd:cd05148   76 PVYIITELMEKGSLLAFL--RSP----------EG---QVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGED 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 627 LHVKISDLGLSReIYSADYYrVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVR 706
Cdd:cd05148  141 LVCKVADFGLAR-LIKEDVY-LSSDKKIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQVPYPGMNNHEVYDQIT 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 223461072 707 KRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd05148  219 AGYRMPCPAKCPQEIYKIMLECWAAEPEDRPSFKALREEL 258
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
479-746 4.97e-68

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: 227.04  E-value: 4.97e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLylpgmdHAQLVAIKTLK-DYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQ 557
Cdd:cd13999    1 IGSGSFGEVYKGKW------RGTDVAIKKLKvEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 558 GDLHEFLIMRSPHsdvgcssdedgtvkssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLS 637
Cdd:cd13999   75 GSLYDLLHKKKIP----------------LSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLS 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 638 REIysaDYYRVQSKSSL-PIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSN-QEVIEMVRKRQLLPCSE 715
Cdd:cd13999  139 RIK---NSTTEKMTGVVgTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLT-GEVPFKELSPiQIAAAVVQKGLRPPIPP 214
                        250       260       270
                 ....*....|....*....|....*....|.
gi 223461072 716 DCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd13999  215 DCPPELSKLIKRCWNEDPEKRPSFSEIVKRL 245
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
479-742 5.96e-68

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: 227.55  E-value: 5.96e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGMDHAQlVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQG 558
Cdd:cd05063   13 IGAGEFGEVFRGILKMPGRKEVA-VAIKTLKPGYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYMENG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 559 DLHEFLimrsphsdvgcsSDEDGTVkSSLDHGDFLHiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSR 638
Cdd:cd05063   92 ALDKYL------------RDHDGEF-SSYQLVGMLR---GIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 639 EIY---SADYyrVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPCSE 715
Cdd:cd05063  156 VLEddpEGTY--TTSGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSFGERPYWDMSNHEVMKAINDGFRLPAPM 233
                        250       260
                 ....*....|....*....|....*..
gi 223461072 716 DCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05063  234 DCPSAVYQLMLQCWQQDRARRPRFVDI 260
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
475-740 1.40e-67

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: 226.18  E-value: 1.40e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYKGhlYLPGMDHaqlVAIKTLKDYNNPQQwtEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd05059    8 FLKELGSGQFGVVHLG--KWRGKID---VAIKMIKEGSMSED--DFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQGDLHEFLIMRsphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd05059   81 MANGCLLNYLRER----------------RGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDF 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 635 GLSREIYSaDYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPCS 714
Cdd:cd05059  145 GLARYVLD-DEYTSSVGTKFPVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEGKMPYERFSNSEVVEHISQGYRLYRP 223
                        250       260
                 ....*....|....*....|....*.
gi 223461072 715 EDCPPRMYSLMTECWNEIPSRRPRFK 740
Cdd:cd05059  224 HLAPTEVYTIMYSCWHEKPEERPTFK 249
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
467-742 4.02e-67

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: 226.00  E-value: 4.02e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGHL--YLPGmDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQ 544
Cdd:cd05061    2 EVSREKITLLRELGQGSFGMVYEGNArdIIKG-EAETRVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 545 EQPVCMLFEYMNQGDLHEFLimRSPHSDvgcSSDEDGTVKSSLDhgDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIG 624
Cdd:cd05061   81 GQPTLVVMELMAHGDLKSYL--RSLRPE---AENNPGRPPPTLQ--EMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 625 EQLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEM 704
Cdd:cd05061  154 HDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKF 233
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 223461072 705 VRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05061  234 VMDGGYLDQPDNCPERVTDLMRMCWQFNPKMRPTFLEI 271
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
477-742 7.15e-66

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: 221.45  E-value: 7.15e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLYLPGMDHAQlVAIKTLKD--YNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQeQPVCMLFEY 554
Cdd:cd05040    1 EKLGDGSFGVVRRGEWTTPSGKVIQ-VAVKCLKSdvLSQPNAMDDFLKEVNAMHSLDHPNLIRLYGVVLS-SPLMMVTEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQGDLHEFLIMRSPHSDVgcssdedgtvkSSLdhgdfLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd05040   79 APLGSLLDRLRKDQGHFLI-----------STL-----CDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDF 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 635 GLSREIYSA-DYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMV-RKRQLLP 712
Cdd:cd05040  143 GLMRALPQNeDHYVMQEHRKVPFAWCAPESLKTRKFSHASDVWMFGVTLWEMFTYGEEPWLGLNGSQILEKIdKEGERLE 222
                        250       260       270
                 ....*....|....*....|....*....|
gi 223461072 713 CSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05040  223 RPDDCPQDIYNVMLQCWAHKPADRPTFVAL 252
CRD_TK_ROR_like cd07459
Cysteine-rich domain of tyrosine kinase-like orphan receptors; The cysteine-rich domain (CRD) ...
168-302 1.03e-65

Cysteine-rich domain of tyrosine kinase-like orphan receptors; The cysteine-rich domain (CRD) is an essential part of the tyrosine kinase-like orphan receptor (Ror) proteins, a conserved family of tyrosine kinases that function in various processes, including neuronal and skeletal development, cell polarity, and cell movement. Ror proteins are receptors of Wnt proteins, which are key players in a number of fundamental cellular processes in embryogenesis and postnatal development. In different cellular contexts, Ror proteins can either activate or repress transcription of Wnt target genes, and can modulate Wnt signaling by sequestering Wnt ligands. In addition, a number of Wnt-independent functions have been proposed for both Ror1 and Ror2.


Pssm-ID: 143568  Cd Length: 135  Bit Score: 216.49  E-value: 1.03e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 168 GFCQPYRGIACARFIGNRTVYMESLHMQGEIENQITAAFTMIGTSSHLSDKCSQFAIPSLCHYAFPYCDETSSVPKPRDL 247
Cdd:cd07459    1 GYCQPYRGSVCAKYLGNKSVYVTSKQTQEDIEEQLSAAFTVISTSSDVSPKCQQYALPSLCYYAFPLCDEGSSTPKPRRI 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 223461072 248 CRDECEVLENVLCQTEYIFARSNPMILMRLKLPNCEDLPQPESPEAANCIRIGIP 302
Cdd:cd07459   81 CRDECELLENDLCKKEYAIAKRHPLIGHQLLLPDCSSLPSPGSPESSNCIRLGIP 135
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
467-742 1.21e-65

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: 222.92  E-value: 1.21e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGHLYlpGM-----DHAQLVAIKTLKDYNNPQQWTEFQQEASLMAEL-HHPNIVCLLG 540
Cdd:cd05099    8 EFPRDRLVLGKPLGEGCFGQVVRAEAY--GIdksrpDQTVTVAVKMLKDNATDKDLADLISEMELMKLIgKHKNIINLLG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 541 AVTQEQPVCMLFEYMNQGDLHEFLIMRSPHS-----DVGCSSDEDGTVKssldhgDFLHIAIQIAAGMEYLSSHFFVHKD 615
Cdd:cd05099   86 VCTQEGPLYVIVEYAAKGNLREFLRARRPPGpdytfDITKVPEEQLSFK------DLVSCAYQVARGMEYLESRRCIHRD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 616 LAARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYG 695
Cdd:cd05099  160 LAARNVLVTEDNVMKIADFGLARGVHDIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTLGGSPYPG 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 223461072 696 FSNQEVIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05099  240 IPVEELFKLLREGHRMDKPSNCTHELYMLMRECWHAVPTQRPTFKQL 286
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
477-746 6.62e-65

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: 218.65  E-value: 6.62e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLYlpgMDHAqLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMN 556
Cdd:cd05084    2 ERIGRGNFGEVFSGRLR---ADNT-PVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLIMRSPHsdvgcssdedgtvkssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGL 636
Cdd:cd05084   78 GGDFLTFLRTEGPR----------------LKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGM 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 637 SREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPCSED 716
Cdd:cd05084  142 SREEEDGVYAATGGMKQIPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGAVPYANLSNQQTREAVEQGVRLPCPEN 221
                        250       260       270
                 ....*....|....*....|....*....|
gi 223461072 717 CPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd05084  222 CPDEVYRLMEQCWEYDPRKRPSFSTVHQDL 251
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
474-742 1.55e-64

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: 218.79  E-value: 1.55e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 474 RFMEELGECTFGKIYKGHLYLPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQ--EQPVCML 551
Cdd:cd05038    7 KFIKQLGEGHFGSVELCRYDPLGDNTGEQVAVKSLQPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESpgRRSLRLI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMNQGDLHEFLimrSPHSDvgcssdedgtvksSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKI 631
Cdd:cd05038   87 MEYLPSGSLRDYL---QRHRD-------------QIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 632 SDLGLSREI-YSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFG-------------LQPYYGFS 697
Cdd:cd05038  151 SDFGLAKVLpEDKEYYYVKEPGESPIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGdpsqsppalflrmIGIAQGQM 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 223461072 698 NQE-VIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05038  231 IVTrLLELLKSGERLPRPPSCPDEVYDLMKECWEYEPQDRPSFSDL 276
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
471-742 2.38e-64

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: 217.81  E-value: 2.38e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 471 SAVRFMEELGECTFGKIYKGHLYLPGMDHAQlVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCM 550
Cdd:cd05066    4 SCIKIEKVIGAGEFGEVCSGRLKLPGKREIP-VAIKTLKAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 551 LFEYMNQGDLHEFLimrsphsdvgcsSDEDG--TVKSsldhgdFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLH 628
Cdd:cd05066   83 VTEYMENGSLDAFL------------RKHDGqfTVIQ------LVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLV 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 629 VKISDLGLSREIY---SADYYRVQSKssLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMV 705
Cdd:cd05066  145 CKVSDFGLSRVLEddpEAAYTTRGGK--IPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWEMSNQDVIKAI 222
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 223461072 706 RKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05066  223 EEGYRLPAPMDCPAALHQLMLDCWQKDRNERPKFEQI 259
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
478-749 5.92e-63

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: 213.67  E-value: 5.92e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 478 ELGECTFGKIYKGhlYLPGMDHAQLVAIKTLK-DYNNPQQWTEFQQEASLMAELHHPNIVCLLGaVTQEQPVCMLFEYMN 556
Cdd:cd05116    2 ELGSGNFGTVKKG--YYQMKKVVKTVAVKILKnEANDPALKDELLREANVMQQLDNPYIVRMIG-ICEAESWMLVMEMAE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLimrsphsdvgcSSDEDGTVKSSLDhgdFLHiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGL 636
Cdd:cd05116   79 LGPLNKFL-----------QKNRHVTEKNITE---LVH---QVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 637 SREIYS-ADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPCSE 715
Cdd:cd05116  142 SKALRAdENYYKAQTHGKWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSYGQKPYKGMKGNEVTQMIEKGERMECPA 221
                        250       260       270
                 ....*....|....*....|....*....|....
gi 223461072 716 DCPPRMYSLMTECWNEIPSRRPRFKDIHVRLRSW 749
Cdd:cd05116  222 GCPPEMYDLMKLCWTYDVDERPGFAAVELRLRNY 255
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
479-742 2.74e-62

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: 212.90  E-value: 2.74e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLY-LPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQ 557
Cdd:cd05045    8 LGEGEFGKVVKATAFrLKGRAGYTTVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 558 GDLHEFLimrSPHSDVGCSSDEDGTVK--SSLDH--------GDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQL 627
Cdd:cd05045   88 GSLRSFL---RESRKVGPSYLGSDGNRnsSYLDNpderaltmGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLVAEGR 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 628 HVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRK 707
Cdd:cd05045  165 KMKISDFGLSRDVYEEDSYVKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIAPERLFNLLKT 244
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 223461072 708 RQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05045  245 GYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADI 279
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
477-748 1.72e-61

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: 209.48  E-value: 1.72e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLylpgmDHAQLVAIKTLKDyNNPQQWT-EFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYM 555
Cdd:cd05085    2 ELLGKGNFGEVYKGTL-----KDKTPVAVKTCKE-DLPQELKiKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQGDLHEFLIMRsphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLG 635
Cdd:cd05085   76 PGGDFLSFLRKK----------------KDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFG 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 636 LSRE----IYSADYYRvqsksSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLL 711
Cdd:cd05085  140 MSRQeddgVYSSSGLK-----QIPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVEKGYRM 214
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 223461072 712 PCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRLRS 748
Cdd:cd05085  215 SAPQRCPEDIYKIMQRCWDYNPENRPKFSELQKELAA 251
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
467-742 1.98e-61

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: 210.27  E-value: 1.98e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGHLYLPGMDHAQL-VAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQE 545
Cdd:cd05062    2 EVAREKITMSRELGQGSFGMVYEGIAKGVVKDEPETrVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 546 QPVCMLFEYMNQGDLHEFLimRSPHSDvgcssDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGE 625
Cdd:cd05062   82 QPTLVIMELMTRGDLKSYL--RSLRPE-----MENNPVQAPPSLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 626 QLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMV 705
Cdd:cd05062  155 DFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGMSNEQVLRFV 234
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 223461072 706 RKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05062  235 MEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEI 271
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
467-740 6.99e-61

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: 208.20  E-value: 6.99e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKI----YKGHlylpgmdhaQLVAIKTLKDynNPQQWTEFQQEASLMAELHHPNIVCLLGAV 542
Cdd:cd05067    3 EVPRETLKLVERLGAGQFGEVwmgyYNGH---------TKVAIKSLKQ--GSMSPDAFLAEANLMKQLQHQRLVRLYAVV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 543 TQEqPVCMLFEYMNQGDLHEFLimrspHSDVGcssdedgtvkSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNIL 622
Cdd:cd05067   72 TQE-PIYIITEYMENGSLVDFL-----KTPSG----------IKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANIL 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 623 IGEQLHVKISDLGLSREIYSADYyRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVI 702
Cdd:cd05067  136 VSDTLSCKIADFGLARLIEDNEY-TAREGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVI 214
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 223461072 703 EMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFK 740
Cdd:cd05067  215 QNLERGYRMPRPDNCPEELYQLMRLCWKERPEDRPTFE 252
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
465-742 2.83e-60

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: 206.88  E-value: 2.83e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 465 AKELPLSAVRFMEELGECTFGKIYKGHlYLPGMDHAQL-VAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVT 543
Cdd:cd05057    1 LRIVKETELEKGKVLGSGAFGTVYKGV-WIPEGEKVKIpVAIKVLREETGPKANEEILDEAYVMASVDHPHLVRLLGICL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 544 QEQpVCMLFEYMNQGDLHEFLimRSPhsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILI 623
Cdd:cd05057   80 SSQ-VQLITQLMPLGCLLDYV--RNH--------------RDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLV 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 624 GEQLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIE 703
Cdd:cd05057  143 KTPNHVKITDFGLAKLLDVDEKEYHAEGGKVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTFGAKPYEGIPAVEIPD 222
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 223461072 704 MVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05057  223 LLEKGERLPQPPICTIDVYMVLVKCWMIDAESRPTFKEL 261
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
479-746 1.05e-59

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: 205.54  E-value: 1.05e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGmDHAQLVAIKTLK-DYNNPQQWTEFQQEASLMAELHHPNIVCLLGA-----VTQEQPVCM-L 551
Cdd:cd05074   17 LGKGEFGSVREAQLKSED-GSFQKVAVKMLKaDIFSSSDIEEFLREAACMKEFDHPNVIKLIGVslrsrAKGRLPIPMvI 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMNQGDLHEFLIMrsphSDVGcssDEDGTVKSSLdhgdFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKI 631
Cdd:cd05074   96 LPFMKHGDLHTFLLM----SRIG---EEPFTLPLQT----LVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 632 SDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLL 711
Cdd:cd05074  165 ADFGLSKKIYSGDYYRQGCASKLPVKWLALESLADNVYTTHSDVWAFGVTMWEIMTRGQTPYAGVENSEIYNYLIKGNRL 244
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 223461072 712 PCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd05074  245 KQPPDCLEDVYELMCQCWSPEPKCRPSFQHLRDQL 279
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
461-742 2.86e-59

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: 205.25  E-value: 2.86e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 461 PKSKAKELPLSAVRFMEELGECTFGKIYKGHLYlpGMD-----HAQLVAIKTLKDYNNPQQWTEFQQEASLMAEL-HHPN 534
Cdd:cd05101   14 PEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAV--GIDkdkpkEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 535 IVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSPHS-----DVGCSSDEDGTVKssldhgDFLHIAIQIAAGMEYLSSH 609
Cdd:cd05101   92 IINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGmeysyDINRVPEEQMTFK------DLVSCTYQLARGMEYLASQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 610 FFVHKDLAARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFG 689
Cdd:cd05101  166 KCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLG 245
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 223461072 690 LQPYYGFSNQEVIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05101  246 GSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQL 298
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
471-739 4.68e-59

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: 202.87  E-value: 4.68e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 471 SAVRFMEELGECTFGKIYKGHLYlpgmdHAQLVAIKTLKDYNNPQQwtEFQQEASLMAELHHPNIVCLLGAVTQEQPVCM 550
Cdd:cd05112    4 SELTFVQEIGSGQFGLVHLGYWL-----NKDKVAIKTIREGAMSEE--DFIEEAEVMMKLSHPKLVQLYGVCLEQAPICL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 551 LFEYMNQGDLHEFLimrsphsdvgcssdedGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVK 630
Cdd:cd05112   77 VFEFMEHGCLSDYL----------------RTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVK 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 631 ISDLGLSREIYSaDYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQL 710
Cdd:cd05112  141 VSDFGMTRFVLD-DQYTSSTGTKFPVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDINAGFR 219
                        250       260
                 ....*....|....*....|....*....
gi 223461072 711 LPCSEDCPPRMYSLMTECWNEIPSRRPRF 739
Cdd:cd05112  220 LYKPRLASTHVYEIMNHCWKERPEDRPSF 248
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
468-746 5.55e-59

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: 202.41  E-value: 5.55e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 468 LPLSAVRFMEELGECTFGKIYKGHlYLpgmdhAQLVAIKTLKDYNNPQQwteFQQEASLMAELHHPNIVCLLGaVTQEQP 547
Cdd:cd05083    3 LNLQKLTLGEIIGEGEFGAVLQGE-YM-----GQKVAVKNIKCDVTAQA---FLEETAVMTKLQHKNLVRLLG-VILHNG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 548 VCMLFEYMNQGDLHEFLIMRSphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQL 627
Cdd:cd05083   73 LYIVMELMSKGNLVNFLRSRG---------------RALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDG 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 628 HVKISDLGLSREIYSADyyrvqSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRK 707
Cdd:cd05083  138 VAKISDFGLAKVGSMGV-----DNSRLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGRAPYPKMSVKEVKEAVEK 212
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 223461072 708 RQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd05083  213 GYRMEPPEGCPPDVYSIMTSCWEAEPGKRPSFKKLREKL 251
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
465-739 8.30e-59

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: 202.58  E-value: 8.30e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 465 AKELPLSAVRFMEELGECTFGKIYKGHlylpgMDHAQLVAIKTLKDYNNPQQwtEFQQEASLMAELHHPNIVCLLGAVTQ 544
Cdd:cd05072    1 AWEIPRESIKLVKKLGAGQFGEVWMGY-----YNNSTKVAVKTLKPGTMSVQ--AFLEEANLMKTLQHDKLVRLYAVVTK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 545 EQPVCMLFEYMNQGDLHEFLimrsphsdvgcSSDEDGTVKSSldhgDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIG 624
Cdd:cd05072   74 EEPIYIITEYMAKGSLLDFL-----------KSDEGGKVLLP----KLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVS 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 625 EQLHVKISDLGLSREIySADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEM 704
Cdd:cd05072  139 ESLMCKIADFGLARVI-EDNEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTYGKIPYPGMSNSDVMSA 217
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 223461072 705 VRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRF 739
Cdd:cd05072  218 LQRGYRMPRMENCPDELYDIMKTCWKEKAEERPTF 252
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
461-742 5.34e-58

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: 201.39  E-value: 5.34e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 461 PKSKAKELPLSAVRFMEELGECTFGKIYKGHLYlpGMDHAQ-----LVAIKTLKDYNNPQQWTEFQQEASLMAEL-HHPN 534
Cdd:cd05098    3 PEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAI--GLDKDKpnrvtKVAVKMLKSDATEKDLSDLISEMEMMKMIgKHKN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 535 IVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSPHSDVGCSsDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHK 614
Cdd:cd05098   81 IINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGMEYCY-NPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 615 DLAARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYY 694
Cdd:cd05098  160 DLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYP 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 223461072 695 GFSNQEVIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05098  240 GVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQL 287
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
472-747 5.41e-58

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: 200.37  E-value: 5.41e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 472 AVRFMEELGECTFGKIYKGhLYLPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQE-QPVCM 550
Cdd:cd05043    7 RVTLSDLLQEGTFGRIFHG-ILRDEKGKEEEVLVKTVKDHASEIQVTMLLQESSLLYGLSHQNLLPILHVCIEDgEKPMV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 551 LFEYMNQGDLHEFLimRSPhsdvgcsSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVK 630
Cdd:cd05043   86 LYPYMNWGNLKLFL--QQC-------RLSEANNPQALSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 631 ISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQL 710
Cdd:cd05043  157 ITDNALSRDLFPMDYHCLGDNENRPIKWMSLESLVNKEYSSASDVWSFGVLLWELMTLGQTPYVEIDPFEMAAYLKDGYR 236
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 223461072 711 LPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRLR 747
Cdd:cd05043  237 LAQPINCPDELFAVMACCWALDPEERPSFQQLVQCLT 273
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
461-742 8.40e-58

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: 202.17  E-value: 8.40e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 461 PKSKAKELPLSAVRFMEELGECTFGKIYKGHLYlpGMDH-----AQLVAIKTLKDYNNPQQWTEFQQEASLMAEL-HHPN 534
Cdd:cd05100    2 PADPKWELSRTRLTLGKPLGEGCFGQVVMAEAI--GIDKdkpnkPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 535 IVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSPhSDVGCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHK 614
Cdd:cd05100   80 IINLLGACTQDGPLYVLVEYASKGNLREYLRARRP-PGMDYSFDTCKLPEEQLTFKDLVSCAYQVARGMEYLASQKCIHR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 615 DLAARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYY 694
Cdd:cd05100  159 DLAARNVLVTEDNVMKIADFGLARDVHNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYP 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 223461072 695 GFSNQEVIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05100  239 GIPVEELFKLLKEGHRMDKPANCTHELYMIMRECWHAVPSQRPTFKQL 286
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
479-746 5.01e-57

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: 198.23  E-value: 5.01e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLP-GMDHAqlVAIKTLKDYNNPQ-QWTEFQQEASLMAELHHPNIVCLLGAV----TQEQPVCM-L 551
Cdd:cd14204   15 LGEGEFGSVMEGELQQPdGTNHK--VAVKTMKLDNFSQrEIEEFLSEAACMKDFNHPNVIRLLGVClevgSQRIPKPMvI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMNQGDLHEFLiMRSPHsdvgcssdEDGTVKSSLDHgdFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKI 631
Cdd:cd14204   93 LPFMKYGDLHSFL-LRSRL--------GSGPQHVPLQT--LLKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTVCV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 632 SDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLL 711
Cdd:cd14204  162 ADFGLSKKIYSGDYYRQGRIAKMPVKWIAVESLADRVYTVKSDVWAFGVTMWEIATRGMTPYPGVQNHEIYDYLLHGHRL 241
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 223461072 712 PCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd14204  242 KQPEDCLDELYDIMYSCWRSDPTDRPTFTQLRENL 276
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
478-749 8.31e-57

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: 196.71  E-value: 8.31e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 478 ELGECTFGKIYKGhlyLPGMDHAQL-VAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGaVTQEQPVCMLFEYMN 556
Cdd:cd05115   11 ELGSGNFGCVKKG---VYKMRKKQIdVAIKVLKQGNEKAVRDEMMREAQIMHQLDNPYIVRMIG-VCEAEALMLVMEMAS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLimrsphsdvgcSSDEDGTVKSSLdhGDFLHiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGL 636
Cdd:cd05115   87 GGPLNKFL-----------SGKKDEITVSNV--VELMH---QVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 637 SREIYSAD-YYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPCSE 715
Cdd:cd05115  151 SKALGADDsYYKARSAGKWPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSYGQKPYKKMKGPEVMSFIEQGKRMDCPA 230
                        250       260       270
                 ....*....|....*....|....*....|....
gi 223461072 716 DCPPRMYSLMTECWNEIPSRRPRFKDIHVRLRSW 749
Cdd:cd05115  231 ECPPEMYALMSDCWIYKWEDRPNFLTVEQRMRTY 264
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
479-739 2.11e-56

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: 195.83  E-value: 2.11e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLylPGMDHAQL-VAIKTLK-DYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQ-------PVC 549
Cdd:cd05035    7 LGEGEFGSVMEAQL--KQDDGSQLkVAVKTMKvDIHTYSEIEEFLSEAACMKDFDHPNVMRLIGVCFTASdlnkppsPMV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 550 MLfEYMNQGDLHEFLIMrsphsdvgcSSDEDGTVKSSLDhgDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHV 629
Cdd:cd05035   85 IL-PFMKHGDLHSYLLY---------SRLGGLPEKLPLQ--TLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 630 KISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQ 709
Cdd:cd05035  153 CVADFGLSRKIYSGDYYRQGRISKMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATRGQTPYPGVENHEIYDYLRNGN 232
                        250       260       270
                 ....*....|....*....|....*....|
gi 223461072 710 LLPCSEDCPPRMYSLMTECWNEIPSRRPRF 739
Cdd:cd05035  233 RLKQPEDCLDEVYFLMYFCWTVDPKDRPTF 262
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
479-739 9.21e-56

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: 193.84  E-value: 9.21e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHlYLPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLG-AVTQEQPVCMLFEYMNQ 557
Cdd:cd05058    3 IGKGHFGCVYHGT-LIDSDGQKIHCAVKSLNRITDIEEVEQFLKEGIIMKDFSHPNVLSLLGiCLPSEGSPLVVLPYMKH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 558 GDLHEFLimRSPhsdvgcssDEDGTVKssldhgDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLS 637
Cdd:cd05058   82 GDLRNFI--RSE--------THNPTVK------DLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLA 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 638 REIYSADYYRVQSKSS--LPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPCSE 715
Cdd:cd05058  146 RDIYDKEYYSVHNHTGakLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVDSFDITVYLLQGRRLLQPE 225
                        250       260
                 ....*....|....*....|....
gi 223461072 716 DCPPRMYSLMTECWNEIPSRRPRF 739
Cdd:cd05058  226 YCPDPLYEVMLSCWHPKPEMRPTF 249
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
467-743 1.34e-55

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: 193.22  E-value: 1.34e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGHLYLPGmDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQ 546
Cdd:cd05064    1 ELDNKSIKIERILGTGRFGELCRGCLKLPS-KRELPVAIHTLRAGCSDKQRRGFLAEALTLGQFDHSNIVRLEGVITRGN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 547 PVCMLFEYMNQGDLHEFLimrSPHsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQ 626
Cdd:cd05064   80 TMMIVTEYMSNGALDSFL---RKH-------------EGQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSD 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 627 LHVKISDLG-LSREIYSADYYRVQSKSslPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMV 705
Cdd:cd05064  144 LVCKISGFRrLQEDKSEAIYTTMSGKS--PVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSYGERPYWDMSGQDVIKAV 221
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 223461072 706 RKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIH 743
Cdd:cd05064  222 EDGFRLPAPRNCPNLLHQLMLDCWQKERGERPRFSQIH 259
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
478-740 1.58e-55

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: 192.44  E-value: 1.58e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 478 ELGECTFGKIYKGHlylpgMDHAQLVAIKTLKDYN-NPQQwteFQQEASLMAELHHPNIVCLLgAVTQEQPVCMLFEYMN 556
Cdd:cd14203    2 KLGQGCFGEVWMGT-----WNGTTKVAIKTLKPGTmSPEA---FLEEAQIMKKLRHDKLVQLY-AVVSEEPIYIVTEFMS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLimrsphsdvgcsSDEDGtvkSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGL 636
Cdd:cd14203   73 KGSLLDFL------------KDGEG---KYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGL 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 637 SREIYSADYYRVQSkSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPCSED 716
Cdd:cd14203  138 ARLIEDNEYTARQG-AKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPPG 216
                        250       260
                 ....*....|....*....|....
gi 223461072 717 CPPRMYSLMTECWNEIPSRRPRFK 740
Cdd:cd14203  217 CPESLHELMCQCWRKDPEERPTFE 240
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
468-747 1.75e-55

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: 192.89  E-value: 1.75e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 468 LPLSAVRFMEELGECTFGKIYKGhlylpgmDH-AQLVAIKTLKDYNNPQQwteFQQEASLMAELHHPNIVCLLGAVTQEQ 546
Cdd:cd05082    3 LNMKELKLLQTIGKGEFGDVMLG-------DYrGNKVAVKCIKNDATAQA---FLAEASVMTQLRHSNLVQLLGVIVEEK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 547 -PVCMLFEYMNQGDLHEFLIMRSphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGE 625
Cdd:cd05082   73 gGLYIVTEYMAKGSLVDYLRSRG---------------RSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSE 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 626 QLHVKISDLGLSREIYSadyyrVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMV 705
Cdd:cd05082  138 DNVAKVSDFGLTKEASS-----TQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPRV 212
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 223461072 706 RKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRLR 747
Cdd:cd05082  213 EKGYKMDAPDGCPPAVYDVMKNCWHLDAAMRPSFLQLREQLE 254
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
461-742 2.90e-55

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: 193.86  E-value: 2.90e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 461 PKSKAKELPLSAVRFMEELGECTFGKIYKGHLYlpGMDHAQL---VAIKTLKDYNNPQQWTEFQQEASLMAEL-HHPNIV 536
Cdd:cd05055   25 PYDLKWEFPRNNLSFGKTLGAGAFGKVVEATAY--GLSKSDAvmkVAVKMLKPTAHSSEREALMSELKIMSHLgNHENIV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 537 CLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDL 616
Cdd:cd05055  103 NLLGACTIGGPILVITEYCCYGDLLNFLRRKR---------------ESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 617 AARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGF 696
Cdd:cd05055  168 AARNVLLTHGKIVKICDFGLARDIMNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFSLGSNPYPGM 247
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 223461072 697 S-NQEVIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05055  248 PvDSKFYKLIKEGYRMAQPEHAPAEIYDIMKTCWDADPLKRPTFKQI 294
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
475-742 5.23e-55

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: 191.25  E-value: 5.23e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYKGHLylpgmdHAQL-VAIKTLKDYNNPQQwtEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFE 553
Cdd:cd05113    8 FLKELGTGQFGVVKYGKW------RGQYdVAIKMIKEGSMSED--EFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 554 YMNQGDLHEFLIMRSPHsdvgcssdedgtvkssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISD 633
Cdd:cd05113   80 YMANGCLLNYLREMRKR----------------FQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSD 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 634 LGLSREIYSaDYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPC 713
Cdd:cd05113  144 FGLSRYVLD-DEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSLGKMPYERFTNSETVEHVSQGLRLYR 222
                        250       260
                 ....*....|....*....|....*....
gi 223461072 714 SEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05113  223 PHLASEKVYTIMYSCWHEKADERPTFKIL 251
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
467-742 4.09e-54

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: 190.39  E-value: 4.09e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGHLY-LPGMDHAQLVAIKTLKDYNNPqqwTEFQqeaSLMAEL-------HHPNIVCL 538
Cdd:cd05054    3 EFPRDRLKLGKPLGRGAFGKVIQASAFgIDKSATCRTVAVKMLKEGATA---SEHK---ALMTELkilihigHHLNVVNL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 539 LGAVT-QEQPVCMLFEYMNQGDL--------HEFLIMRSPH-SDVGCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSS 608
Cdd:cd05054   77 LGACTkPGGPLMVIVEFCKFGNLsnylrskrEEFVPYRDKGaRDVEEEEDDDELYKEPLTLEDLICYSFQVARGMEFLAS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 609 HFFVHKDLAARNILIGEQLHVKISDLGLSREIYS-ADYYRvQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFS 687
Cdd:cd05054  157 RKCIHRDLAARNILLSENNVVKICDFGLARDIYKdPDYVR-KGDARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFS 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 223461072 688 FGLQPYYGFS-NQEVIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05054  236 LGASPYPGVQmDEEFCRRLKEGTRMRAPEYTTPEIYQIMLDCWHGEPKERPTFSEL 291
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
479-746 1.01e-53

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: 188.33  E-value: 1.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGMDHAqlVAIKTLKDYNNPQQWTEFQQEASLMAEL-HHPNIVCLLGAVTQEQPVCMLFEYMNQ 557
Cdd:cd05047    3 IGEGNFGQVLKARIKKDGLRMD--AAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 558 GDLHEFLIMRSPHSDVGCSSDEDGTVkSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLS 637
Cdd:cd05047   81 GNLLDFLRKSRVLETDPAFAIANSTA-STLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 638 ReiySADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPCSEDC 717
Cdd:cd05047  160 R---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNC 236
                        250       260
                 ....*....|....*....|....*....
gi 223461072 718 PPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd05047  237 DDEVYDLMRQCWREKPYERPSFAQILVSL 265
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
479-746 1.45e-53

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: 187.91  E-value: 1.45e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLylpGMDHAQL-VAIKTLK-DYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQE-------QPVC 549
Cdd:cd05075    8 LGEGEFGSVMEGQL---NQDDSVLkVAVKTMKiAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLQNtesegypSPVV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 550 MLfEYMNQGDLHEFLImrspHSDVGcssdeDGTVksSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHV 629
Cdd:cd05075   85 IL-PFMKHGDLHSFLL----YSRLG-----DCPV--YLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 630 KISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQ 709
Cdd:cd05075  153 CVADFGLSKKIYNGDYYRQGRISKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATRGQTPYPGVENSEIYDYLRQGN 232
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 223461072 710 LLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd05075  233 RLKQPPDCLDGLYELMSSCWLLNPKDRPSFETLRCEL 269
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
444-742 1.97e-52

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: 188.13  E-value: 1.97e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 444 KP---VRGQNVEMSMLNAYK-------PKSKAKELPLSAVRFMEELGECTFGKIYKGHLY-LPGMDHAQLVAIKTLKDYN 512
Cdd:cd05106    1 KPkyeIRWKIIEAAEGNNYTfidptqlPYNEKWEFPRDNLQFGKTLGAGAFGKVVEATAFgLGKEDNVLRVAVKMLKASA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 513 NPQQWTEFQQEASLMAEL-HHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFL--------------------------- 564
Cdd:cd05106   81 HTDEREALMSELKILSHLgQHKNIVNLLGACTHGGPVLVITEYCCYGDLLNFLrkkaetflnfvmalpeisetssdykni 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 565 ----------------------IMR---SPHSDVGCSSDEDGTVKS-SLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAA 618
Cdd:cd05106  161 tlekkyirsdsgfssqgsdtyvEMRpvsSSSSQSSDSKDEEDTEDSwPLDLDDLLRFSSQVAQGMDFLASKNCIHRDVAA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 619 RNILIGEQLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFS- 697
Cdd:cd05106  241 RNVLLTDGRVAKICDFGLARDIMNDSNYVVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGKSPYPGILv 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 223461072 698 NQEVIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05106  321 NSKFYKMVKRGYQMSRPDFAPPEIYSIMKMCWNLEPTERPTFSQI 365
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
474-742 4.68e-52

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 182.73  E-value: 4.68e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072   474 RFMEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFE 553
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDKKTG----KLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072   554 YMNQGDLHEFLIMRSPhsdvgcssdedgtvkssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISD 633
Cdd:smart00220  78 YCEGGDLFDLLKKRGR-----------------LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLAD 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072   634 LGLSREIYSADYYRVQSKSslpIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVI-EMVRKR--QL 710
Cdd:smart00220 141 FGLARQLDPGEKLTTFVGT---PEYMAPEVLLGKGYGKAVDIWSLGVILYELLT-GKPPFPGDDQLLELfKKIGKPkpPF 216
                          250       260       270
                   ....*....|....*....|....*....|..
gi 223461072   711 LPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:smart00220 217 PPPEWDISPEAKDLIRKLLVKDPEKRLTAEEA 248
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
473-746 6.63e-52

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: 184.05  E-value: 6.63e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 473 VRFMEELGECTFGKIYKGHLYLPGMDHAqlVAIKTLKDYNNPQQWTEFQQEASLMAEL-HHPNIVCLLGAVTQEQPVCML 551
Cdd:cd05089    4 IKFEDVIGEGNFGQVIKAMIKKDGLKMN--AAIKMLKEFASENDHRDFAGELEVLCKLgHHPNIINLLGACENRGYLYIA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMNQGDLHEFLIMRSPHSDVGCSSDEDGTVkSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKI 631
Cdd:cd05089   82 IEYAPYGNLLDFLRKSRVLETDPAFAKEHGTA-STLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 632 SDLGLSReiySADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLL 711
Cdd:cd05089  161 ADFGLSR---GEEVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRM 237
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 223461072 712 PCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd05089  238 EKPRNCDDEVYELMRQCWRDRPYERPPFSQISVQL 272
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
467-740 2.39e-51

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: 181.81  E-value: 2.39e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGhlylpGMDHAQLVAIKTLKDYN-NPQQwteFQQEASLMAELHHPNIVCLLgAVTQE 545
Cdd:cd05070    5 EIPRESLQLIKRLGNGQFGEVWMG-----TWNGNTKVAIKTLKPGTmSPES---FLEEAQIMKKLKHDKLVQLY-AVVSE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 546 QPVCMLFEYMNQGDLHEFLimrsphsdvgcssdEDGTVKSsLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGE 625
Cdd:cd05070   76 EPIYIVTEYMSKGSLLDFL--------------KDGEGRA-LKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGN 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 626 QLHVKISDLGLSREIYSADYYRVQSkSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMV 705
Cdd:cd05070  141 GLICKIADFGLARLIEDNEYTARQG-AKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQV 219
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 223461072 706 RKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFK 740
Cdd:cd05070  220 ERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFE 254
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
465-749 3.06e-51

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: 181.42  E-value: 3.06e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 465 AKELPLSAVRFMEELGECTFGKIYKGhlylpGMDHAQLVAIKTLKDYN-NPQQwteFQQEASLMAELHHPNIVCLLgAVT 543
Cdd:cd05071    3 AWEIPRESLRLEVKLGQGCFGEVWMG-----TWNGTTRVAIKTLKPGTmSPEA---FLQEAQVMKKLRHEKLVQLY-AVV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 544 QEQPVCMLFEYMNQGDLHEFLimrsphsdvgcssdeDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILI 623
Cdd:cd05071   74 SEEPIYIVTEYMSKGSLLDFL---------------KGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILV 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 624 GEQLHVKISDLGLSREIYSADYYRVQSkSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIE 703
Cdd:cd05071  139 GENLVCKVADFGLARLIEDNEYTARQG-AKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLD 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 223461072 704 MVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRLRSW 749
Cdd:cd05071  218 QVERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDY 263
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
465-749 2.02e-50

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: 179.11  E-value: 2.02e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 465 AKELPLSAVRFMEELGECTFGKIYKGhlylpGMDHAQLVAIKTLKDYN-NPQQwteFQQEASLMAELHHPNIVCLLgAVT 543
Cdd:cd05069    6 AWEIPRESLRLDVKLGQGCFGEVWMG-----TWNGTTKVAIKTLKPGTmMPEA---FLQEAQIMKKLRHDKLVPLY-AVV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 544 QEQPVCMLFEYMNQGDLHEFLimrsphsdvgcsSDEDGtvkSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILI 623
Cdd:cd05069   77 SEEPIYIVTEFMGKGSLLDFL------------KEGDG---KYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILV 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 624 GEQLHVKISDLGLSREIYSADYYRVQSkSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIE 703
Cdd:cd05069  142 GDNLVCKIADFGLARLIEDNEYTARQG-AKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMVNREVLE 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 223461072 704 MVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRLRSW 749
Cdd:cd05069  221 QVERGYRMPCPQGCPESLHELMKLCWKKDPDERPTFEYIQSFLEDY 266
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
471-742 2.59e-50

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: 178.13  E-value: 2.59e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 471 SAVRFMEELGECTFGKIYKGHLylpgmdHAQL-VAIKTLKDYNNPQQwtEFQQEASLMAELHHPNIVCLLGAVTQEQPVC 549
Cdd:cd05114    4 SELTFMKELGSGLFGVVRLGKW------RAQYkVAIKAIREGAMSEE--DFIEEAKVMMKLTHPKLVQLYGVCTQQKPIY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 550 MLFEYMNQGDLHEFLIMRsphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHV 629
Cdd:cd05114   76 IVTEFMENGCLLNYLRQR----------------RGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVV 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 630 KISDLGLSREIYSaDYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQ 709
Cdd:cd05114  140 KVSDFGMTRYVLD-DQYTSSSGAKFPVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEGKMPFESKSNYEVVEMVSRGH 218
                        250       260       270
                 ....*....|....*....|....*....|...
gi 223461072 710 LLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05114  219 RLYRPKLASKSVYEVMYSCWHEKPEGRPTFADL 251
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
465-740 8.55e-50

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: 177.14  E-value: 8.55e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 465 AKELPLSAVRFMEELGECTFGKIYkghlyLPGMDHAQLVAIKTLKDynNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQ 544
Cdd:cd05073    5 AWEIPRESLKLEKKLGAGQFGEVW-----MATYNKHTKVAVKTMKP--GSMSVEAFLAEANVMKTLQHDKLVKLHAVVTK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 545 EqPVCMLFEYMNQGDLHEFLimrsphsdvgcSSDEDGTVKSSldhgDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIG 624
Cdd:cd05073   78 E-PIYIITEFMAKGSLLDFL-----------KSDEGSKQPLP----KLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVS 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 625 EQLHVKISDLGLSReIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEM 704
Cdd:cd05073  142 ASLVCKIADFGLAR-VIEDNEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRA 220
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 223461072 705 VRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFK 740
Cdd:cd05073  221 LERGYRMPRPENCPEELYNIMMRCWKNRPEERPTFE 256
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
466-742 5.96e-49

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: 175.21  E-value: 5.96e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 466 KELPLSAVRFmeeLGECTFGKIYKGhLYLPGMDHAQL-VAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGA--V 542
Cdd:cd05109    5 KETELKKVKV---LGSGAFGTVYKG-IWIPDGENVKIpVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVCRLLGIclT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 543 TQEQPVCMLFEYmnqgdlheflimrsphsdvGCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNIL 622
Cdd:cd05109   81 STVQLVTQLMPY-------------------GCLLDYVRENKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 623 IGEQLHVKISDLGLSR--EIYSADYYRVQSKssLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQE 700
Cdd:cd05109  142 VKSPNHVKITDFGLARllDIDETEYHADGGK--VPIKWMALESILHRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPARE 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 223461072 701 VIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05109  220 IPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFREL 261
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
468-746 1.74e-48

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: 174.42  E-value: 1.74e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 468 LPLSAVRFMEELGECTFGKIYKGHLYLPG--MDhaqlVAIKTLKDYNNPQQWTEFQQEASLMAEL-HHPNIVCLLGAVTQ 544
Cdd:cd05088    4 LEWNDIKFQDVIGEGNFGQVLKARIKKDGlrMD----AAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 545 EQPVCMLFEYMNQGDLHEFLiMRSPHSDVGCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIG 624
Cdd:cd05088   80 RGYLYLAIEYAPHGNLLDFL-RKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 625 EQLHVKISDLGLSReiySADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEM 704
Cdd:cd05088  159 ENYVAKIADFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEK 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 223461072 705 VRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd05088  236 LPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSL 277
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
479-742 3.58e-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: 170.53  E-value: 3.58e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQG 558
Cdd:cd00180    1 LGKGSFGKVYKARDKETG----KKVAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 559 DLHEFLIMRSPHsdvgcssdedgtvkssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSR 638
Cdd:cd00180   77 SLKDLLKENKGP----------------LSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAK 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 639 EIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIfsfglqpyygfsnqeviemvrkrqllpcsedcp 718
Cdd:cd00180  141 DLDSDDSLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL--------------------------------- 187
                        250       260
                 ....*....|....*....|....
gi 223461072 719 PRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd00180  188 EELKDLIRRMLQYDPKKRPSAKEL 211
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
473-746 4.55e-48

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: 172.89  E-value: 4.55e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 473 VRFMEELGECTFGKIYKGHlYLPGMDH-AQLVAIKTLKdYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQ--EQPVC 549
Cdd:cd14205    6 LKFLQQLGKGNFGSVEMCR-YDPLQDNtGEVVAVKKLQ-HSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSagRRNLR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 550 MLFEYMNQGDLHEFLimrSPHsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHV 629
Cdd:cd14205   84 LIMEYLPYGSLRDYL---QKH-------------KERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 630 KISDLGLSREI-YSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSF---GLQPYYGFSNQ------ 699
Cdd:cd14205  148 KIGDFGLTKVLpQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYiekSKSPPAEFMRMigndkq 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 223461072 700 ------EVIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd14205  228 gqmivfHLIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRV 280
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
467-746 1.07e-47

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: 173.65  E-value: 1.07e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGHLYlpGMDHA---QLVAIKTLKDYNNPQQWTEFQQEASLMAEL-HHPNIVCLLGAV 542
Cdd:cd14207    3 EFARERLKLGKSLGRGAFGKVVQASAF--GIKKSptcRVVAVKMLKEGATASEYKALMTELKILIHIgHHLNVVNLLGAC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 543 TQEQ-PVCMLFEYMNQGDLHEFLIMRS-----------------------------------PHSDVGCSS--------- 577
Cdd:cd14207   81 TKSGgPLMVIVEYCKYGNLSNYLKSKRdffvtnkdtslqeelikekkeaeptggkkkrlesvTSSESFASSgfqedksls 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 578 -------DEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIY-SADYYRvQ 649
Cdd:cd14207  161 dveeeeeDSGDFYKRPLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYkNPDYVR-K 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 650 SKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFS-NQEVIEMVRKRQLLPCSEDCPPRMYSLMTEC 728
Cdd:cd14207  240 GDARLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSLGASPYPGVQiDEDFCSKLKEGIRMRAPEFATSEIYQIMLDC 319
                        330
                 ....*....|....*...
gi 223461072 729 WNEIPSRRPRFKDIHVRL 746
Cdd:cd14207  320 WQGDPNERPRFSELVERL 337
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
467-746 2.87e-47

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: 172.47  E-value: 2.87e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGHLYlpGMDHA---QLVAIKTLKDYNNPQQWTEFQQEASLMAEL-HHPNIVCLLGAV 542
Cdd:cd05103    3 EFPRDRLKLGKPLGRGAFGQVIEADAF--GIDKTatcRTVAVKMLKEGATHSEHRALMSELKILIHIgHHLNVVNLLGAC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 543 TQEQ-PVCMLFEYMNQGDLHEFL---------------IMRSPHSDVG------------------------------CS 576
Cdd:cd05103   81 TKPGgPLMVIVEFCKFGNLSAYLrskrsefvpyktkgaRFRQGKDYVGdisvdlkrrldsitssqssassgfveekslSD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 577 SDED-----GTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYS-ADYYRvQS 650
Cdd:cd05103  161 VEEEeagqeDLYKDFLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKdPDYVR-KG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 651 KSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFS-NQEVIEMVRKRQLLPCSEDCPPRMYSLMTECW 729
Cdd:cd05103  240 DARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKiDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCW 319
                        330
                 ....*....|....*..
gi 223461072 730 NEIPSRRPRFKDIHVRL 746
Cdd:cd05103  320 HGEPSQRPTFSELVEHL 336
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
465-742 2.96e-47

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: 170.14  E-value: 2.96e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 465 AKELPLSAVRFMEELGECTFGKIYKGhLYLPGMDHAQL-VAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGA-- 541
Cdd:cd05111    1 ARIFKETELRKLKVLGSGVFGTVHKG-IWIPEGDSIKIpVAIKVIQDRSGRQSFQAVTDHMLAIGSLDHAYIVRLLGIcp 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 542 ------VTQEQPVCMLFEYMNQGdlheflimrsphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKD 615
Cdd:cd05111   80 gaslqlVTQLLPLGSLLDHVRQH-------------------------RGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRN 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 616 LAARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYG 695
Cdd:cd05111  135 LAARNVLLKSPSQVQVADFGVADLLYPDDKKYFYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTFGAEPYAG 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 223461072 696 FSNQEVIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05111  215 MRLAEVPDLLEKGERLAQPQICTIDVYMVMVKCWMIDENIRPTFKEL 261
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
479-742 3.32e-47

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: 171.36  E-value: 3.32e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGhLYLPGMDHAQL-VAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGA--------VTQEQPVC 549
Cdd:cd05108   15 LGSGAFGTVYKG-LWIPEGEKVKIpVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGIcltstvqlITQLMPFG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 550 MLFEYMNQgdlheflimrspHSDVGCSSDedgtvkssldhgdFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHV 629
Cdd:cd05108   94 CLLDYVRE------------HKDNIGSQY-------------LLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHV 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 630 KISDLGLSReIYSADYYRVQSKS-SLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKR 708
Cdd:cd05108  149 KITDFGLAK-LLGAEEKEYHAEGgKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKG 227
                        250       260       270
                 ....*....|....*....|....*....|....
gi 223461072 709 QLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05108  228 ERLPQPPICTIDVYMIMVKCWMIDADSRPKFREL 261
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
467-742 3.94e-46

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: 170.08  E-value: 3.94e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGHLY-LPGMDHAQLVAIKTLKDynnPQQWTEfqQEAsLMAEL-------HHPNIVCL 538
Cdd:cd05104   31 EFPRDRLRFGKTLGAGAFGKVVEATAYgLAKADSAMTVAVKMLKP---SAHSTE--REA-LMSELkvlsylgNHINIVNL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 539 LGAVTQEQPVCMLFEYMNQGDLHEFL-------------------------IMRSPHSD--------------------- 572
Cdd:cd05104  105 LGACTVGGPTLVITEYCCYGDLLNFLrrkrdsficpkfedlaeaalyrnllHQREMACDslneymdmkpsvsyvvptkad 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 573 ------VGCSSDEDGTVKS------SLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREI 640
Cdd:cd05104  185 krrgvrSGSYVDQDVTSEIleedelALDTEDLLSFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFGLARDI 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 641 YSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFS-NQEVIEMVRKRQLLPCSEDCPP 719
Cdd:cd05104  265 RNDSNYVVKGNARLPVKWMAPESIFECVYTFESDVWSYGILLWEIFSLGSSPYPGMPvDSKFYKMIKEGYRMDSPEFAPS 344
                        330       340
                 ....*....|....*....|...
gi 223461072 720 RMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05104  345 EMYDIMRSCWDADPLKRPTFKQI 367
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
466-742 4.08e-46

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: 167.94  E-value: 4.08e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 466 KELPLSAVRFmeeLGECTFGKIYKGhLYLPGMDHAQL-VAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGA--- 541
Cdd:cd05110    5 KETELKRVKV---LGSGAFGTVYKG-IWVPEGETVKIpVAIKILNETTGPKANVEFMDEALIMASMDHPHLVRLLGVcls 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 542 -----VTQEQPVCMLFEYMNQgdlheflimrspHSDvgcssdedgTVKSSLdhgdFLHIAIQIAAGMEYLSSHFFVHKDL 616
Cdd:cd05110   81 ptiqlVTQLMPHGCLLDYVHE------------HKD---------NIGSQL----LLNWCVQIAKGMMYLEERRLVHRDL 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 617 AARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGF 696
Cdd:cd05110  136 AARNVLVKSPNHVKITDFGLARLLEGDEKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGI 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 223461072 697 SNQEVIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05110  216 PTREIPDLLEKGERLPQPPICTIDVYMVMVKCWMIDADSRPKFKEL 261
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
467-742 5.31e-46

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: 168.62  E-value: 5.31e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGHLYlpGMDH---AQLVAIKTLKdynnpQQWTEFQQEAsLMAEL-------HHPNIV 536
Cdd:cd05102    3 EFPRDRLRLGKVLGHGAFGKVVEASAF--GIDKsssCETVAVKMLK-----EGATASEHKA-LMSELkilihigNHLNVV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 537 CLLGAVTQEQ-PVCMLFEYMNQGDLHEFLIM----------RSPH---------------------SDVGCSSDEDGTV- 583
Cdd:cd05102   75 NLLGACTKPNgPLMVIVEFCKYGNLSNFLRAkregfspyreRSPRtrsqvrsmveavradrrsrqgSDRVASFTESTSSt 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 584 -----------KSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYS-ADYYRvQSK 651
Cdd:cd05102  155 nqprqevddlwQSPLTMEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKdPDYVR-KGS 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 652 SSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFS-NQEVIEMVRKRQLLPCSEDCPPRMYSLMTECWN 730
Cdd:cd05102  234 ARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQiNEEFCQRLKDGTRMRAPEYATPEIYRIMLSCWH 313
                        330
                 ....*....|..
gi 223461072 731 EIPSRRPRFKDI 742
Cdd:cd05102  314 GDPKERPTFSDL 325
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
477-746 5.67e-45

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: 163.53  E-value: 5.67e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLYlPGMDHAQLVaIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMN 556
Cdd:cd05042    1 QEIGNGWFGKVLLGEIY-SGTSVAQVV-VKELKASANPKEQDTFLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFCD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLIMRSPHSdvgcSSDEDGTVkssldhgdFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGL 636
Cdd:cd05042   79 LGDLKAYLRSEREHE----RGDSDTRT--------LQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 637 SREIYSADYYRVQSKSSLPIRWMPPEAI--MYGKF-----SSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVI-EMVRKR 708
Cdd:cd05042  147 AHSRYKEDYIETDDKLWFPLRWTAPELVteFHDRLlvvdqTKYSNIWSLGVTLWELFENGAQPYSNLSDLDVLaQVVREQ 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 223461072 709 QL--------LPCSEdcppRMYSLMTECWNEiPSRRPRFKDIHVRL 746
Cdd:cd05042  227 DTklpkpqleLPYSD----RWYEVLQFCWLS-PEQRPAAEDVHLLL 267
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
484-746 6.44e-45

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: 162.95  E-value: 6.44e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 484 FGKIYKGhlylpgMDHAQLVAIKTLKDY--NNPQQWTE-FQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDL 560
Cdd:cd14061    7 FGKVYRG------IWRGEEVAVKAARQDpdEDISVTLEnVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGGAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 561 HEFLimrsphsdvgcssdedgtVKSSLDHGDFLHIAIQIAAGMEYLSSH---FFVHKDLAARNILIGEQLH--------V 629
Cdd:cd14061   81 NRVL------------------AGRKIPPHVLVDWAIQIARGMNYLHNEapvPIIHRDLKSSNILILEAIEnedlenktL 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 630 KISDLGLSREIYSADyyRVQSKSSLPirWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRKRQ 709
Cdd:cd14061  143 KITDFGLAREWHKTT--RMSAAGTYA--WMAPEVIKSSTFSKASDVWSYGVLLWELLT-GEVPYKGIDGLAVAYGVAVNK 217
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 223461072 710 L-LPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd14061  218 LtLPIPSTCPEPFAQLMKDCWQPDPHDRPSFADILKQL 255
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
473-748 1.51e-44

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: 162.76  E-value: 1.51e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 473 VRFMEELGECTFGKIYKgHLYLPGMDH-AQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQ--EQPVC 549
Cdd:cd05080    6 LKKIRDLGEGHFGKVSL-YCYDPTNDGtGEMVAVKALKADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEqgGKSLQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 550 MLFEYMNQGDLHEFLimrsPHSDVGCSSdedgtvkssldhgdFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHV 629
Cdd:cd05080   85 LIMEYVPLGSLRDYL----PKHSIGLAQ--------------LLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLV 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 630 KISDLGLSREIYSA-DYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEI-------------FSFGLQPYYG 695
Cdd:cd05080  147 KIGDFGLAKAVPEGhEYYRVREDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELlthcdssqspptkFLEMIGIAQG 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 223461072 696 FSNQ-EVIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRLRS 748
Cdd:cd05080  227 QMTVvRLIELLERGERLPCPDKCPQEVYHLMKNCWETEASFRPTFENLIPILKT 280
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
475-748 2.47e-44

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: 161.66  E-value: 2.47e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYKGHL---YLPgmdhAQLVaIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCML 551
Cdd:cd14206    1 YLQEIGNGWFGKVILGEIfsdYTP----AQVV-VKELRVSAGPLEQRKFISEAQPYRSLQHPNILQCLGLCTETIPFLLI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMNQGDLHEFLimRSPHSDVGCSSDedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKI 631
Cdd:cd14206   76 MEFCQLGDLKRYL--RAQRKADGMTPD-----LPTRDLRTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRI 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 632 SDLGLSREIYSADYYRVQSKSSLPIRWMPPEAI--MYGKF-----SSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEM 704
Cdd:cd14206  149 GDYGLSHNNYKEDYYLTPDRLWIPLRWVAPELLdeLHGNLivvdqSKESNVWSLGVTIWELFEFGAQPYRHLSDEEVLTF 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 223461072 705 VRKRQLLPCSEdcpPRM--------YSLMTECWNEiPSRRPRFKDIHVRLRS 748
Cdd:cd14206  229 VVREQQMKLAK---PRLklpyadywYEIMQSCWLP-PSQRPSVEELHLQLSY 276
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
474-742 4.76e-44

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: 161.25  E-value: 4.76e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 474 RFME---ELGECTFGKIYKGHLYLPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQE--QPV 548
Cdd:cd05079    4 RFLKrirDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 549 CMLFEYMNQGDLHEFLimrsPHSdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLH 628
Cdd:cd05079   84 KLIMEFLPSGSLKEYL----PRN------------KNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 629 VKISDLGLSREIYS-ADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFG-------------LQPYY 694
Cdd:cd05079  148 VKIGDFGLTKAIETdKEYYTVKDDLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTYCdsesspmtlflkmIGPTH 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 223461072 695 G-FSNQEVIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05079  228 GqMTVTRLVRVLEEGKRLPRPPNCPEEVYQLMRKCWEFQPSKRTTFQNL 276
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
473-746 3.64e-43

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: 158.52  E-value: 3.64e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 473 VRFMEELGECTFGKIYKGHLYLPGMDHAQLVAIKTLKdYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQ--EQPVCM 550
Cdd:cd05081    6 LKYISQLGKGNFGSVELCRYDPLGDNTGALVAVKQLQ-HSGPDQQRDFQREIQILKALHSDFIVKYRGVSYGpgRRSLRL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 551 LFEYMNQGDLHEFLIMRsphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVK 630
Cdd:cd05081   85 VMEYLPSGCLRDFLQRH----------------RARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 631 ISDLGLSREI-YSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSF---GLQPYYGFSNQ------- 699
Cdd:cd05081  149 IADFGLAKLLpLDKDYYVVREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTYcdkSCSPSAEFLRMmgcerdv 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 223461072 700 ----EVIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd05081  229 palcRLLELLEEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSALGPQL 279
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
311-393 3.88e-42

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


Pssm-ID: 214527  Cd Length: 83  Bit Score: 148.31  E-value: 3.88e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072   311 HKCYNSTGVDYRGTVSVTKSGRQCQPWNSQYPHTHSFTALRFPELNGGHSYCRNPGNQKEAPWCFTLDENFKSDLCDIPA 390
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80

                   ...
gi 223461072   391 CDS 393
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
310-392 2.26e-40

Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.


Pssm-ID: 238056  Cd Length: 83  Bit Score: 143.29  E-value: 2.26e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 310 NHKCYNSTGVDYRGTVSVTKSGRQCQPWNSQYPHTHSFTALRFPELNGGHSYCRNPGNQKEAPWCFTLDENFKSDLCDIP 389
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIP 80

                 ...
gi 223461072 390 ACD 392
Cdd:cd00108   81 RCE 83
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
461-739 7.86e-40

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: 152.49  E-value: 7.86e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 461 PKSKAKELPLSAVRFMEELGECTFGKIYKGHLYlpGMDHAQ---LVAIKTLKDYNNPQQWTEFQQEASLMAEL-HHPNIV 536
Cdd:cd05105   27 PYDSRWEFPRDGLVLGRILGSGAFGKVVEGTAY--GLSRSQpvmKVAVKMLKPTARSSEKQALMSELKIMTHLgPHLNIV 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 537 CLLGAVTQEQPVCMLFEYMNQGDL----H------------------------------------------EFLIMR--- 567
Cdd:cd05105  105 NLLGACTKSGPIYIITEYCFYGDLvnylHknrdnflsrhpekpkkdldifginpadestrsyvilsfenkgDYMDMKqad 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 568 -------------SPHSDVGCS---------SDEDGTVKSSL-DHG-------DFLHIAIQIAAGMEYLSSHFFVHKDLA 617
Cdd:cd05105  185 ttqyvpmleikeaSKYSDIQRSnydrpasykGSNDSEVKNLLsDDGseglttlDLLSFTYQVARGMEFLASKNCVHRDLA 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 618 ARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGF- 696
Cdd:cd05105  265 ARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMi 344
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 223461072 697 SNQEVIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRF 739
Cdd:cd05105  345 VDSTFYNKIKSGYRMAKPDHATQEVYDIMVKCWNSEPEKRPSF 387
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
475-746 1.68e-39

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: 147.83  E-value: 1.68e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYKGHLYlPGMDHAQLVaIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd05087    1 YLKEIGHGWFGKVFLGEVN-SGLSSTQVV-VKELKASASVQDQMQFLEEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQGDLHEFLimRSphsdvgCSSDEDGTVksslDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd05087   79 CPLGDLKGYL--RS------CRAAESMAP----DPLTLQRMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDY 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 635 GLSREIYSADYYRVQSKSSLPIRWMPPEAI--MYGKF-----SSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIE-MVR 706
Cdd:cd05087  147 GLSHCKYKEDYFVTADQLWVPLRWIAPELVdeVHGNLlvvdqTKQSNVWSLGVTIWELFELGNQPYRHYSDRQVLTyTVR 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 223461072 707 KRQL--------LPCSEdcppRMYSLMTECWNEiPSRRPRFKDIHVRL 746
Cdd:cd05087  227 EQQLklpkpqlkLSLAE----RWYEVMQFCWLQ-PEQRPTAEEVHLLL 269
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
461-739 1.83e-39

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: 151.32  E-value: 1.83e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 461 PKSKAKELPLSAVRFMEELGECTFGKIYKGHLYlpGMDHAQL---VAIKTLKDYNNPQQWTEFQQEASLMAELH-HPNIV 536
Cdd:cd05107   27 PYDSAWEMPRDNLVLGRTLGSGAFGRVVEATAH--GLSHSQStmkVAVKMLKSTARSSEKQALMSELKIMSHLGpHLNIV 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 537 CLLGAVTQEQPVCMLFEYMNQGDL--------HEFL---------------------------IMRSPHSDVG---CSSD 578
Cdd:cd05107  105 NLLGACTKGGPIYIITEYCRYGDLvdylhrnkHTFLqyyldknrddgslisggstplsqrkshVSLGSESDGGymdMSKD 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 579 ED----------GTVKSS---------------------------------LDHGDFLHIAIQIAAGMEYLSSHFFVHKD 615
Cdd:cd05107  185 ESadyvpmqdmkGTVKYAdiessnyespydqylpsapertrrdtlinespaLSYMDLVGFSYQVANGMEFLASKNCVHRD 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 616 LAARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYG 695
Cdd:cd05107  265 LAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNNLYTTLSDVWSFGILLWEIFTLGGTPYPE 344
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 223461072 696 FS-NQEVIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRF 739
Cdd:cd05107  345 LPmNEQFYNAIKRGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDF 389
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
473-748 3.52e-39

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: 146.71  E-value: 3.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 473 VRFMEELGECTFGKIYKGHLylpgmdHAQLVAIKTLK---DYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVC 549
Cdd:cd14147    5 LRLEEVIGIGGFGKVYRGSW------RGELVAVKAARqdpDEDISVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 550 MLFEYMNQGDLHEFLIMRS--PHSdvgcssdedgtvkssldhgdFLHIAIQIAAGMEYLSSHFFV---HKDLAARNILIG 624
Cdd:cd14147   79 LVMEYAAGGPLSRALAGRRvpPHV--------------------LVNWAVQIARGMHYLHCEALVpviHRDLKSNNILLL 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 625 --------EQLHVKISDLGLSREIYSAdyyrVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGF 696
Cdd:cd14147  139 qpienddmEHKTLKITDFGLAREWHKT----TQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLT-GEVPYRGI 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 223461072 697 SNQEVIEMVRKRQL-LPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRLRS 748
Cdd:cd14147  214 DCLAVAYGVAVNKLtLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEA 266
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
475-743 5.11e-39

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: 146.16  E-value: 5.11e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYKGHLYlPGMDHAQLVaIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd05086    1 YIQEIGNGWFGKVLLGEIY-TGTSVARVV-VKELKASANPKEQDDFLQQGEPYYILQHPNILQCVGQCVEAIPYLLVFEF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQGDLHEFLimrsphsdvgcsSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd05086   79 CDLGDLKTYL------------ANQQEKLRGDSQIMLLQRMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDY 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 635 GLSREIYSADYYRVQSKSSLPIRWMPPE-------AIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVI-EMVR 706
Cdd:cd05086  147 GIGFSRYKEDYIETDDKKYAPLRWTAPElvtsfqdGLLAAEQTKYSNIWSLGVTLWELFENAAQPYSDLSDREVLnHVIK 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 223461072 707 KRQL--------LPCSEdcppRMYSLMTECWNEiPSRRPRFKDIH 743
Cdd:cd05086  227 ERQVklfkphleQPYSD----RWYEVLQFCWLS-PEKRPTAEEVH 266
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
479-746 1.63e-38

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: 144.52  E-value: 1.63e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKG-HLYLPGMdhaqlVAIKTLK-DYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMN 556
Cdd:cd13978    1 LGSGGFGTVSKArHVSWFGM-----VAIKCLHsSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYME 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLIMrsphsdvgcssdEDGTVKSSLdHGDFLHiaiQIAAGMEYLSSHF--FVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd13978   76 NGSLKSLLER------------EIQDVPWSL-RFRIIH---EIALGMNFLHNMDppLLHHDLKPENILLDNHFHVKISDF 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 635 GLSR---EIYSADYYRVQSKSSLPIRWMPPEAI--MYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIeMVRKRQ 709
Cdd:cd13978  140 GLSKlgmKSISANRRRGTENLGGTPIYMAPEAFddFNKKPTSKSDVYSFAIVIWAVLT-RKEPFENAINPLLI-MQIVSK 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 223461072 710 -----LLPCSEDC----PPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd13978  218 gdrpsLDDIGRLKqienVQELISLMIRCWDGNPDARPTFLECLDRL 263
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
467-742 6.93e-38

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: 142.87  E-value: 6.93e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGhlyLPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQ 546
Cdd:cd14145    2 EIDFSELVLEEIIGIGGFGKVYRA---IWIGDEVAVKAARHDPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 547 PVCMLFEYMNQGDLHEFLIMRSPHSDVgcssdedgtvkssldhgdFLHIAIQIAAGMEYLSSHFFV---HKDLAARNILI 623
Cdd:cd14145   79 NLCLVMEFARGGPLNRVLSGKRIPPDI------------------LVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILI 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 624 GEQLH--------VKISDLGLSREiysadYYRVQSKSSL-PIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYY 694
Cdd:cd14145  141 LEKVEngdlsnkiLKITDFGLARE-----WHRTTKMSAAgTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLT-GEVPFR 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 223461072 695 GFSNQEVIEMVRKRQL-LPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14145  215 GIDGLAVAYGVAMNKLsLPIPSTCPEPFARLMEDCWNPDPHSRPPFTNI 263
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
479-742 2.48e-37

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: 141.33  E-value: 2.48e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLylpgmdHAQLVAIKTLKdyNNPQQ-----WTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFE 553
Cdd:cd14146    2 IGVGGFGKVYRATW------KGQEVAVKAAR--QDPDEdikatAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVME 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 554 YMNQGDLHEFLimrsphsdVGCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFV---HKDLAARNILIGEQLH-- 628
Cdd:cd14146   74 FARGGTLNRAL--------AAANAAPGPRRARRIPPHILVNWAVQIARGMLYLHEEAVVpilHRDLKSSNILLLEKIEhd 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 629 ------VKISDLGLSREiysadYYRVQSKSSL-PIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEV 701
Cdd:cd14146  146 dicnktLKITDFGLARE-----WHRTTKMSAAgTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLT-GEVPYRGIDGLAV 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 223461072 702 IEMVRKRQL-LPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14146  220 AYGVAVNKLtLPIPSTCPEPFAKLMKECWEQDPHIRPSFALI 261
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
479-742 3.03e-37

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: 141.26  E-value: 3.03e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLylpgmDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQG 558
Cdd:cd14066    1 IGSGGFGTVYKGVL-----ENGTVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 559 DLHEFLimrsphsdvGCS-SDEDGTVKSSLDhgdflhIAIQIAAGMEYLSSHFF---VHKDLAARNILIGEQLHVKISDL 634
Cdd:cd14066   76 SLEDRL---------HCHkGSPPLPWPQRLK------IAKGIARGLEYLHEECPppiIHGDIKSSNILLDEDFEPKLTDF 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 635 GLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPY-------------------YG 695
Cdd:cd14066  141 GLARLIPPSESVSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLT-GKPAVdenrenasrkdlvewveskGK 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 223461072 696 FSNQEVIEMvRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14066  220 EELEDILDK-RLVDDDGVEEEEVEALLRLALLCTRSDPSLRPSMKEV 265
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
479-746 4.06e-37

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: 140.51  E-value: 4.06e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGhlylpgMDHAQLVAIKTLKdyNNPQQ-----WTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFE 553
Cdd:cd14148    2 IGVGGFGKVYKG------LWRGEEVAVKAAR--QDPDEdiavtAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVME 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 554 YMNQGDLHEFLIMRS--PHSdvgcssdedgtvkssldhgdFLHIAIQIAAGMEYLSSHFFV---HKDLAARNILIGEQLH 628
Cdd:cd14148   74 YARGGALNRALAGKKvpPHV--------------------LVNWAVQIARGMNYLHNEAIVpiiHRDLKSSNILILEPIE 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 629 --------VKISDLGLSREiysadYYRVQSKSSL-PIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQ 699
Cdd:cd14148  134 nddlsgktLKITDFGLARE-----WHKTTKMSAAgTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLT-GEVPYREIDAL 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 223461072 700 EVIEMVRKRQL-LPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd14148  208 AVAYGVAMNKLtLPIPSTCPEPFARLLEECWDPDPHGRPDFGSILKRL 255
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
479-742 3.29e-36

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: 136.86  E-value: 3.29e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLylpgmdHAQLVAIKTLKDynnpQQWTEFQQeaslMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQG 558
Cdd:cd14059    1 LGSGAQGAVFLGKF------RGEEVAVKKVRD----EKETDIKH----LRKLNHPNIIKFKGVCTQAPCYCILMEYCPYG 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 559 DLHEFLIMRSPhsdvgcssdedgtVKSSLdhgdFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSR 638
Cdd:cd14059   67 QLYEVLRAGRE-------------ITPSL----LVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSK 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 639 EiysadYYRVQSKSSLP--IRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRKRQL-LPCSE 715
Cdd:cd14059  130 E-----LSEKSTKMSFAgtVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLT-GEIPYKDVDSSAIIWGVGSNSLqLPVPS 203
                        250       260
                 ....*....|....*....|....*..
gi 223461072 716 DCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14059  204 TCPDGFKLLMKQCWNSKPRNRPSFRQI 230
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
475-746 1.82e-35

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: 135.69  E-value: 1.82e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYKGHLYLPGMDHAQLVAIkTLK--DYNNPQQWTEFQQEASLMAELHHPNIVCLLGaVTQEQPVCMLF 552
Cdd:cd05037    3 FHEHLGQGTFTNIYDGILREVGDGRVQEVEV-LLKvlDSDHRDISESFFETASLMSQISHKHLVKLYG-VCVADENIMVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 EYMNQGDLHEFLIMRSPHSDVGCssdedgtvkssldhgdFLHIAIQIAAGMEYLSSHFFVHKDLAARNILI------GEQ 626
Cdd:cd05037   81 EYVRYGPLDKYLRRMGNNVPLSW----------------KLQVAKQLASALHYLEDKKLIHGNVRGRNILLaregldGYP 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 627 LHVKISDLGLSREIYSADYyRVqskssLPIRWMPPEAI--MYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEM 704
Cdd:cd05037  145 PFIKLSDPGVPITVLSREE-RV-----DRIPWIAPECLrnLQANLTIAADKWSFGTTLWEICSGGEEPLSALSSQEKLQF 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 223461072 705 VRKRQLLPcSEDCPPrMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd05037  219 YEDQHQLP-APDCAE-LAELIMQCWTYEPTKRPSFRAILRDL 258
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
479-742 5.53e-34

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: 131.02  E-value: 5.53e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLylpgmdHAQLVAIKTLKDYNNPQqwtEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQG 558
Cdd:cd14058    1 VGRGSFGVVCKARW------RNQIVAVKIIESESEKK---AFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 559 DLHEFLimrspHSDvgcssdeDGTVKSSLDHGdfLHIAIQIAAGMEYLSSHF---FVHKDLAARNILIGEQLHV-KISDL 634
Cdd:cd14058   72 SLYNVL-----HGK-------EPKPIYTAAHA--MSWALQCAKGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTVlKICDF 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 635 GLSREIYSadyYRVQSKSSLPirWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPY--YGFSNQEVIEMVRKRQLLP 712
Cdd:cd14058  138 GTACDIST---HMTNNKGSAA--WMAPEVFEGSKYSEKCDVFSWGIILWEVIT-RRKPFdhIGGPAFRIMWAVHNGERPP 211
                        250       260       270
                 ....*....|....*....|....*....|
gi 223461072 713 CSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14058  212 LIKNCPKPIESLMTRCWSKDPEKRPSMKEI 241
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
477-738 6.31e-34

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: 131.17  E-value: 6.31e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHlylpgmdHAQL---VAIKTLK--DYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCML 551
Cdd:cd14014    6 RLLGRGGMGEVYRAR-------DTLLgrpVAIKVLRpeLAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMNQGDLHEFLIMRSPhsdvgcssdedgtvkssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKI 631
Cdd:cd14014   79 MEYVEGGSLADLLRERGP-----------------LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 632 SDLGLSREIYSADYYRVQSKS-SLPirWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRKRQL 710
Cdd:cd14014  142 TDFGIARALGDSGLTQTGSVLgTPA--YMAPEQARGGPVDPRSDIYSLGVVLYELLT-GRPPFDGDSPAAVLAKHLQEAP 218
                        250       260       270
                 ....*....|....*....|....*....|.
gi 223461072 711 LPCSE---DCPPRMYSLMTECWNEIPSRRPR 738
Cdd:cd14014  219 PPPSPlnpDVPPALDAIILRALAKDPEERPQ 249
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
479-747 6.44e-33

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: 127.89  E-value: 6.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPgmdhaqlVAIKTLKDYN-NPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQpVCMLFEYMNQ 557
Cdd:cd14062    1 IGSGSFGTVYKGRWHGD-------VAVKKLNVTDpTPSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQ-LAIVTQWCEG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 558 GDLHEFLIMRSPHSDVGcssdedgtvkssldhgDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLS 637
Cdd:cd14062   73 SSLYKHLHVLETKFEML----------------QLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLA 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 638 --REIYSADYYRVQSKSSlpIRWMPPEAI-MYGK--FSSDSDIWSFGVVLWEIFSFGLqPYYGFSNQE-VIEMVRKRQLL 711
Cdd:cd14062  137 tvKTRWSGSQQFEQPTGS--ILWMAPEVIrMQDEnpYSFQSDVYAFGIVLYELLTGQL-PYSHINNRDqILFMVGRGYLR 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 223461072 712 P----CSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRLR 747
Cdd:cd14062  214 PdlskVRSDTPKALRRLMEDCIKFQRDERPLFPQILASLE 253
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
480-742 6.08e-32

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: 125.07  E-value: 6.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 480 GECTFGKIYKGHLylpgMDHAQLVAIKTLkdynnpqqwTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGD 559
Cdd:cd14060    2 GGGSFGSVYRAIW----VSQDKEVAVKKL---------LKIEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGS 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 560 LHEFLimrsphsdvgcSSDEdgtvKSSLDHGDFLHIAIQIAAGMEYLSSHF---FVHKDLAARNILIGEQLHVKISDLGL 636
Cdd:cd14060   69 LFDYL-----------NSNE----SEEMDMDQIMTWATDIAKGMHYLHMEApvkVIHRDLKSRNVVIAADGVLKICDFGA 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 637 SReiYSADYYRVQSKSSLPirWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLqPYYGFSNQEVIEMV-RKRQLLPCSE 715
Cdd:cd14060  134 SR--FHSHTTHMSLVGTFP--WMAPEVIQSLPVSETCDTYSYGVVLWEMLTREV-PFKGLEGLQVAWLVvEKNERPTIPS 208
                        250       260
                 ....*....|....*....|....*..
gi 223461072 716 DCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14060  209 SCPRSFAELMRRCWEADVKERPSFKQI 235
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
477-699 6.73e-32

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: 125.33  E-value: 6.73e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGhlylpgMDHA--QLVAIKTLKDYNNPQQWTE-FQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFE 553
Cdd:cd06606    6 ELLGKGSFGSVYLA------LNLDtgELMAVKEVELSGDSEEELEaLEREIRILSSLKHPNIVRYLGTERTENTLNIFLE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 554 YMNQGDLHEFLIMrsphsdvgCSSDEDGTVKSsldhgdflhIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISD 633
Cdd:cd06606   80 YVPGGSLASLLKK--------FGKLPEPVVRK---------YTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLAD 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223461072 634 LGLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQ 699
Cdd:cd06606  143 FGCAKRLAEIATGEGTKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMAT-GKPPWSELGNP 207
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
473-737 4.78e-31

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: 122.70  E-value: 4.78e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 473 VRFMEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKdYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLF 552
Cdd:cd05122    2 FEILEKIGKGGFGVVYKARHKKTG----QIVAIKKIN-LESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 EYMNQGDLHEFLimrsphsdvgcssdeDGTVKsSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKIS 632
Cdd:cd05122   77 EFCSGGSLKDLL---------------KNTNK-TLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLI 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 633 DLGLSREIysadyyrvqSKSSLPIR------WMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVIEMVR 706
Cdd:cd05122  141 DFGLSAQL---------SDGKTRNTfvgtpyWMAPEVIQGKPYGFKADIWSLGITAIEMA-EGKPPYSELPPMKALFLIA 210
                        250       260       270
                 ....*....|....*....|....*....|...
gi 223461072 707 KRQL--LPCSEDCPPRMYSLMTECWNEIPSRRP 737
Cdd:cd05122  211 TNGPpgLRNPKKWSKEFKDFLKKCLQKDPEKRP 243
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
484-747 3.94e-30

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: 120.30  E-value: 3.94e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 484 FGKIYKGHLYLPGmdhaqLVAIKTLkdYNNPQQwTEFQ----QEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGD 559
Cdd:cd14027    6 FGKVSLCFHRTQG-----LVVLKTV--YTGPNC-IEHNeallEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 560 LHEFL-IMRSPHSdvgcssdedgtVKSsldhgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGL-S 637
Cdd:cd14027   78 LMHVLkKVSVPLS-----------VKG--------RIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLaS 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 638 REIYSA---DYYRVQSK-------SSLPIRWMPPEAI--MYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMV 705
Cdd:cd14027  139 FKMWSKltkEEHNEQREvdgtakkNAGTLYYMAPEHLndVNAKPTEKSDVYSFAIVLWAIFA-NKEPYENAINEDQIIMC 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 223461072 706 RKRQLLPCSED----CPPRMYSLMTECWNEIPSRRPRFKDIHVRLR 747
Cdd:cd14027  218 IKSGNRPDVDDiteyCPREIIDLMKLCWEANPEARPTFPGIEEKFR 263
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
476-707 4.11e-30

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: 120.05  E-value: 4.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGHLYLPGmdhaQLVAIK-TLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd14002    6 LELIGEGSFGKVYKGRRKYTG----QVVALKfIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MnQGDLHEFLimrsphsdvgcssDEDGTVKSSLDHGdflhIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd14002   82 A-QGELFQIL-------------EDDGTLPEEEVRS----IAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDF 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223461072 635 GLSREIySADYYRVQSKSSLPIrWMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVIEMVRK 707
Cdd:cd14002  144 GFARAM-SCNTLVLTSIKGTPL-YMAPELVQEQPYDHTADLWSLGCILYELF-VGQPPFYTNSIYQLVQMIVK 213
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
477-720 2.01e-29

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 123.20  E-value: 2.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHlylpgmDHA--QLVAIKTLK-DYNNPQQWTE-FQQEASLMAELHHPNIVCLLGAVTQEQPVCMLF 552
Cdd:COG0515   13 RLLGRGGMGVVYLAR------DLRlgRPVALKVLRpELAADPEARErFRREARALARLNHPNIVRVYDVGEEDGRPYLVM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 EYMNQGDLHEFLIMRSPhsdvgcssdedgtvkssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKIS 632
Cdd:COG0515   87 EYVEGESLADLLRRRGP-----------------LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 633 DLGLSREIYSADyyrvQSKSSLPI---RWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRKRQ 709
Cdd:COG0515  150 DFGIARALGGAT----LTQTGTVVgtpGYMAPEQARGEPVDPRSDVYSLGVTLYELLT-GRPPFDGDSPAELLRAHLREP 224
                        250
                 ....*....|....
gi 223461072 710 LLPCSE---DCPPR 720
Cdd:COG0515  225 PPPPSElrpDLPPA 238
Pkinase pfam00069
Protein kinase domain;
475-742 1.43e-28

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 114.26  E-value: 1.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  475 FMEELGECTFGKIYKGHLYLPGmdhaQLVAIKTL-KDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFE 553
Cdd:pfam00069   3 VLRKLGSGSFGTVYKAKHRDTG----KIVAIKKIkKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  554 YMNQGDLHEFLimrsphsdvgcssdedgTVKSSLDHGDFLHIAIQIAAGMEYlsshffvhkdlaarniliGEQLHVKISD 633
Cdd:pfam00069  79 YVEGGSLFDLL-----------------SEKGAFSEREAKFIMKQILEGLES------------------GSSLTTFVGT 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  634 LGlsreiysadyyrvqsksslpirWMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVIEMVRKRQLLPC 713
Cdd:pfam00069 124 PW----------------------YMAPEVLGGNPYGPKVDVWSLGCILYELL-TGKPPFPGINGNEIYELIIDQPYAFP 180
                         250       260       270
                  ....*....|....*....|....*....|.
gi 223461072  714 SED--CPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:pfam00069 181 ELPsnLSEEAKDLLKKLLKKDPSKRLTATQA 211
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
467-742 2.38e-28

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: 115.54  E-value: 2.38e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGHLylpgmdHAQlVAIKTLK-DYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQE 545
Cdd:cd14151    4 EIPDGQITVGQRIGSGSFGTVYKGKW------HGD-VAVKMLNvTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 546 QpVCMLFEYMNQGDLHEFLimrsphsdvgcssdedGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGE 625
Cdd:cd14151   77 Q-LAIVTQWCEGSSLYHHL----------------HIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHE 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 626 QLHVKISDLGLS--REIYSADYYRVQSKSSlpIRWMPPEAIMY---GKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQ- 699
Cdd:cd14151  140 DLTVKIGDFGLAtvKSRWSGSHQFEQLSGS--ILWMAPEVIRMqdkNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRd 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 223461072 700 EVIEMVRKRQLLP----CSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14151  217 QIIFMVGRGYLSPdlskVRSNCPKAMKRLMAECLKKKRDERPLFPQI 263
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
474-742 4.22e-28

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: 114.15  E-value: 4.22e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 474 RFMEELGECTFGKIYKGHLYLPGmdhaQLVAIKTL-KDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLF 552
Cdd:cd14003    3 ELGKTLGEGSFGKVKLARHKLTG----EKVAIKIIdKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 EYMNQGDLHEFLIMRSPhsdvgcssdedgtvkssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKIS 632
Cdd:cd14003   79 EYASGGELFDYIVNNGR-----------------LSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKII 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 633 DLGLSREIYSADYYRVQSKSslpIRWMPPEAIM----YGKfssDSDIWSFGVVLWEIFsFGlqpYYGFSNQEVIEMvrKR 708
Cdd:cd14003  142 DFGLSNEFRGGSLLKTFCGT---PAYAAPEVLLgrkyDGP---KADVWSLGVILYAML-TG---YLPFDDDNDSKL--FR 209
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 223461072 709 QLLPCSEDCPPRmysLMTECWNEI-------PSRRPRFKDI 742
Cdd:cd14003  210 KILKGKYPIPSH---LSPDARDLIrrmlvvdPSKRITIEEI 247
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
313-391 4.69e-27

Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.


Pssm-ID: 395005  Cd Length: 79  Bit Score: 105.08  E-value: 4.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  313 CYNSTGVDYRGTVSVTKSGRQCQPWNSQYPHTHSF-TALRFPELNGGHSYCRNPGNQkEAPWCFTLDENFKSDLCDIPAC 391
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGD-ERPWCYTTDPRVRWEYCDIPRC 79
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
479-742 1.14e-26

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: 109.89  E-value: 1.14e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKghlylpgMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQG 558
Cdd:cd14065    1 LGKGFFGEVYK-------VTHRETGKVMVMKELKRFDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 559 DLHEfLIMRSphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQ---LHVKISDLG 635
Cdd:cd14065   74 TLEE-LLKSM---------------DEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREAnrgRNAVVADFG 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 636 LSREIysADYYRVQSKSSLPIR------WMPPEAIMYGKFSSDSDIWSFGVVLWEIFS--------------FGLQpyyg 695
Cdd:cd14065  138 LAREM--PDEKTKKPDRKKRLTvvgspyWMAPEMLRGESYDEKVDVFSFGIVLCEIIGrvpadpdylprtmdFGLD---- 211
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 223461072 696 fsnqeviemVRK-RQLLPcsEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14065  212 ---------VRAfRTLYV--PDCPPSFLPLAIRCCQLDPEKRPSFVEL 248
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
473-742 2.07e-26

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: 2.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 473 VRFMEELGECTFGKIYKGHLylpgmdHAQlVAIKTLKDYN-NPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQpVCML 551
Cdd:cd14150    2 VSMLKRIGTGSFGTVFRGKW------HGD-VAVKILKVTEpTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTRPN-FAII 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMNQGDLHEFLimrspHsdvgcssdedgTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKI 631
Cdd:cd14150   74 TQWCEGSSLYRHL-----H-----------VTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKI 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 632 SDLGLS--REIYSADYYRVQSKSSlpIRWMPPEAIMY---GKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQ-EVIEMV 705
Cdd:cd14150  138 GDFGLAtvKTRWSGSQQVEQPSGS--ILWMAPEVIRMqdtNPYSFQSDVYAYGVVLYELMS-GTLPYSNINNRdQIIFMV 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 223461072 706 RKRQLLP----CSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14150  215 GRGYLSPdlskLSSNCPKAMKRLLIDCLKFKREERPLFPQI 255
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
476-715 7.82e-26

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: 108.34  E-value: 7.82e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGHlylpGMDHAQLVAIKTLKdynNPQQWTEFQQ----EASLMAELHHPNIVCLLGAVTQEQPVCML 551
Cdd:cd07829    4 LEKLGEGTYGVVYKAK----DKKTGEIVALKKIR---LDNEEEGIPStalrEISLLKELKHPNIVKLLDVIHTENKLYLV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMNQgDLHEFLIMRSPHSDVGcssdedgTVKSsldhgdflhIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKI 631
Cdd:cd07829   77 FEYCDQ-DLKKYLDKRPGPLPPN-------LIKS---------IMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKL 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 632 SDLGLSREI------YSAD----YYRvqsksslpirwmPPEAIMYGKFSSDS-DIWSFGVVLweifsfglqpyygfsnqe 700
Cdd:cd07829  140 ADFGLARAFgiplrtYTHEvvtlWYR------------APEILLGSKHYSTAvDIWSVGCIF------------------ 189
                        250
                 ....*....|....*.
gi 223461072 701 vIEMVRKRQLLPC-SE 715
Cdd:cd07829  190 -AELITGKPLFPGdSE 204
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
501-742 1.25e-25

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: 107.48  E-value: 1.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 501 QLVAIK--TLKDYNNPQQWTEFQQeaslMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRsphsDVGCssd 578
Cdd:cd13992   26 RTVAIKhiTFSRTEKRTILQELNQ----LKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNR----EIKM--- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 579 eDGTVKSSLdhgdflhiAIQIAAGMEYL-SSHFFVHKDLAARNILIGEQLHVKISDLGLsREIYSADyyRVQSKSSLPIR 657
Cdd:cd13992   95 -DWMFKSSF--------IKDIVKGMNYLhSSSIGYHGRLKSSNCLVDSRWVVKLTDFGL-RNLLEEQ--TNHQLDEDAQH 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 658 ----WMPPEAI----MYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVIEMVRKRQ-------LLPCSEDCPPRMY 722
Cdd:cd13992  163 kkllWTAPELLrgslLEVRGTQKGDVYSFAIILYEIL-FRSDPFALEREVAIVEKVISGGnkpfrpeLAVLLDEFPPRLV 241
                        250       260
                 ....*....|....*....|
gi 223461072 723 SLMTECWNEIPSRRPRFKDI 742
Cdd:cd13992  242 LLVKQCWAENPEKRPSFKQI 261
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
479-748 1.91e-25

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: 107.20  E-value: 1.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLylpgmdHAQLVAIKTL---KDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYM 555
Cdd:cd14158   23 LGEGGFGVVFKGYI------NDKNVAVKKLaamVDISTEDLTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYM 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQGDLHEFLimrsphsdvGCSSDEDG-TVKSSLDhgdflhIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd14158   97 PNGSLLDRL---------ACLNDTPPlSWHMRCK------IAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 635 GLSREIYSADYYRVQSKSSLPIRWMPPEAIMyGKFSSDSDIWSFGVVLWEIFSfGLQPY-YGFSNQEVIEMvrKRQLlpC 713
Cdd:cd14158  162 GLARASEKFSQTIMTERIVGTTAYMAPEALR-GEITPKSDIFSFGVVLLEIIT-GLPPVdENRDPQLLLDI--KEEI--E 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 223461072 714 SE-------------DCPP----RMYSLMTECWNEIPSRRPRFKDIHVRLRS 748
Cdd:cd14158  236 DEektiedyvdkkmgDWDStsieAMYSVASQCLNDKKNRRPDIAKVQQLLQE 287
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
447-737 2.86e-25

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: 106.54  E-value: 2.86e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 447 RGQNVEMSMLNAYKPKSKAKELPLSAVRFMEELGECtfgkiykghlylpgmdhaqlvaiktlkdynnpQQWTEFQQEASL 526
Cdd:cd14000   16 KGEPVAVKIFNKHTSSNFANVPADTMLRHLRATDAM--------------------------------KNFRLLRQELTV 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 527 MAELHHPNIVCLLGAVTqeQPVCMLFEYMNQGDLHEFLimrsphsdvgcssDEDGTVKSSLDHGDFLHIAIQIAAGMEYL 606
Cdd:cd14000   64 LSHLHHPSIVYLLGIGI--HPLMLVLELAPLGSLDHLL-------------QQDSRSFASLGRTLQQRIALQVADGLRYL 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 607 SSHFFVHKDLAARNILI-----GEQLHVKISDLGLSREIYSADYYRVQSKSSlpirWMPPEAIMYG-KFSSDSDIWSFGV 680
Cdd:cd14000  129 HSAMIIYRDLKSHNVLVwtlypNSAIIIKIADYGISRQCCRMGAKGSEGTPG----FRAPEIARGNvIYNEKVDVFSFGM 204
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 681 VLWEIFSfGLQPYYGFSNQEVIEMVRKRQLLPCSE-DC--PPRMYSLMTECWNEIPSRRP 737
Cdd:cd14000  205 LLYEILS-GGAPMVGHLKFPNEFDIHGGLRPPLKQyECapWPEVEVLMKKCWKENPQQRP 263
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
473-737 5.06e-25

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: 105.54  E-value: 5.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 473 VRFMEELGECTFGKIYKGhLYlpgmdHAQLVAIKTLKDY-NNPQQWTEFQQEASLmAELHHPNIVCLLGAVTQEQPVC-- 549
Cdd:cd13979    5 LRLQEPLGSGGFGSVYKA-TY-----KGETVAVKIVRRRrKNRASRQSFWAELNA-ARLRHENIVRVLAAETGTDFASlg 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 550 -MLFEYMNQGDLHEFLimrsphsdvgcssdeDGTVKSsLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLH 628
Cdd:cd13979   78 lIIMEYCGNGTLQQLI---------------YEGSEP-LPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGV 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 629 VKISDLGLSREIYSADyyRVQSKSSL---PIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIfSFGLQPYYGfSNQEVIEMV 705
Cdd:cd13979  142 CKLCDFGCSVKLGEGN--EVGTPRSHiggTYTYRAPELLKGERVTPKADIYSFGITLWQM-LTRELPYAG-LRQHVLYAV 217
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 223461072 706 RKRQLLPC----SEDCPPRMY-SLMTECWNEIPSRRP 737
Cdd:cd13979  218 VAKDLRPDlsglEDSEFGQRLrSLISRCWSAQPAERP 254
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
479-736 7.55e-25

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: 104.52  E-value: 7.55e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYK------GHLYlpgmdhaqlvAIKTL-KDY---NNPQQWTefQQEASLMAELHHPNIVCLLGAVTQEQPV 548
Cdd:cd05123    1 LGKGSFGKVLLvrkkdtGKLY----------AMKVLrKKEiikRKEVEHT--LNERNILERVNHPFIVKLHYAFQTEEKL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 549 CMLFEYMNQGDLHeFLIMRSPHSDVGCSSdedgtvkssldhgdFlhIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLH 628
Cdd:cd05123   69 YLVLDYVPGGELF-SHLSKEGRFPEERAR--------------F--YAAEIVLALEYLHSLGIIYRDLKPENILLDSDGH 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 629 VKISDLGLSREIYSADYYRVQSKSSLPirWMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVIEMVRKR 708
Cdd:cd05123  132 IKLTDFGLAKELSSDGDRTYTFCGTPE--YLAPEVLLGKGYGKAVDWWSLGVLLYEML-TGKPPFYAENRKEIYEKILKS 208
                        250       260
                 ....*....|....*....|....*....
gi 223461072 709 QL-LPcsEDCPPRMYSLMTECWNEIPSRR 736
Cdd:cd05123  209 PLkFP--EYVSPEAKSLISGLLQKDPTKR 235
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
479-746 2.62e-24

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 102.99  E-value: 2.62e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLylpgmdHAQLVAIKTLKD--YNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQE-QPVCMLFEYM 555
Cdd:cd14064    1 IGSGSFGKVYKGRC------RNKIVAIKRYRAntYCSKSDVDMFCREVSILCRLNHPCVIQFVGACLDDpSQFAIVTQYV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQGDLHEFLimrspHSDvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYL--SSHFFVHKDLAARNILIGEQLHVKISD 633
Cdd:cd14064   75 SGGSLFSLL-----HEQ-----------KRVIDLQSKLIIAVDVAKGMEYLhnLTQPIIHRDLNSHNILLYEDGHAVVAD 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 634 LGLSREIYSADYYRVqSKSSLPIRWMPPEAIMY-GKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLP 712
Cdd:cd14064  139 FGESRFLQSLDEDNM-TKQPGNLRWMAPEVFTQcTRYSIKADVFSYALCLWELLTGEIPFAHLKPAAAAADMAYHHIRPP 217
                        250       260       270
                 ....*....|....*....|....*....|....
gi 223461072 713 CSEDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd14064  218 IGYSIPKPISSLLMRGWNAEPESRPSFVEIVALL 251
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
477-737 3.06e-24

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: 103.07  E-value: 3.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHlylpGMDHAQLVAIKTLKDYNNPQQ-WTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYM 555
Cdd:cd06627    6 DLIGRGAFGSVYKGL----NLNTGEFVAIKQISLEKIPKSdLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQGDLHEflimrsphsdvgcssdedgTVKsslDHGDF------LHIAiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHV 629
Cdd:cd06627   82 ENGSLAS-------------------IIK---KFGKFpeslvaVYIY-QVLEGLAYLHEQGVIHRDIKGANILTTKDGLV 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 630 KISDLGLSREIYSADyyrVQSKSSL--PiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFsnQEVIEMVR- 706
Cdd:cd06627  139 KLADFGVATKLNEVE---KDENSVVgtP-YWMAPEVIEMSGVTTASDIWSVGCTVIELLT-GNPPYYDL--QPMAALFRi 211
                        250       260       270
                 ....*....|....*....|....*....|..
gi 223461072 707 -KRQLLPCSEDCPPRMYSLMTECWNEIPSRRP 737
Cdd:cd06627  212 vQDDHPPLPENISPELRDFLLQCFQKDPTLRP 243
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
479-742 3.09e-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: 103.34  E-value: 3.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHlylpgMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQG 558
Cdd:cd14664    1 IGRGGAGTVYKGV-----MPNGTLVAVKRLKGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 559 DLHEFLIMRSPHsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSH---FFVHKDLAARNILIGEQLHVKISDLG 635
Cdd:cd14664   76 SLGELLHSRPES-------------QPPLDWETRQRIALGSARGLAYLHHDcspLIIHRDVKSNNILLDEEFEAHVADFG 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 636 LSREIysaDYYRVQSKSSL--PIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVR-KRQLLp 712
Cdd:cd14664  143 LAKLM---DDKDSHVMSSVagSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELIT-GKRPFDEAFLDDGVDIVDwVRGLL- 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 223461072 713 cSEDC-----PPRM--YSLMTE----------CWNEIPSRRPRFKDI 742
Cdd:cd14664  218 -EEKKvealvDPDLqgVYKLEEveqvfqvallCTQSSPMERPTMREV 263
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
467-742 4.29e-24

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: 103.19  E-value: 4.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 467 ELPLSAVRFMEELGECTFGKIYKGHLylpgmdHAQlVAIKTLKDYN-NPQQWTEFQQEASLMAELHHPNIVCLLGAVTQE 545
Cdd:cd14149    8 EIEASEVMLSTRIGSGSFGTVYKGKW------HGD-VAVKILKVVDpTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 546 QpVCMLFEYMNQGDLHEFLimrsphsdvgcssdedGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGE 625
Cdd:cd14149   81 N-LAIVTQWCEGSSLYKHL----------------HVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHE 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 626 QLHVKISDLGLS--REIYSADYYRVQSKSSlpIRWMPPEAIMY---GKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQ- 699
Cdd:cd14149  144 GLTVKIGDFGLAtvKSRWSGSQQVEQPTGS--ILWMAPEVIRMqdnNPFSFQSDVYSYGIVLYELMT-GELPYSHINNRd 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 223461072 700 EVIEMVRKRQLLP----CSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14149  221 QIIFMVGRGYASPdlskLYKNCPKAMKRLVADCIKKVKEERPLFPQI 267
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
476-742 1.38e-23

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: 101.00  E-value: 1.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYkghLYLPGMDHaQLVAIKTLK-DYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd08215    5 IRVIGKGSFGSAY---LVRRKSDG-KLYVLKEIDlSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQGDLHEFLimrsphsdvgcssDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd08215   81 ADGGDLAQKI-------------KKQKKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDF 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 635 GLSREIYSAD----------YYrvqsksslpirwMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfgLQ-PYYGFSNQEVIE 703
Cdd:cd08215  148 GISKVLESTTdlaktvvgtpYY------------LSPELCENKPYNYKSDIWALGCVLYELCT--LKhPFEANNLPALVY 213
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 223461072 704 MVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd08215  214 KIVKGQYPPIPSQYSSELRDLVNSMLQKDPEKRPSANEI 252
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
522-746 4.46e-23

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: 99.47  E-value: 4.46e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 522 QEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSPHSdvgcssdedGTVKssldhgdfLHIAIQIAA 601
Cdd:cd14155   37 REVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLEQLLDSNEPLS---------WTVR--------VKLALDIAR 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 602 GMEYLSSHFFVHKDLAARNILI---GEQLHVKISDLGLSREIYSADYyrvqSKSSLPI----RWMPPEAIMYGKFSSDSD 674
Cdd:cd14155  100 GLSYLHSKGIFHRDLTSKNCLIkrdENGYTAVVGDFGLAEKIPDYSD----GKEKLAVvgspYWMAPEVLRGEPYNEKAD 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 675 IWSFGVVLWEIF--------------SFGLQpYYGFsnqeviemvrkRQLLPcseDCPPRMYSLMTECWNEIPSRRPRFK 740
Cdd:cd14155  176 VFSYGIILCEIIariqadpdylprteDFGLD-YDAF-----------QHMVG---DCPPDFLQLAFNCCNMDPKSRPSFH 240

                 ....*.
gi 223461072 741 DIHVRL 746
Cdd:cd14155  241 DIVKTL 246
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
475-732 7.77e-23

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: 99.09  E-value: 7.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYKGHLYLPGmdhaQLVAIKTL-KDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFE 553
Cdd:cd05117    4 LGKVLGRGSFGVVRLAVHKKTG----EEYAVKIIdKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 554 YMNQGDLHEFLIMrsphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILI---GEQLHVK 630
Cdd:cd05117   80 LCTGGELFDRIVK-----------------KGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIK 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 631 ISDLGLSREI----------YSADYyrvqsksslpirwMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQE 700
Cdd:cd05117  143 IIDFGLAKIFeegeklktvcGTPYY-------------VAPEVLKGKGYGKKCDIWSLGVILYILLC-GYPPFYGETEQE 208
                        250       260       270
                 ....*....|....*....|....*....|..
gi 223461072 701 VIEMVRKRQllpcsedcpprmYSLMTECWNEI 732
Cdd:cd05117  209 LFEKILKGK------------YSFDSPEWKNV 228
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
479-684 1.39e-22

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


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 99.18  E-value: 1.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGmdhaQLVAIKTLKdynnPQQWTEFQ--------QEASLMAELHHPNIVCLLGAVTQEQPVCM 550
Cdd:cd07841    8 LGEGTYAVVYKARDKETG----RIVAIKKIK----LGERKEAKdginftalREIKLLQELKHPNIIGLLDVFGHKSNINL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 551 LFEYMnQGDLhEFLImrsphsdvgcssdEDGTVksSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVK 630
Cdd:cd07841   80 VFEFM-ETDL-EKVI-------------KDKSI--VLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLK 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 631 ISDLGLSREIYSADY---YRVQSksslpiRWM-PPEaIMYG--KFSSDSDIWSFGVVLWE 684
Cdd:cd07841  143 LADFGLARSFGSPNRkmtHQVVT------RWYrAPE-LLFGarHYGVGVDMWSVGCIFAE 195
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
476-688 3.18e-22

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: 97.60  E-value: 3.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKD-YNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd07830    4 IKQLGDGTFGSVYLARNKETG----ELVAIKKMKKkFYSWEECMNLREVKSLRKLNEHPNIVKLKEVFRENDELYFVFEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQgDLHEFliMRSphSDVGCSSDEdgTVKSsldhgdflhIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd07830   80 MEG-NLYQL--MKD--RKGKPFSES--VIRS---------IIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADF 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223461072 635 GLSREIYS----ADY-----YRVqsksslpirwmpPEAIMY-GKFSSDSDIWSFGVVLWEIFSF 688
Cdd:cd07830  144 GLAREIRSrppyTDYvstrwYRA------------PEILLRsTSYSSPVDIWALGCIMAELYTL 195
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
505-737 5.57e-22

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: 96.96  E-value: 5.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 505 IKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGavTQEQPVCMLFEYMNQGDLHEFLimrsphsdvgcSSDEDGTVK 584
Cdd:cd14067   42 LKHLRAADAMKNFSEFRQEASMLHSLQHPCIVYLIG--ISIHPLCFALELAPLGSLNTVL-----------EENHKGSSF 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 585 SSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILI-----GEQLHVKISDLGLSREIYSADYYRVQSKSSlpirWM 659
Cdd:cd14067  109 MPLGHMLTFKIAYQIAAGLAYLHKKNIIFCDLKSDNILVwsldvQEHINIKLSDYGISRQSFHEGALGVEGTPG----YQ 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 660 PPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRK--RQLLPCSEDCP-PRMYSLMTECWNEIPSRR 736
Cdd:cd14067  185 APEIRPRIVYDEKVDMFSYGMVLYELLS-GQRPSLGHHQLQIAKKLSKgiRPVLGQPEEVQfFRLQALMMECWDTKPEKR 263

                 .
gi 223461072 737 P 737
Cdd:cd14067  264 P 264
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
477-737 7.79e-22

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: 96.30  E-value: 7.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHlylpGMDHAQLVAIK------TLKDYNNPQQWT---EFQQEASLMAELHHPNIVCLLGAVTQEQP 547
Cdd:cd06629    7 ELIGKGTYGRVYLAM----NATTGEMLAVKqvelpkTSSDRADSRQKTvvdALKSEIDTLKDLDHPNIVQYLGFEETEDY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 548 VCMLFEYMNQGDLHEFLIMRSPHsdvgcssdEDGTVKssldhgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQL 627
Cdd:cd06629   83 FSIFLEYVPGGSIGSCLRKYGKF--------EEDLVR---------FFTRQILDGLAYLHSKGILHRDLKADNILVDLEG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 628 HVKISDLGLSREiySADYYRVQSKSSL--PIRWMPPEAIM-YGK-FSSDSDIWSFGVVLWEIFSfGLQPYygfSNQEVIE 703
Cdd:cd06629  146 ICKISDFGISKK--SDDIYGNNGATSMqgSVFWMAPEVIHsQGQgYSAKVDIWSLGCVVLEMLA-GRRPW---SDDEAIA 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 223461072 704 MV----RKRQLLPCSEDC--PPRMYSLMTECWNEIPSRRP 737
Cdd:cd06629  220 AMfklgNKRSAPPVPEDVnlSPEALDFLNACFAIDPRDRP 259
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
479-728 8.27e-22

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: 95.75  E-value: 8.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGmdhaQLVAIKTL-KDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQ 557
Cdd:cd14009    1 IGRGSFATVWKGRHKQTG----EVVAIKEIsRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 558 GDLHEFLIMRSPHSDVGCssdedgtvkssldhgdfLHIAIQIAAGMEYLSSHFFVHKDLAARNILI---GEQLHVKISDL 634
Cdd:cd14009   77 GDLSQYIRKRGRLPEAVA-----------------RHFMQQLASGLKFLRSKNIIHRDLKPQNLLLstsGDDPVLKIADF 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 635 GLSREIYSADYYRVQSKSSLpirWMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVIEMVRKRQLlpcs 714
Cdd:cd14009  140 GFARSLQPASMAETLCGSPL---YMAPEILQFQKYDAKADLWSVGAILFEML-VGKPPFRGSNHVQLLRNIERSDA---- 211
                        250
                 ....*....|....
gi 223461072 715 EDCPPRMYSLMTEC 728
Cdd:cd14009  212 VIPFPIAAQLSPDC 225
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
475-742 8.42e-22

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: 95.79  E-value: 8.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYKGhlylpgMDHA-QLVAIKTLKD--YNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCML 551
Cdd:cd14161    7 FLETLGKGTYGRVKKA------RDSSgRLVAIKSIRKdrIKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMNQGDLHEFLIMRSPHSDVGCSsdedgtvkssldhgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKI 631
Cdd:cd14161   81 MEYASRGDLYDYISERQRLSELEAR-----------------HFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKI 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 632 SDLGLSrEIYSADYYrVQSKSSLPIrWMPPEaIMYGK--FSSDSDIWSFGVVLWeIFSFGLQPYYGFSNQEVIEMVRK-- 707
Cdd:cd14161  144 ADFGLS-NLYNQDKF-LQTYCGSPL-YASPE-IVNGRpyIGPEVDSWSLGVLLY-ILVHGTMPFDGHDYKILVKQISSga 218
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 223461072 708 -RQLLPCSEDCPPRMYSLMTEcwneiPSRRPRFKDI 742
Cdd:cd14161  219 yREPTKPSDACGLIRWLLMVN-----PERRATLEDV 249
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
476-697 9.49e-22

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: 96.58  E-value: 9.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGHlylpGMDHAQLVAIKTLKDYNN----PQQWTefqQEASLMAEL---HHPNIVCLLG-----AVT 543
Cdd:cd07838    4 VAEIGEGAYGTVYKAR----DLQDGRFVALKKVRVPLSeegiPLSTI---REIALLKQLesfEHPNVVRLLDvchgpRTD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 544 QEQPVCMLFEYMNQgDLHEFLimrSPHSDVGCSSDedgTVKssldhgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILI 623
Cdd:cd07838   77 RELKLTLVFEHVDQ-DLATYL---DKCPKPGLPPE---TIK---------DLMRQLLRGLDFLHSHRIVHRDLKPQNILV 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 624 GEQLHVKISDLGLSReIYSAD----------YYRvqsksslpirwmPPEAIMYGKFSSDSDIWSFGVVLWEIFSfgLQP- 692
Cdd:cd07838  141 TSDGQVKLADFGLAR-IYSFEmaltsvvvtlWYR------------APEVLLQSSYATPVDMWSVGCIFAELFN--RRPl 205

                 ....*
gi 223461072 693 YYGFS 697
Cdd:cd07838  206 FRGSS 210
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
477-742 1.27e-21

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: 95.64  E-value: 1.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKghlylpgmdhAQLVAIKT---LKDYN----NPQQWTEFQQEASLMAELHHPNIVCLLGAVTQeqPVC 549
Cdd:cd14025    2 EKVGSGGFGQVYK----------VRHKHWKTwlaIKCPPslhvDDSERMELLEEAKKMEMAKFRHILPVYGICSE--PVG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 550 MLFEYMNQGDLHEFLimrsphsdvgcssdedgtVKSSLDHGDFLHIAIQIAAGMEYLSSHF--FVHKDLAARNILIGEQL 627
Cdd:cd14025   70 LVMEYMETGSLEKLL------------------ASEPLPWELRFRIIHETAVGMNFLHCMKppLLHLDLKPANILLDAHY 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 628 HVKISDLGLSR-EIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDS--DIWSFGVVLWEIFSfGLQPYYGFSNQEVIeM 704
Cdd:cd14025  132 HVKISDFGLAKwNGLSHSHDLSRDGLRGTIAYLPPERFKEKNRCPDTkhDVYSFAIVIWGILT-QKKPFAGENNILHI-M 209
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 223461072 705 VR----KRQLLPCSEDCPPR----MYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14025  210 VKvvkgHRPSLSPIPRQRPSecqqMICLMKRCWDQDPRKRPTFQDI 255
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
479-717 1.80e-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: 95.31  E-value: 1.80e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGmdhaQLVAIKTLK------------DYNNPQQWTE-FQQEASLMAELHHPNIVCLLGAVT-- 543
Cdd:cd14008    1 LGRGSFGKVKLALDTETG----QLYAIKIFNksrlrkrregknDRGKIKNALDdVRREIAIMKKLDHPNIVRLYEVIDdp 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 544 QEQPVCMLFEYMNQGDlheflIMrsphsdvgcsSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILI 623
Cdd:cd14008   77 ESDKLYLVLEYCEGGP-----VM----------ELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 624 GEQLHVKISDLGLSREIYSADYYRVQSKSSlPIrWMPPEAIMYGKFSSD---SDIWSFGVVLWeIFSFGLQPYYGFSNQE 700
Cdd:cd14008  142 TADGTVKISDFGVSEMFEDGNDTLQKTAGT-PA-FLAPELCDGDSKTYSgkaADIWALGVTLY-CLVFGRLPFNGDNILE 218
                        250       260
                 ....*....|....*....|..
gi 223461072 701 VIEMVRKRQL-----LPCSEDC 717
Cdd:cd14008  219 LYEAIQNQNDefpipPELSPEL 240
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
479-737 2.01e-21

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: 94.78  E-value: 2.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHlylpGMDHAQLVAIKTLKDYNNPQQWTE----FQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd06632    8 LGSGSFGSVYEGF----NGDTGDFFAVKEVSLVDDDKKSREsvkqLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQGDLHEFLimrsphsdvgcssdedgtvkssLDHGDFLHIAI-----QIAAGMEYLSSHFFVHKDLAARNILIGEQLHV 629
Cdd:cd06632   84 VPGGSIHKLL----------------------QRYGAFEEPVIrlytrQILSGLAYLHSRNTVHRDIKGANILVDTNGVV 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 630 KISDLGLSREIYSADYYRVQSKSSLpirWMPPEAIM-----YGkfsSDSDIWSFGVVLWEIFSfGLQPYYGFSN-QEVIE 703
Cdd:cd06632  142 KLADFGMAKHVEAFSFAKSFKGSPY---WMAPEVIMqknsgYG---LAVDIWSLGCTVLEMAT-GKPPWSQYEGvAAIFK 214
                        250       260       270
                 ....*....|....*....|....*....|....
gi 223461072 704 MVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRP 737
Cdd:cd06632  215 IGNSGELPPIPDHLSPDAKDFIRLCLQRDPEDRP 248
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
475-742 2.60e-21

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: 94.63  E-value: 2.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYKGHLYLPGmDHAQL----VAIKTL-KDYNNpqqWTE-FQQEASLMAELHHPNIVCLLGAVTQEQPV 548
Cdd:cd05078    3 FNESLGQGTFTKIFKGIRREVG-DYGQLheteVLLKVLdKAHRN---YSEsFFEAASMMSQLSHKHLVLNYGVCVCGDEN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 549 CMLFEYMNQGDLHEFLIMRsphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILI----- 623
Cdd:cd05078   79 ILVQEYVKFGSLDTYLKKN----------------KNCINILWKLEVAKQLAWAMHFLEEKTLVHGNVCAKNILLireed 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 624 ---GEQLHVKISDLGLSREIYSADYYRVQsksslpIRWMPPEAIMYGK-FSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQ 699
Cdd:cd05078  143 rktGNPPFIKLSDPGISITVLPKDILLER------IPWVPPECIENPKnLSLATDKWSFGTTLWEICSGGDKPLSALDSQ 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 223461072 700 EVIEMVRKRQLLPCSEdcPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05078  217 RKLQFYEDRHQLPAPK--WTELANLINNCMDYEPDHRPSFRAI 257
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
478-737 5.24e-21

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: 93.81  E-value: 5.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 478 ELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQ 557
Cdd:cd06623    8 VLGQGSSGVVYKVRHKPTG----KIYALKKIHVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 558 GDLHEFLIMRSPHSDVGCSSdedgtvkssldhgdflhIAIQIAAGMEYL-SSHFFVHKDLAARNILIGEQLHVKISDLGL 636
Cdd:cd06623   84 GSLADLLKKVGKIPEPVLAY-----------------IARQILKGLDYLhTKRHIIHRDIKPSNLLINSKGEVKIADFGI 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 637 SREIYSADYYRVQSKSSLPirWMPPEAIMYGKFSSDSDIWSFGVVLWEiFSFGLQPYYGFSNQEVIEMVRK----RQLLP 712
Cdd:cd06623  147 SKVLENTLDQCNTFVGTVT--YMSPERIQGESYSYAADIWSLGLTLLE-CALGKFPFLPPGQPSFFELMQAicdgPPPSL 223
                        250       260
                 ....*....|....*....|....*
gi 223461072 713 CSEDCPPRMYSLMTECWNEIPSRRP 737
Cdd:cd06623  224 PAEEFSPEFRDFISACLQKDPKKRP 248
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
479-687 6.74e-21

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: 93.07  E-value: 6.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLylpgMDHAQLVAIKTLKDYNNPQQWTEFqqEASLMAEL----HHPNIVCLLGAVT--QEQPVCMLF 552
Cdd:cd05118    7 IGEGAFGTVWLARD----KVTGEKVAIKKIKNDFRHPKAALR--EIKLLKHLndveGHPNIVKLLDVFEhrGGNHLCLVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 EYMNQgDLHEFLIMRSPHsdvgcssdedgtvkssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQL-HVKI 631
Cdd:cd05118   81 ELMGM-NLYELIKDYPRG----------------LPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELgQLKL 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 223461072 632 SDLGLSREIYSADYY-RVQSksslpiRW-MPPEAIMYGKFSSDS-DIWSFGVVLWEIFS 687
Cdd:cd05118  144 ADFGLARSFTSPPYTpYVAT------RWyRAPEVLLGAKPYGSSiDIWSLGCILAELLT 196
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
479-742 9.88e-21

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: 92.54  E-value: 9.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGmdhaQLVAIK-----TLKDYNNPQQwteFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFE 553
Cdd:cd14007    8 LGKGKFGNVYLAREKKSG----FIVALKvisksQLQKSGLEHQ---LRREIEIQSHLRHPNILRLYGYFEDKKRIYLILE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 554 YMNQGDLHEFLiMRSPHSDvgcssdeDGTVKssldhgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISD 633
Cdd:cd14007   81 YAPNGELYKEL-KKQKRFD-------EKEAA---------KYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLAD 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 634 LGLSREIYSA---------DYyrvqsksslpirwMPPEAIMYGKFSSDSDIWSFGVVLWEiFSFGLQPYYGFSNQEVIEM 704
Cdd:cd14007  144 FGWSVHAPSNrrktfcgtlDY-------------LPPEMVEGKEYDYKVDIWSLGVLCYE-LLVGKPPFESKSHQETYKR 209
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 223461072 705 VRKRQLlpcseDCPPRMYSlmtECWNEI-------PSRRPRFKDI 742
Cdd:cd14007  210 IQNVDI-----KFPSSVSP---EAKDLIskllqkdPSKRLSLEQV 246
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
474-742 1.85e-20

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: 92.07  E-value: 1.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 474 RFMEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKD--YNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCML 551
Cdd:cd14073    4 ELLETLGKGTYGKVKLAIERATG----REVAIKSIKKdkIEDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMNQGDLHEFLIMRSphsdvgcssdedgtvksSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKI 631
Cdd:cd14073   80 MEYASGGELYDYISERR-----------------RLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKI 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 632 SDLGLSREIYSADYYRVQSKSSLpirWMPPEaIMYGK--FSSDSDIWSFGVVLWeIFSFGLQPYYGFSNQEVIEMV-RKR 708
Cdd:cd14073  143 ADFGLSNLYSKDKLLQTFCGSPL---YASPE-IVNGTpyQGPEVDCWSLGVLLY-TLVYGTMPFDGSDFKRLVKQIsSGD 217
                        250       260       270
                 ....*....|....*....|....*....|....
gi 223461072 709 QLLPCSedcPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14073  218 YREPTQ---PSDASGLIRWMLTVNPKRRATIEDI 248
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
469-742 2.51e-20

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: 92.06  E-value: 2.51e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 469 PLSAVRFMEELGECTFGKIYKGHLYLPgmdhAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPV 548
Cdd:cd06641    2 PEELFTKLEKIGKGSFGEVFKGIDNRT----QKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 549 CMLFEYMNQGDLHEFLimrsphsdvgcssdEDGtvksSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLH 628
Cdd:cd06641   78 WIIMEYLGGGSALDLL--------------EPG----PLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGE 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 629 VKISDLGLSREIYSADYYRvQSKSSLPIrWMPPEAIMYGKFSSDSDIWSFGVVLWEIfSFGLQPYYGFSNQEVIEMVRKR 708
Cdd:cd06641  140 VKLADFGVAGQLTDTQIKR-N*FVGTPF-WMAPEVIKQSAYDSKADIWSLGITAIEL-ARGEPPHSELHPMKVLFLIPKN 216
                        250       260       270
                 ....*....|....*....|....*....|....
gi 223461072 709 QLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd06641  217 NPPTLEGNYSKPLKEFVEACLNKEPSFRPTAKEL 250
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
478-685 3.00e-20

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: 92.11  E-value: 3.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 478 ELGECTFGKIYKGHLYLPGmdhaQLVAIKTLkDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQ 557
Cdd:cd06611   12 ELGDGAFGKVYKAQHKETG----LFAAAKII-QIESEEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFCDG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 558 GDLHEflIMrsphsdvgcssDEdgtVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLS 637
Cdd:cd06611   87 GALDS--IM-----------LE---LERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVS 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 223461072 638 REIYSADyyrvQSKSSL---PiRWMPPEAIMYGKFSSD-----SDIWSFGVVLWEI 685
Cdd:cd06611  151 AKNKSTL----QKRDTFigtP-YWMAPEVVACETFKDNpydykADIWSLGITLIEL 201
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
479-748 3.65e-20

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: 91.42  E-value: 3.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKghlylpgMDHAQ---LVAIKTLKDYNNPQQWTeFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYM 555
Cdd:cd14154    1 LGKGFFGQAIK-------VTHREtgeVMVMKELIRFDEEAQRN-FLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYI 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQGDLHEFLimRSPhsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLG 635
Cdd:cd14154   73 PGGTLKDVL--KDM--------------ARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFG 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 636 LSREI---------YSADYYRVQSKSSLPIR---------WMPPEAIMYGKFSSDSDIWSFGVVLWEIF----------- 686
Cdd:cd14154  137 LARLIveerlpsgnMSPSETLRHLKSPDRKKrytvvgnpyWMAPEMLNGRSYDEKVDIFSFGIVLCEIIgrveadpdylp 216
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223461072 687 ---SFGLqpyygfsNQEVIEMvrkrQLLPcseDCPPRMYSLMTECWNEIPSRRPRFKDIHVRLRS 748
Cdd:cd14154  217 rtkDFGL-------NVDSFRE----KFCA---GCPPPFFKLAFLCCDLDPEKRPPFETLEEWLEA 267
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
479-749 3.74e-20

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: 91.17  E-value: 3.74e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKghlyLPGMDHAQLVAIKTLKDYNNPQQWTeFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQG 558
Cdd:cd14221    1 LGKGCFGQAIK----VTHRETGEVMVMKELIRFDEETQRT-FLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 559 DLHeflimrsphsdvgcssdedGTVKSSLDH---GDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLG 635
Cdd:cd14221   76 TLR-------------------GIIKSMDSHypwSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFG 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 636 LSR----EIYSADYYRVQSKSSLPIR--------WMPPEAIMYGKFSSDSDIWSFGVVLWEIFS-FGLQPYYGFSNQEVI 702
Cdd:cd14221  137 LARlmvdEKTQPEGLRSLKKPDRKKRytvvgnpyWMAPEMINGRSYDEKVDVFSFGIVLCEIIGrVNADPDYLPRTMDFG 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 223461072 703 EMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFkdihVRLRSW 749
Cdd:cd14221  217 LNVRGFLDRYCPPNCPPSFFPIAVLCCDLDPEKRPSF----SKLEHW 259
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
477-741 3.74e-20

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: 90.81  E-value: 3.74e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGhlYLPGmDHAQLVAIKTLKDYNNPQQWTE-FQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYM 555
Cdd:cd14121    1 EKLGSGTYATVYKA--YRKS-GAREVVAVKCVSKSSLNKASTEnLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQGDLHEFLIMRS--PHSdvgcssdedgTVKSsldhgdFLHiaiQIAAGMEYLSSHFFVHKDLAARNILI--GEQLHVKI 631
Cdd:cd14121   78 SGGDLSRFIRSRRtlPES----------TVRR------FLQ---QLASALQFLREHNISHMDLKPQNLLLssRYNPVLKL 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 632 SDLGLSREIYSADYYRVQSKSSLpirWMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVIEMVRKRQ-- 709
Cdd:cd14121  139 ADFGFAQHLKPNDEAHSLRGSPL---YMAPEMILKKKYDARVDLWSVGVILYECL-FGRAPFASRSFEELEEKIRSSKpi 214
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 223461072 710 LLPC----SEDCPPRMYSLMtecwNEIPSRRPRFKD 741
Cdd:cd14121  215 EIPTrpelSADCRDLLLRLL----QRDPDRRISFEE 246
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
471-737 3.75e-20

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: 91.27  E-value: 3.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 471 SAVRFMEELGECTFGKIYKGHlYLPgmdHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCM 550
Cdd:cd06610    1 DDYELIEVIGSGATAVVYAAY-CLP---KKEKVAIKRIDLEKCQTSMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 551 LFEYMNQGDLHEflIMRSPHSDVGCSSDEDGTV-KSSLDhgdflhiaiqiaaGMEYLSSHFFVHKDLAARNILIGEQLHV 629
Cdd:cd06610   77 VMPLLSGGSLLD--IMKSSYPRGGLDEAIIATVlKEVLK-------------GLEYLHSNGQIHRDVKAGNILLGEDGSV 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 630 KISDLGLSREIYsaDYYRVQSKSSLPIR----WMPPEAIMYGK-FSSDSDIWSFGVVLWEIfSFGLQPYYGFSNQEVIEM 704
Cdd:cd06610  142 KIADFGVSASLA--TGGDRTRKVRKTFVgtpcWMAPEVMEQVRgYDFKADIWSFGITAIEL-ATGAAPYSKYPPMKVLML 218
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 223461072 705 VRKRQLLPCSEDCPPRMYS-----LMTECWNEIPSRRP 737
Cdd:cd06610  219 TLQNDPPSLETGADYKKYSksfrkMISLCLQKDPSKRP 256
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
473-746 4.00e-20

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: 91.26  E-value: 4.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 473 VRFMEELGECTFGKIYKGHLylpgmdHAQlVAIKTLK-DYNNPQQWTEFQQEASLMAELHHPNIVCLLGAvtqeqpvCMl 551
Cdd:cd14063    2 LEIKEVIGKGRFGRVHRGRW------HGD-VAIKLLNiDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGA-------CM- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 feymnqgDLHEFLIM------RSPHSDVgcssdEDGtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIgE 625
Cdd:cd14063   67 -------DPPHLAIVtslckgRTLYSLI-----HER--KEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFL-E 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 626 QLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMP---PEAI---MYGK-------FSSDSDIWSFGVVLWEIFSFGLqP 692
Cdd:cd14063  132 NGRVVITDFGLFSLSGLLQPGRREDTLVIPNGWLCylaPEIIralSPDLdfeeslpFTKASDVYAFGTVWYELLAGRW-P 210
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 223461072 693 YYGFSNQEVIEMVRKRQLLPCSE-DCPPRMYSLMTECWNEIPSRRPRF---KDIHVRL 746
Cdd:cd14063  211 FKEQPAESIIWQVGCGKKQSLSQlDIGREVKDILMQCWAYDPEKRPTFsdlLRMLERL 268
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
475-742 4.37e-20

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: 91.12  E-value: 4.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYKG--HLYLPGMDHAQLVAIKTL-KDYNNPQQwtEFQQEASLMAELHHPNIVcLLGAVTQEQPVCML 551
Cdd:cd14208    3 FMESLGKGSFTKIYRGlrTDEEDDERCETEVLLKVMdPTHGNCQE--SFLEAASIMSQISHKHLV-LLHGVCVGKDSIMV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMNQGDLHEFLimRSPHSDvgcssdedGTVKSSLDhgdfLHIAIQIAAGMEYLSSHFFVHKDLAARNILI------GE 625
Cdd:cd14208   80 QEFVCHGALDLYL--KKQQQK--------GPVAISWK----LQVVKQLAYALNYLEDKQLVHGNVSAKKVLLsregdkGS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 626 QLHVKISDLGLSREIYSADYYRVQsksslpIRWMPPEAIMYGK-FSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEM 704
Cdd:cd14208  146 PPFIKLSDPGVSIKVLDEELLAER------IPWVAPECLSDPQnLALEADKWGFGATLWEIFSGGHMPLSALDPSKKLQF 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 223461072 705 VRKRQLLPCsedcpPR---MYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14208  220 YNDRKQLPA-----PHwieLASLIQQCMSYNPLLRPSFRAI 255
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
476-712 4.40e-20

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: 91.41  E-value: 4.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLK-DYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd07860    5 VEKIGEGTYGVVYKARNKLTG----EVVALKKIRlDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQgDLHEFLIMrSPHSDVGCSsdedgTVKSSLdhgdflhiaIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd07860   81 LHQ-DLKKFMDA-SALTGIPLP-----LIKSYL---------FQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADF 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 635 GLSREIysadyyrvqsksSLPIR----------WMPPEAIMYGKF-SSDSDIWSFGVvlweIFSfglqpyygfsnqeviE 703
Cdd:cd07860  145 GLARAF------------GVPVRtythevvtlwYRAPEILLGCKYySTAVDIWSLGC----IFA---------------E 193

                 ....*....
gi 223461072 704 MVRKRQLLP 712
Cdd:cd07860  194 MVTRRALFP 202
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
479-743 1.05e-19

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: 90.00  E-value: 1.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQWTeFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQG 558
Cdd:cd14222    1 LGKGFFGQAIKVTHKATG----KVMVMKELIRCDEETQKT-FLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 559 DLHEFLimrspHSDVGCSSDEDgtvkssldhgdfLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSR 638
Cdd:cd14222   76 TLKDFL-----RADDPFPWQQK------------VSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSR 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 639 EIYSADYYRVQSKSSLPIR------------------WMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfglQPY------- 693
Cdd:cd14222  139 LIVEEKKKPPPDKPTTKKRtlrkndrkkrytvvgnpyWMAPEMLNGKSYDEKVDIFSFGIVLCEIIG---QVYadpdclp 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 223461072 694 ----YGFSNQEVIEmvrkrQLLPcsEDCPPRMYSLMTECWNEIPSRRPRFKDIH 743
Cdd:cd14222  216 rtldFGLNVRLFWE-----KFVP--KDCPPAFFPLAAICCRLEPDSRPAFSKLE 262
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
476-712 1.55e-19

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: 90.04  E-value: 1.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLK----DYNNPQqwTEFQqEASLMAELHHPNIVCLLGAVTQEQPVCML 551
Cdd:cd07835    4 LEKIGEGTYGVVYKARDKLTG----EIVALKKIRleteDEGVPS--TAIR-EISLLKELNHPNIVRLLDVVHSENKLYLV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMNQgDLHEFLiMRSPHSDVGCSsdedgTVKSsldhgdFLHiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKI 631
Cdd:cd07835   77 FEFLDL-DLKKYM-DSSPLTGLDPP-----LIKS------YLY---QLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 632 SDLGLSREIysadyyrvqsksSLPIR---------WM-PPEAIMYGK-FSSDSDIWSFGVvlweIFSfglqpyygfsnqe 700
Cdd:cd07835  141 ADFGLARAF------------GVPVRtythevvtlWYrAPEILLGSKhYSTPVDIWSVGC----IFA------------- 191
                        250
                 ....*....|..
gi 223461072 701 viEMVRKRQLLP 712
Cdd:cd07835  192 --EMVTRRPLFP 201
I-set pfam07679
Immunoglobulin I-set domain;
63-148 1.80e-19

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 83.85  E-value: 1.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072   63 PMNNITTSLGQTAELHCKVSGNPPPSIRWFKNDAPvVQEPRRISFRATNYGSRLRIRNLDTTDTGYFQCVATNGKKVVST 142
Cdd:pfam07679   6 KPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQP-LRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEA 84

                  ....*.
gi 223461072  143 TGVLFV 148
Cdd:pfam07679  85 SAELTV 90
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
479-700 3.11e-19

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: 88.19  E-value: 3.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKG-HLYLPGMDhaqlVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAvtQEQP--VCMLFEYM 555
Cdd:cd14120    1 IGHGAFAVVFKGrHRKKPDLP----VAIKCITKKNLSKSQNLLGKEIKILKELSHENVVALLDC--QETSssVYLVMEYC 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQGDLHEFLimrsphsdvgcssdedgTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILI---------GEQ 626
Cdd:cd14120   75 NGGDLADYL-----------------QAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLshnsgrkpsPND 137
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223461072 627 LHVKISDLGLSREIYSADYYRVQSKSSLpirWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQE 700
Cdd:cd14120  138 IRLKIADFGFARFLQDGMMAATLCGSPM---YMAPEVIMSLQYDAKADLWSIGTIVYQCLT-GKAPFQAQTPQE 207
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
479-705 3.62e-19

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: 88.05  E-value: 3.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGMDHAQLVaIKTLKdynnPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQG 558
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKF-IKCRK----AKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 559 DLHEFLImrsphsdvgcssDEDgtvkSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQL--HVKISDLGL 636
Cdd:cd14103   76 ELFERVV------------DDD----FELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTgnQIKIIDFGL 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223461072 637 SReiysadyyRVQSKSSLPIRW-----MPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMV 705
Cdd:cd14103  140 AR--------KYDPDKKLKVLFgtpefVAPEVVNYEPISYATDMWSVGVICYVLLS-GLSPFMGDNDAETLANV 204
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
479-687 4.23e-19

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 89.82  E-value: 4.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQWTEFQQ-------------EASLMAELHHPNIVCLLGAVTQE 545
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTG----KIVAIKKVKIIEISNDVTKDRQlvgmcgihfttlrELKIMNEIKHENIMGLVDVYVEG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 546 QPVCMLFEYMnQGDLHEFL--IMRSPHSDVGCssdedgtvkssldhgdflhIAIQIAAGMEYLSSHFFVHKDLAARNILI 623
Cdd:PTZ00024  93 DFINLVMDIM-ASDLKKVVdrKIRLTESQVKC-------------------ILLQILNGLNVLHKWYFMHRDLSPANIFI 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223461072 624 GEQLHVKISDLGLSREIYSADYYRVQSKSSLPIR-----------WM-PPEAIM-YGKFSSDSDIWSFGVVLWEIFS 687
Cdd:PTZ00024 153 NSKGICKIADFGLARRYGYPPYSDTLSKDETMQRreemtskvvtlWYrAPELLMgAEKYHFAVDMWSVGCIFAELLT 229
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
66-148 5.71e-19

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 82.17  E-value: 5.71e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072    66 NITTSLGQTAELHCKVSGNPPPSIRWFKNDAPVVQEPRRISFRATNYGSRLRIRNLDTTDTGYFQCVATNGKKVVSTTGV 145
Cdd:smart00410   3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                   ...
gi 223461072   146 LFV 148
Cdd:smart00410  83 LTV 85
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
479-712 6.42e-19

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: 87.76  E-value: 6.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHlylPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQG 558
Cdd:cd14202   10 IGHGAFAVVFKGR---HKEKHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 559 DLHEFLimrspHSdVGCSSDEdgTVKSSLDhgdflhiaiQIAAGMEYLSSHFFVHKDLAARNILIG---------EQLHV 629
Cdd:cd14202   87 DLADYL-----HT-MRTLSED--TIRLFLQ---------QIAGAMKMLHSKGIIHRDLKPQNILLSysggrksnpNNIRI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 630 KISDLGLSREIYSADYYRVQSKSSLpirWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRK-R 708
Cdd:cd14202  150 KIADFGFARYLQNNMMAATLCGSPM---YMAPEVIMSQHYDAKADLWSIGTIIYQCLT-GKAPFQASSPQDLRLFYEKnK 225

                 ....
gi 223461072 709 QLLP 712
Cdd:cd14202  226 SLSP 229
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
475-710 6.80e-19

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: 88.04  E-value: 6.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYKGHLYLPGmdhaQLVAIKTL-KDYNNPQQWTEF-QQEASLMAELHHPNIVCLLGAVTQEQPVCMLF 552
Cdd:cd05581    5 FGKPLGEGSYSTVVLAKEKETG----KEYAIKVLdKRHIIKEKKVKYvTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 EYMNQGDLHEFLimrsphsdvgcssdedgTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKIS 632
Cdd:cd05581   81 EYAPNGDLLEYI-----------------RKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKIT 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 633 DLGlSREIYSADYYRVQSK--SSLPIRWM--------------PPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGF 696
Cdd:cd05581  144 DFG-TAKVLGPDSSPESTKgdADSQIAYNqaraasfvgtaeyvSPELLNEKPAGKSSDLWALGCIIYQMLT-GKPPFRGS 221
                        250
                 ....*....|....
gi 223461072 697 SNQEVIEMVRKRQL 710
Cdd:cd05581  222 NEYLTFQKIVKLEY 235
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
477-687 8.33e-19

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: 88.00  E-value: 8.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNN----PQQwteFQQEASLMAELHHPNIVCLLGAVTQEQP----- 547
Cdd:cd07840    5 AQIGEGTYGQVYKARNKKTG----ELVALKKIRMENEkegfPIT---AIREIKLLQKLDHPNVVRLKEIVTSKGSakykg 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 548 -VCMLFEYMNQgDLHEFLimRSPHSDVGCSSdedgtVKssldhgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQ 626
Cdd:cd07840   78 sIYMVFEYMDH-DLTGLL--DNPEVKFTESQ-----IK---------CYMKQLLEGLQYLHSNGILHRDIKGSNILINND 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 627 LHVKISDLGLSREI---YSADY-YRVQSksslpiRWM-PPE----AIMYGkfsSDSDIWSFGVVLWEIFS 687
Cdd:cd07840  141 GVLKLADFGLARPYtkeNNADYtNRVIT------LWYrPPElllgATRYG---PEVDMWSVGCILAELFT 201
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
474-737 9.52e-19

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: 87.35  E-value: 9.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 474 RFMEE------LGECTFGKIYK------GHLYlpgmdhaqlvAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGA 541
Cdd:cd13996    3 RYLNDfeeielLGSGGFGSVYKvrnkvdGVTY----------AIKKIRLTEKSSASEKVLREVKALAKLNHPNIVRYYTA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 542 VTQEQPVCMLFEYMNQGDLHEFLimrsphsdvgcssdEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNI 621
Cdd:cd13996   73 WVEEPPLYIQMELCEGGTLRDWI--------------DRRNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNI 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 622 LI-GEQLHVKISDLGLSREI---------YSADYYRVQSKSSLPI---RWMPPEAIMYGKFSSDSDIWSFGVVLWEIfsf 688
Cdd:cd13996  139 FLdNDDLQVKIGDFGLATSIgnqkrelnnLNNNNNGNTSNNSVGIgtpLYASPEQLDGENYNEKADIYSLGIILFEM--- 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 223461072 689 glqpYYGFSNQ----EVIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRP 737
Cdd:cd13996  216 ----LHPFKTAmersTILTDLRNGILPESFKAKHPKEADLIQSLLSKNPEERP 264
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
522-749 1.33e-18

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: 87.11  E-value: 1.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 522 QEASLMAELHHPNIVCLLGAVTQEQP-VCMLFEYMNQGDLHEFLIMRSPHSDVGCSsdedgtvkssldhgdflHIAIQIA 600
Cdd:cd06620   52 RELQILHECHSPYIVSFYGAFLNENNnIIICMEYMDCGSLDKILKKKGPFPEEVLG-----------------KIAVAVL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 601 AGMEYL-SSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYS--ADYYRVQSKsslpirWMPPEAIMYGKFSSDSDIWS 677
Cdd:cd06620  115 EGLTYLyNVHRIIHRDIKPSNILVNSKGQIKLCDFGVSGELINsiADTFVGTST------YMSPERIQGGKYSVKSDVWS 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 678 FGVVLWEI------FSFGLQPYYGFSNQEVIEMVRKRQL------LPCSEDCPPRMYSLMTECWNEIPSRRPRFKDIH-- 743
Cdd:cd06620  189 LGLSIIELalgefpFAGSNDDDDGYNGPMGILDLLQRIVneppprLPKDRIFPKDLRDFVDRCLLKDPRERPSPQLLLdh 268
                        250
                 ....*....|....*..
gi 223461072 744 -----------VRLRSW 749
Cdd:cd06620  269 dpfiqavrasdVDLRAW 285
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
474-682 1.33e-18

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: 86.47  E-value: 1.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 474 RFMEELGECTFGKIYKGHLYLPGmdHAQLVAIKTLKDYNNPQqwtEFQQ-----EASLMAELHHPNIVCLLGAVTQEQPV 548
Cdd:cd14080    3 RLGKTIGEGSYSKVKLAEYTKSG--LKEKVACKIIDKKKAPK---DFLEkflprELEILRKLRHPNIIQVYSIFERGSKV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 549 CMLFEYMNQGDLHEFLIMRsphsdvgcssdedGTVKSSLDHGDFLhiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLH 628
Cdd:cd14080   78 FIFMEYAEHGDLLEYIQKR-------------GALSESQARIWFR----QLALAVQYLHSLDIAHRDLKCENILLDSNNN 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 629 VKISDLGLSREIySADYYRVQSKS---SLPirWMPPE---AIMYGKFSsdSDIWSFGVVL 682
Cdd:cd14080  141 VKLSDFGFARLC-PDDDGDVLSKTfcgSAA--YAAPEilqGIPYDPKK--YDIWSLGVIL 195
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
474-736 1.48e-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: 86.64  E-value: 1.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 474 RFMEELGECTFGKIYKGH-LYLPgmdhaQLVAIKTL-KDYNNPQQWTEFQ-----QEASLMAELH-HPNIVCLLGAVTQE 545
Cdd:cd13993    3 QLISPIGEGAYGVVYLAVdLRTG-----RKYAIKCLyKSGPNSKDGNDFQklpqlREIDLHRRVSrHPNIITLHDVFETE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 546 QPVCMLFEYMNQGDLHEflimrsphsdvgCSSDEDGTVKSSLDhgdFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGE 625
Cdd:cd13993   78 VAIYIVLEYCPNGDLFE------------AITENRIYVGKTEL---IKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQ 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 626 Q-LHVKISDLGLS-REIYSADyYRVQSKsslpiRWMPPEAIM-YGKFSS-----DSDIWSFGVVLWEIfSFGLQP----- 692
Cdd:cd13993  143 DeGTVKLCDFGLAtTEKISMD-FGVGSE-----FYMAPECFDeVGRSLKgypcaAGDIWSLGIILLNL-TFGRNPwkias 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 223461072 693 ------YYGFSNQEVIemvrKRQLLPCSEDCpprmYSLMTECWNEIPSRR 736
Cdd:cd13993  216 esdpifYDYYLNSPNL----FDVILPMSDDF----YNLLRQIFTVNPNNR 257
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
474-697 1.56e-18

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


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 86.11  E-value: 1.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 474 RFMEELGECTFGKIYKGHLYLPGMDhaqlVAIKTLKDYNNPQQWTefQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFE 553
Cdd:cd06614    3 KNLEKIGEGASGEVYKATDRATGKE----VAIKKMRLRKQNKELI--INEILIMKECKHPNIVDYYDSYLVGDELWVVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 554 YMNQGDLHEFLImrspHSDVGCSSDEDGTVkssldhgdflhiAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISD 633
Cdd:cd06614   77 YMDGGSLTDIIT----QNPVRMNESQIAYV------------CREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLAD 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223461072 634 LGLSREIYSAdyyrVQSKSSL---PIrWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFS 697
Cdd:cd06614  141 FGFAAQLTKE----KSKRNSVvgtPY-WMAPEVIKRKDYGPKVDIWSLGIMCIEMAE-GEPPYLEEP 201
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
476-742 1.69e-18

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: 86.31  E-value: 1.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYN-NPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd08529    5 LNKLGKGSFGVVYKVVRKVDG----RVYALKQIDISRmSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQGDLHEFLimrspHSDVGCSSDEDGTVKssldhgdflhIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd08529   81 AENGDLHSLI-----KSQRGRPLPEDQIWK----------FFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 635 GLSReIYSADYYRVQSKSSLPIrWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFglqpYYGFSNQEVIEMVRK---RQLL 711
Cdd:cd08529  146 GVAK-ILSDTTNFAQTIVGTPY-YLSPELCEDKPYNEKSDVWALGCVLYELCTG----KHPFEAQNQGALILKivrGKYP 219
                        250       260       270
                 ....*....|....*....|....*....|.
gi 223461072 712 PCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd08529  220 PISASYSQDLSQLIDSCLTKDYRQRPDTTEL 250
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
479-746 1.81e-18

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: 86.03  E-value: 1.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKghlylpgMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQG 558
Cdd:cd14156    1 IGSGFFSKVYK-------VTHGATGKVMVVKIYKNDVDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 559 DLHEFLimrsphsdvgcsSDEDgtvkSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVK---ISDLG 635
Cdd:cd14156   74 CLEELL------------AREE----LPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFG 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 636 LSREIYSADYYRVQSKSSL--PIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIfsFGLQPyygfSNQEVIEMVRK------ 707
Cdd:cd14156  138 LAREVGEMPANDPERKLSLvgSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEI--LARIP----ADPEVLPRTGDfgldvq 211
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 223461072 708 --RQLLPcseDCPPRMYSLMTECWNEIPSRRPRFKDIHVRL 746
Cdd:cd14156  212 afKEMVP---GCPEPFLDLAASCCRMDAFKRPSFAELLDEL 249
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
474-709 2.00e-18

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: 86.17  E-value: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 474 RFMEELGECTFGKIYKG-HlylpgMDHAQLVAIKTLKDYNNPQqwtEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLF 552
Cdd:cd06612    6 DILEKLGEGSYGSVYKAiH-----KETGQVVAIKVVPVEEDLQ---EIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 EYMNQGDLHEflIMRSphsdvgcssdedgtVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKIS 632
Cdd:cd06612   78 EYCGAGSVSD--IMKI--------------TNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLA 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223461072 633 DLGLSREIYSADYYRvQSKSSLPIrWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRKRQ 709
Cdd:cd06612  142 DFGVSGQLTDTMAKR-NTVIGTPF-WMAPEVIQEIGYNNKADIWSLGITAIEMAE-GKPPYSDIHPMRAIFMIPNKP 215
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
522-739 2.44e-18

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: 86.51  E-value: 2.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 522 QEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSPHSDVGCSSDedgtvkssldhgdfLHIAIQIAA 601
Cdd:cd14026   46 KEAEILHKARFSYILPILGICNEPEFLGIVTEYMTNGSLNELLHEKDIYPDVAWPLR--------------LRILYEIAL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 602 GMEYLS--SHFFVHKDLAARNILIGEQLHVKISDLGLSReiysadyYRV----QSKSSLP------IRWMPPEAIMYGKF 669
Cdd:cd14026  112 GVNYLHnmSPPLLHHDLKTQNILLDGEFHVKIADFGLSK-------WRQlsisQSRSSKSapeggtIIYMPPEEYEPSQK 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 670 SSDS---DIWSFGVVLWEIFSFGlQPYYGFSNQ-EVIEMVRKRQLLPCSEDCPP-------RMYSLMTECWNEIPSRRPR 738
Cdd:cd14026  185 RRASvkhDIYSYAIIMWEVLSRK-IPFEEVTNPlQIMYSVSQGHRPDTGEDSLPvdiphraTLINLIESGWAQNPDERPS 263

                 .
gi 223461072 739 F 739
Cdd:cd14026  264 F 264
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
475-718 2.62e-18

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: 86.78  E-value: 2.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQW-TEFQQEASLMAELHHPNIVCLLGAVTQEQPVC---- 549
Cdd:cd07864   11 IIGIIGEGTYGQVYKAKDKDTG----ELVALKKVRLDNEKEGFpITAIREIKILRQLNHRSVVNLKEIVTDKQDALdfkk 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 550 ------MLFEYMNQgDLHEFLimrsphsdvgcssdEDGTVKSSLDHgdFLHIAIQIAAGMEYLSSHFFVHKDLAARNILI 623
Cdd:cd07864   87 dkgafyLVFEYMDH-DLMGLL--------------ESGLVHFSEDH--IKSFMKQLLEGLNYCHKKNFLHRDIKCSNILL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 624 GEQLHVKISDLGLSReIYSADYYRVQSKSSLPIRWMPPEAIM-YGKFSSDSDIWSFGVVLWEIFSfgLQPYYGfSNQEV- 701
Cdd:cd07864  150 NNKGQIKLADFGLAR-LYNSEESRPYTNKVITLWYRPPELLLgEERYGPAIDVWSCGCILGELFT--KKPIFQ-ANQELa 225
                        250
                 ....*....|....*...
gi 223461072 702 -IEMVRKRqllpCSEDCP 718
Cdd:cd07864  226 qLELISRL----CGSPCP 239
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
515-748 2.66e-18

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: 85.62  E-value: 2.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 515 QQWTEFQQEASLMAEL-HHPNIVCLLGAVTQeqpvcmlFEYMNQGDLHEFLIMRSPHSDVGCSsdedgtVKSSLDHGDFL 593
Cdd:cd13975   39 KHWNDLALEFHYTRSLpKHERIVSLHGSVID-------YSYGGGSSIAVLLIMERLHRDLYTG------IKAGLSLEERL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 594 HIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSReiysADYYRVQSKSSLPIRwMPPEaIMYGKFSSDS 673
Cdd:cd13975  106 QIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCK----PEAMMSGSIVGTPIH-MAPE-LFSGKYDNSV 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 674 DIWSFGVVLWEIFSFGLQPYYGFSN--------QEVIEMVRKRQLLPCSEDCpprmYSLMTECWNEIPSRRPRFKDIHVR 745
Cdd:cd13975  180 DVYAFGILFWYLCAGHVKLPEAFEQcaskdhlwNNVRKGVRPERLPVFDEEC----WNLMEACWSGDPSQRPLLGIVQPK 255

                 ...
gi 223461072 746 LRS 748
Cdd:cd13975  256 LQG 258
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
479-707 3.01e-18

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: 85.60  E-value: 3.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGMDHA--QLVAIKTLKDYNNPQQwteFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMN 556
Cdd:cd14098    8 LGSGTFAEVKKAVEVETGKMRAikQIVKRKVAGNDKNLQL---FQREINILKSLEHPGIVRLIDWYEDDQHIYLVMEYVE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLImrsphsdvgcssdEDGtvksSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQ--LHVKISDL 634
Cdd:cd14098   85 GGDLMDFIM-------------AWG----AIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDdpVIVKISDF 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223461072 635 GLSREIYSADYYRVQSKSslpIRWMPPEAIMY------GKFSSDSDIWSFGVVLWEIFSFGLqPYYGFSNQEVIEMVRK 707
Cdd:cd14098  148 GLAKVIHTGTFLVTFCGT---MAYLAPEILMSkeqnlqGGYSNLVDMWSVGCLVYVMLTGAL-PFDGSSQLPVEKRIRK 222
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
479-702 5.03e-18

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: 85.28  E-value: 5.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGmdhaQLVAIKTLK----DYNNPQQ----WTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCM 550
Cdd:cd06628    8 IGSGSFGSVYLGMNASSG----ELMAVKQVElpsvSAENKDRkksmLDALQREIALLRELQHENIVQYLGSSSDANHLNI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 551 LFEYMNQGDLHEFLIMRSphsdvgcsSDEDGTVKSsldhgdFLHiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVK 630
Cdd:cd06628   84 FLEYVPGGSVATLLNNYG--------AFEESLVRN------FVR---QILKGLNYLHNRGIIHRDIKGANILVDNKGGIK 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223461072 631 ISDLGLSR--EIYSADYYRVQSKSSL--PIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVI 702
Cdd:cd06628  147 ISDFGISKklEANSLSTKNNGARPSLqgSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLT-GTHPFPDCTQMQAI 221
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
474-729 5.20e-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: 84.88  E-value: 5.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 474 RFMEELGECTFGKIYKGHLYLPGMDhaqlVAIKTL-KDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLF 552
Cdd:cd14072    3 RLLKTIGKGNFAKVKLARHVLTGRE----VAIKIIdKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 EYMNQGDLHEFLIMRsphsdvgcssdedGTVKSSLDHGDFLhiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKIS 632
Cdd:cd14072   79 EYASGGEVFDYLVAH-------------GRMKEKEARAKFR----QIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIA 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 633 DLGLSREiysadyYRVQSK-----SSLPirWMPPEAIMYGKFSS-DSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMV- 705
Cdd:cd14072  142 DFGFSNE------FTPGNKldtfcGSPP--YAAPELFQGKKYDGpEVDVWSLGVILYTLVS-GSLPFDGQNLKELRERVl 212
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 223461072 706 RKRQLLP--CSEDC-----------PPRMYSL---MTECW 729
Cdd:cd14072  213 RGKYRIPfyMSTDCenllkkflvlnPSKRGTLeqiMKDRW 252
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
472-705 5.99e-18

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


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 84.63  E-value: 5.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 472 AVRFMEELGECTFGKIYKGHLYLPGMD-HAQLVAIKTLKDYNnpqqwtEFQQEASLMAELHHPNIVCLLGAVTQEQPVCM 550
Cdd:cd14192    5 AVCPHEVLGGGRFGQVHKCTELSTGLTlAAKIIKVKGAKERE------EVKNEINIMNQLNHVNLIQLYDAFESKTNLTL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 551 LFEYMNQGDLHEFLImrsphsdvgcssDEdgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQL--H 628
Cdd:cd14192   79 IMEYVDGGELFDRIT------------DE----SYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTgnQ 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223461072 629 VKISDLGLSREIYSADYYRVQSKSSlpiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMV 705
Cdd:cd14192  143 IKIIDFGLARRYKPREKLKVNFGTP---EFLAPEVVNYDFVSFPTDMWSVGVITYMLLS-GLSPFLGETDAETMNNI 215
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
477-705 7.88e-18

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: 84.29  E-value: 7.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKghlyLPGMDHAQLVAIKTLKDYNNPQQwTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMN 556
Cdd:cd14191    8 ERLGSGKFGQVFR----LVEKKTKKVWAGKFFKAYSAKEK-ENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLImrsphsdvgcssDEDgtvkSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQL--HVKISDL 634
Cdd:cd14191   83 GGELFERII------------DED----FELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTgtKIKLIDF 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223461072 635 GLSREIYSADYYRVQSKSSlpiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMV 705
Cdd:cd14191  147 GLARRLENAGSLKVLFGTP---EFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMGDNDNETLANV 213
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
476-742 8.78e-18

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: 84.24  E-value: 8.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYkghLYLPGMDHAQLVaIKTLKDYNNPQQWTEF-QQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd08225    5 IKKIGEGSFGKIY---LAKAKSDSEHCV-IKEIDLTKMPVKEKEAsKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQGDLhefliMRSPHSDVGCSSDEDgtvkssldhgDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHV-KISD 633
Cdd:cd08225   81 CDGGDL-----MKRINRQRGVLFSED----------QILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGD 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 634 LGLSREIYSADYYrVQSKSSLPIrWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGlQPYYGFSNQEVIEMVRKRQLLPC 713
Cdd:cd08225  146 FGIARQLNDSMEL-AYTCVGTPY-YLSPEICQNRPYNNKTDIWSLGCVLYELCTLK-HPFEGNNLHQLVLKICQGYFAPI 222
                        250       260
                 ....*....|....*....|....*....
gi 223461072 714 SEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd08225  223 SPNFSRDLRSLISQLFKVSPRDRPSITSI 251
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
477-742 9.50e-18

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: 84.14  E-value: 9.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLylpgMDHAQLVAIKTL--KDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd14099    7 KFLGKGGFAKCYEVTD----MSTGKVYAGKVVpkSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQGDLHEFLIMRSPHSDVGCSsdedgtvkssldhgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd14099   83 CSNGSLMELLKRRKALTEPEVR-----------------YFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDF 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 635 GLSREIYSADyyrvQSKSSL---PiRWMPPEaIMYGK--FSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVIEMVRKRQ 709
Cdd:cd14099  146 GLAARLEYDG----ERKKTLcgtP-NYIAPE-VLEKKkgHSFEVDIWSLGVILYTLL-VGKPPFETSDVKETYKRIKKNE 218
                        250       260       270
                 ....*....|....*....|....*....|....
gi 223461072 710 -LLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14099  219 ySFPSHLSISDEAKDLIRSMLQPDPTKRPSLDEI 252
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
477-741 1.15e-17

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: 84.22  E-value: 1.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMN 556
Cdd:cd06609    7 ERIGKGSFGEVYKGIDKRTN----QVVAIKVIDLEEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEYCG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLIMrsphsdvgCSSDEDgtvkssldhgdflHIAI---QIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISD 633
Cdd:cd06609   83 GGSVLDLLKP--------GPLDET-------------YIAFilrEVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLAD 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 634 LGLSREIYSAdyyrvQSKSS----LPIrWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIemvrkrQ 709
Cdd:cd06609  142 FGVSGQLTST-----MSKRNtfvgTPF-WMAPEVIKQSGYDEKADIWSLGITAIELAK-GEPPLSDLHPMRVL------F 208
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 223461072 710 LLPCSEdcPPR----MYS-----LMTECWNEIPSRRPRFKD 741
Cdd:cd06609  209 LIPKNN--PPSlegnKFSkpfkdFVELCLNKDPKERPSAKE 247
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
476-707 1.34e-17

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: 84.24  E-value: 1.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLkdYNNPQQWTEFQ--QEASLMAELHHPNIVCLLGAVTQEQPVCMLFE 553
Cdd:cd07870    5 LEKLGEGSYATVYKGISRING----QLVALKVI--SMKTEEGVPFTaiREASLLKGLKHANIVLLHDIIHTKETLTFVFE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 554 YMnQGDLHEFLImrsphsdvgcssdedgtvksslDHGDFLH------IAIQIAAGMEYLSSHFFVHKDLAARNILIGEQL 627
Cdd:cd07870   79 YM-HTDLAQYMI----------------------QHPGGLHpynvrlFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLG 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 628 HVKISDLGLSR--EIYSADYyrvqSKSSLPIRWMPPEAIMYG-KFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNqeVIEM 704
Cdd:cd07870  136 ELKLADFGLARakSIPSQTY----SSEVVTLWYRPPDVLLGAtDYSSALDIWGAGCIFIEMLQ-GQPAFPGVSD--VFEQ 208

                 ...
gi 223461072 705 VRK 707
Cdd:cd07870  209 LEK 211
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
479-687 1.40e-17

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: 84.49  E-value: 1.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLylpgmdHAQLVAIKTLKDyNNPQQWT----EFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd14159    1 IGEGGFGCVYQAVM------RNTEYAVKRLKE-DSELDWSvvknSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQGDLHEFLimrspHSDVGCSSdedgtvkssLDHGDFLHIAIQIAAGMEYLSSH--FFVHKDLAARNILIGEQLHVKIS 632
Cdd:cd14159   74 LPNGSLEDRL-----HCQVSCPC---------LSWSQRLHVLLGTARAIQYLHSDspSLIHGDVKSSNILLDAALNPKLG 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223461072 633 DLGLSReiySADYYRVQSKSSLPIR---------WMPPEAIMYGKFSSDSDIWSFGVVLWEIFS 687
Cdd:cd14159  140 DFGLAR---FSRRPKQPGMSSTLARtqtvrgtlaYLPEEYVKTGTLSVEIDVYSFGVVLLELLT 200
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
527-748 1.43e-17

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: 83.61  E-value: 1.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 527 MAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLimrsPHSDVGCssdeDGTVKSSLdhgdflhiAIQIAAGMEYL 606
Cdd:cd14043   50 LRELRHENVNLFLGLFVDCGILAIVSEHCSRGSLEDLL----RNDDMKL----DWMFKSSL--------LLDLIKGMRYL 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 607 SSHFFVHKDLAARNILIGEQLHVKISDLGLSrEIYSADYYRVQSKSSLPIRWMPPE----AIMYGKFSSDSDIWSFGVVL 682
Cdd:cd14043  114 HHRGIVHGRLKSRNCVVDGRFVLKITDYGYN-EILEAQNLPLPEPAPEELLWTAPEllrdPRLERRGTFPGDVFSFAIIM 192
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223461072 683 WEIFSFGLqPY--YGFSNQEVIEMVRKRQLLpC----SED-CPPRMYSLMTECWNEIPSRRPRFKDIHVRLRS 748
Cdd:cd14043  193 QEVIVRGA-PYcmLGLSPEEIIEKVRSPPPL-CrpsvSMDqAPLECIQLMKQCWSEAPERRPTFDQIFDQFKS 263
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
501-748 1.60e-17

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: 83.80  E-value: 1.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 501 QLVAIKTLkDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTqEQP-VCMLFEYMNQGDLHEflIMRSPHSDVgcssde 579
Cdd:cd14042   31 NLVAIKKV-NKKRIDLTREVLKELKHMRDLQHDNLTRFIGACV-DPPnICILTEYCPKGSLQD--ILENEDIKL------ 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 580 DGTVKSSLDHgdflhiaiQIAAGMEYL-SSHFFVHKDLAARNILIGEQLHVKISDLGLsREIYSADYYRVQSKSSLPIR- 657
Cdd:cd14042  101 DWMFRYSLIH--------DIVKGMHYLhDSEIKSHGNLKSSNCVVDSRFVLKITDFGL-HSFRSGQEPPDDSHAYYAKLl 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 658 WMPPEAIMYGKFSS----DSDIWSFGVVLWEIFS----FGLQPYyGFSNQEVIEMVRKRQLLP------CSEDCPPRMYS 723
Cdd:cd14042  172 WTAPELLRDPNPPPpgtqKGDVYSFGIILQEIATrqgpFYEEGP-DLSPKEIIKKKVRNGEKPpfrpslDELECPDEVLS 250
                        250       260
                 ....*....|....*....|....*
gi 223461072 724 LMTECWNEIPSRRPRFKDIHVRLRS 748
Cdd:cd14042  251 LMQRCWAEDPEERPDFSTLRNKLKK 275
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
471-736 1.82e-17

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: 83.68  E-value: 1.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 471 SAVRFMEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQWTEFQQEASLMAELHH---PNIVCLLGAVTQEQP 547
Cdd:cd06917    1 SLYRRLELVGRGSYGAVYRGYHVKTG----RVVALKVLNLDTDDDDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 548 VCMLFEYMnqgdlheflimrsphsdvgcssdEDGTVKSSLDHG--DFLHIAI---QIAAGMEYLSSHFFVHKDLAARNIL 622
Cdd:cd06917   77 LWIIMDYC-----------------------EGGSIRTLMRAGpiAERYIAVimrEVLVALKFIHKDGIIHRDIKAANIL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 623 IGEQLHVKISDLGLSREIYSADYYRvQSKSSLPIrWMPPEAIMYGK-FSSDSDIWSFGVVLWEIfSFGLQPYYGfsnqev 701
Cdd:cd06917  134 VTNTGNVKLCDFGVAASLNQNSSKR-STFVGTPY-WMAPEVITEGKyYDTKADIWSLGITTYEM-ATGNPPYSD------ 204
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 223461072 702 IEMVRKRQLLPCSEdcPPRM----YS-LMTE----CWNEIPSRR 736
Cdd:cd06917  205 VDALRAVMLIPKSK--PPRLegngYSpLLKEfvaaCLDEEPKDR 246
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
477-737 1.83e-17

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


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 83.86  E-value: 1.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLylpgmdHAQLVAIKTL--KDynnPQQW---TEFQQeaSLMaeLHHPNIVCLLGA-------VTQ 544
Cdd:cd14056    1 KTIGKGRYGEVWLGKY------RGEKVAVKIFssRD---EDSWfreTEIYQ--TVM--LRHENILGFIAAdikstgsWTQ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 545 eqpVCMLFEYMNQGDLHEFLimrsphsdvgcssdedgtVKSSLDHGDFLHIAIQIAAGMEYLSSHFF--------VHKDL 616
Cdd:cd14056   68 ---LWLITEYHEHGSLYDYL------------------QRNTLDTEEALRLAYSAASGLAHLHTEIVgtqgkpaiAHRDL 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 617 AARNILIGEQLHVKISDLGL-------SREIYSADYYRVQSKsslpiRWMPPEAI---MYGK-FSS--DSDIWSFGVVLW 683
Cdd:cd14056  127 KSKNILVKRDGTCCIADLGLavrydsdTNTIDIPPNPRVGTK-----RYMAPEVLddsINPKsFESfkMADIYSFGLVLW 201
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223461072 684 EIF----SFGL-----QPYYGF-----SNQEVIEMV---RKRQLLP---CSEDCPPRMYSLMTECWNEIPSRRP 737
Cdd:cd14056  202 EIArrceIGGIaeeyqLPYFGMvpsdpSFEEMRKVVcveKLRPPIPnrwKSDPVLRSMVKLMQECWSENPHARL 275
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
476-685 2.14e-17

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: 83.62  E-value: 2.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLK----DYNNPQQWTefqQEASLMAELHHPNIVCLLGAVTQEQPVCML 551
Cdd:cd07861    5 IEKIGEGTYGVVYKGRNKKTG----QIVAMKKIRleseEEGVPSTAI---REISLLKELQHPNIVCLEDVLMQENRLYLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMNQgDLHEFLimrspHSDVGCSSDEDGTVKSSLdhgdflhiaIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKI 631
Cdd:cd07861   78 FEFLSM-DLKKYL-----DSLPKGKYMDAELVKSYL---------YQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKL 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 223461072 632 SDLGLSREIysADYYRVQSKSSLPIRWMPPEAIMYG-KFSSDSDIWSFGVVLWEI 685
Cdd:cd07861  143 ADFGLARAF--GIPVRVYTHEVVTLWYRAPEVLLGSpRYSTPVDIWSIGTIFAEM 195
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
501-743 2.20e-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: 83.42  E-value: 2.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 501 QLVAIKTLK--DYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMrsphsdVGCSsD 578
Cdd:cd05579   19 DLYAIKVIKkrDMIRKNQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDLYSLLEN------VGAL-D 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 579 EDgTVKssldhgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLS------REIYSADYYRVQSKS 652
Cdd:cd05579   92 ED-VAR---------IYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSkvglvrRQIKLSIQKKSNGAP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 653 SLPIR-------WMPPEAIMYGKFSSDSDIWSFGVVLWEiFSFGLQPYYGFSNQEVIEMVRKRQL-LPCSEDCPPRMYSL 724
Cdd:cd05579  162 EKEDRrivgtpdYLAPEILLGQGHGKTVDWWSLGVILYE-FLVGIPPFHAETPEEIFQNILNGKIeWPEDPEVSDEAKDL 240
                        250       260       270
                 ....*....|....*....|....*....|.
gi 223461072 725 MTECWNEIPSRR------------PRFKDIH 743
Cdd:cd05579  241 ISKLLTPDPEKRlgakgieeiknhPFFKGID 271
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
170-288 2.23e-17

Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This domain of unknown function has been independently identified by several groups. The domain contains 10 conserved cysteines.


Pssm-ID: 460190  Cd Length: 116  Bit Score: 78.76  E-value: 2.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  170 CQPYRGIACARFIGNRTVYMESLHMQGEIENQITAAFTMIGTSSHLSD-KCSQFAIPSLCHYAFPYCDETSSVPKPRDLC 248
Cdd:pfam01392   1 CEPITLPMCLGLGYNATVFPNLLGHQTQEEAELSLAYLVLSEFEPLVDlSCSPSLRLFLCSLYFPPCTLGPSPKPVCPPC 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 223461072  249 RDECEVLENvLCQTEYIFARSNPMILMRLklpNCEDLPQP 288
Cdd:pfam01392  81 RSLCEEVRY-GCEPLLEEAKFGFSWPEFL---DCDSLPAD 116
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
503-712 2.40e-17

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: 83.13  E-value: 2.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 503 VAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGavTQEQP--VCMLFEYMNQGDLHEFLIMRSPHSdvgcssdED 580
Cdd:cd14201   35 VAIKSINKKNLSKSQILLGKEIKILKELQHENIVALYD--VQEMPnsVFLVMEYCNGGDLADYLQAKGTLS-------ED 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 581 gTVKSsldhgdFLHiaiQIAAGMEYLSSHFFVHKDLAARNILIG---------EQLHVKISDLGLSREIYSADYYRVQSK 651
Cdd:cd14201  106 -TIRV------FLQ---QIAAAMRILHSKGIIHRDLKPQNILLSyasrkkssvSGIRIKIADFGFARYLQSNMMAATLCG 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223461072 652 SSLpirWMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVIEMVRK-RQLLP 712
Cdd:cd14201  176 SPM---YMAPEVIMSQHYDAKADLWSIGTVIYQCL-VGKPPFQANSPQDLRMFYEKnKNLQP 233
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
522-707 2.46e-17

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: 82.70  E-value: 2.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 522 QEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLImrspHSDVGCSSDedgtVKssldhgDFLHiaiQIAA 601
Cdd:cd14006   38 REISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELLDRLA----ERGSLSEEE----VR------TYMR---QLLE 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 602 GMEYLSSHFFVHKDLAARNILIGEQL--HVKISDLGLSREIYSADYYRVQsKSSLpiRWMPPEAIMYGKFSSDSDIWSFG 679
Cdd:cd14006  101 GLQYLHNHHILHLDLKPENILLADRPspQIKIIDFGLARKLNPGEELKEI-FGTP--EFVAPEIVNGEPVSLATDMWSIG 177
                        170       180
                 ....*....|....*....|....*...
gi 223461072 680 VVLWEIFSfGLQPYYGFSNQEVIEMVRK 707
Cdd:cd14006  178 VLTYVLLS-GLSPFLGEDDQETLANISA 204
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
476-700 2.70e-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: 83.30  E-value: 2.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLK-DYNNPQQWTEFQqEASLMAELHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd07836    5 LEKLGEGTYATVYKGRNRTTG----EIVALKEIHlDAEEGTPSTAIR-EISLMKELKHENIVRLHDVIHTENKLMLVFEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQgDLHEFLimrSPHSDVGcsSDEDGTVKSsldhgdFLHiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd07836   80 MDK-DLKKYM---DTHGVRG--ALDPNTVKS------FTY---QLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADF 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223461072 635 GLSREI------YSAD----YYRvqsksslpirwmPPEAIMYGK-FSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQE 700
Cdd:cd07836  145 GLARAFgipvntFSNEvvtlWYR------------APDVLLGSRtYSTSIDIWSVGCIMAEMIT-GRPLFPGTNNED 208
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
480-738 2.90e-17

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: 82.74  E-value: 2.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 480 GECTFGKIYKGHlylpGMDHAQLVAIKTLKDY-NNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQG 558
Cdd:cd06626    9 GEGTFGKVYTAV----NLDTGELMAMKEIRFQdNDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQEG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 559 DLHEFLimrsphsDVGCSSDEDGTVKssldhgdflhIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSR 638
Cdd:cd06626   85 TLEELL-------RHGRILDEAVIRV----------YTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 639 EIYS----ADYYRVQSKSSLPIrWMPPEAIMYGKFSSD---SDIWSFGVVLWEIFSfGLQPYYGFSNQEVI----EMVRK 707
Cdd:cd06626  148 KLKNntttMAPGEVNSLVGTPA-YMAPEVITGNKGEGHgraADIWSLGCVVLEMAT-GKRPWSELDNEWAImyhvGMGHK 225
                        250       260       270
                 ....*....|....*....|....*....|.
gi 223461072 708 RQlLPCSEDCPPRMYSLMTECWNEIPSRRPR 738
Cdd:cd06626  226 PP-IPDSLQLSPEGKDFLSRCLESDPKKRPT 255
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
476-742 3.08e-17

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: 83.18  E-value: 3.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGhlylpgMDH--AQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFE 553
Cdd:cd06640    9 LERIGKGSFGEVFKG------IDNrtQQVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 554 YMNQGDLHEFLimrsphsdvgcssdedgtVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISD 633
Cdd:cd06640   83 YLGGGSALDLL------------------RAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLAD 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 634 LGLSREIYSADYYRvQSKSSLPIrWMPPEAIMYGKFSSDSDIWSFGVVLWEIfSFGLQPYYGFSNQEVIEMVRKRQLLPC 713
Cdd:cd06640  145 FGVAGQLTDTQIKR-NTFVGTPF-WMAPEVIQQSAYDSKADIWSLGITAIEL-AKGEPPNSDMHPMRVLFLIPKNNPPTL 221
                        250       260
                 ....*....|....*....|....*....
gi 223461072 714 SEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd06640  222 VGDFSKPFKEFIDACLNKDPSFRPTAKEL 250
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
60-143 3.54e-17

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 77.43  E-value: 3.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  60 LDEPMNNITTSLGQTAELHCKVSGNPPPSIRWFKNDAPVVQEPRRISFRAtnygSRLRIRNLDTTDTGYFQCVATN--GK 137
Cdd:cd20978    4 IQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVED----GTLTIINVQPEDTGYYGCVATNeiGD 79

                 ....*.
gi 223461072 138 KVVSTT 143
Cdd:cd20978   80 IYTETL 85
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
477-687 4.47e-17

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: 82.32  E-value: 4.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHlylpGMDHAQLVAIKTLKdyNNPQQWTEFQQEASLMAELH------HPNIVCLLGAVTQEQPVCM 550
Cdd:cd14133    5 EVLGKGTFGQVVKCY----DLLTGEEVALKIIK--NNKDYLDQSLDEIRLLELLNkkdkadKYHIVRLKDVFYFKNHLCI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 551 LFEYMNQgDLHEFLIMrsphsdvgcssdedgTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQ--LH 628
Cdd:cd14133   79 VFELLSQ-NLYEFLKQ---------------NKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYsrCQ 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 223461072 629 VKISDLGLSREIYSADYYRVQSKSslpirWMPPEAIMYGKFSSDSDIWSFGVVLWEIFS 687
Cdd:cd14133  143 IKIIDFGSSCFLTQRLYSYIQSRY-----YRAPEVILGLPYDEKIDMWSLGCILAELYT 196
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
479-748 5.26e-17

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: 81.92  E-value: 5.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLylpgmdHAQLVAIKTlkdYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQeqPVCMLFEYMNQG 558
Cdd:cd14068    2 LGDGGFGSVYRAVY------RGEDVAVKI---FNKHTSFRLLRQELVVLSHLHHPSLVALLAAGTA--PRMLVMELAPKG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 559 DLHEFLimrsphsdvgcsSDEDGTVKSSLDHgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILI-----GEQLHVKISD 633
Cdd:cd14068   71 SLDALL------------QQDNASLTRTLQH----RIALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIAD 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 634 LGLSREIYSADyyrVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYG--FSNqEVIEMVRKRQLL 711
Cdd:cd14068  135 YGIAQYCCRMG---IKTSEGTPGFRAPEVARGNVIYNQQADVYSFGLLLYDILTCGERIVEGlkFPN-EFDELAIQGKLP 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 223461072 712 -PCSE-DCP--PRMYSLMTECWNEIPSRRPRFKDIHVRLRS 748
Cdd:cd14068  211 dPVKEyGCApwPGVEALIKDCLKENPQCRPTSAQVFDILNS 251
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
475-737 5.59e-17

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: 81.97  E-value: 5.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLK-----DYnnpqqwTEFQQEASLMAELHHPNIVCLLGAVTQEQP-- 547
Cdd:cd06613    4 LIQRIGSGTYGDVYKARNIATG----ELAAVKVIKlepgdDF------EIIQQEISMLKECRHPNIVAYFGSYLRRDKlw 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 548 VCMlfEYMNQGDLHEFLIMRSPHSDVGCSsdedgtvkssldhgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQL 627
Cdd:cd06613   74 IVM--EYCGGGSLQDIYQVTGPLSELQIA-----------------YVCRETLKGLAYLHSTGKIHRDIKGANILLTEDG 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 628 HVKISDLGLSREIySADYYRVQSKSSLPIrWMPPEAI---MYGKFSSDSDIWSFGVVLWEIfSFGLQPYYGFSNQEVIEM 704
Cdd:cd06613  135 DVKLADFGVSAQL-TATIAKRKSFIGTPY-WMAPEVAaveRKGGYDGKCDIWALGITAIEL-AELQPPMFDLHPMRALFL 211
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 223461072 705 VRKRQLLPCS----EDCPPRMYSLMTECWNEIPSRRP 737
Cdd:cd06613  212 IPKSNFDPPKlkdkEKWSPDFHDFIKKCLTKNPKKRP 248
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
479-696 5.72e-17

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: 81.60  E-value: 5.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKI----YKGHlylpgmdhAQLVAIKTLKDYNNPQQwtEFQQEASLMAEL-HHPNIVCLLGaVTQEQPVCMLF- 552
Cdd:cd13987    1 LGEGTYGKVllavHKGS--------GTKMALKFVPKPSTKLK--DFLREYNISLELsVHPHIIKTYD-VAFETEDYYVFa 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 -EYMNQGDLHEFLImrsphSDVGCssDEDgTVKSsldhgdflhIAIQIAAGMEYLSSHFFVHKDLAARNILI--GEQLHV 629
Cdd:cd13987   70 qEYAPYGDLFSIIP-----PQVGL--PEE-RVKR---------CAAQLASALDFMHSKNLVHRDIKPENVLLfdKDCRRV 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 630 KISDLGLSREIYSadyyRVQSKS-SLPirWMPPE---AIMYGKFSSD--SDIWSFGVVL---------WEIFSFGLQPYY 694
Cdd:cd13987  133 KLCDFGLTRRVGS----TVKRVSgTIP--YTAPEvceAKKNEGFVVDpsIDVWAFGVLLfccltgnfpWEKADSDDQFYE 206

                 ..
gi 223461072 695 GF 696
Cdd:cd13987  207 EF 208
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
479-737 5.98e-17

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: 81.63  E-value: 5.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGMDhaqlVAIKTLK-DYNNPQQWTE---FQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd06625    8 LGQGAFGQVYLCYDADTGRE----LAVKQVEiDPINTEASKEvkaLECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQGDLHEFLimrsphSDVGCSSdEDGTVKSSLdhgdflhiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd06625   84 MPGGSVKDEI------KAYGALT-ENVTRKYTR----------QILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDF 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 635 GLSReiysadyyRVQS-KSSLPIR-------WMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVR 706
Cdd:cd06625  147 GASK--------RLQTiCSSTGMKsvtgtpyWMSPEVINGEGYGRKADIWSVGCTVVEMLT-TKPPWAEFEPMAAIFKIA 217
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 223461072 707 KRQLLP-----CSEDCpprmYSLMTECWNEIPSRRP 737
Cdd:cd06625  218 TQPTNPqlpphVSEDA----RDFLSLIFVRNKKQRP 249
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
476-725 6.00e-17

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: 82.10  E-value: 6.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGHlylpGMDHAQLVAIKTLK-DYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd07839    5 LEKIGEGTYGTVFKAK----NRETHEIVALKRVRlDDDDEGVPSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVFEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQgDLHEFLimrsphsDvGCSSDEDGTVKSSLdhgdflhiAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd07839   81 CDQ-DLKKYF-------D-SCNGDIDPEIVKSF--------MFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADF 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 635 GLSREI------YSAD----YYRvqsksslpirwmPPEAIMYGKFSSDS-DIWSFGVVLWEIFSFGlQPYygFSNQEVIE 703
Cdd:cd07839  144 GLARAFgipvrcYSAEvvtlWYR------------PPDVLFGAKLYSTSiDMWSAGCIFAELANAG-RPL--FPGNDVDD 208
                        250       260
                 ....*....|....*....|....
gi 223461072 704 MVRK--RQLLPCSEDCPPRMYSLM 725
Cdd:cd07839  209 QLKRifRLLGTPTEESWPGVSKLP 232
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
476-742 9.27e-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: 81.64  E-value: 9.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGhlylpgMDH--AQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFE 553
Cdd:cd06642    9 LERIGKGSFGEVYKG------IDNrtKEVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 554 YMNQGDLHEFLimrSPhsdvgcssdedgtvkSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISD 633
Cdd:cd06642   83 YLGGGSALDLL---KP---------------GPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLAD 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 634 LGLSREIYSADYYRvQSKSSLPIrWMPPEAIMYGKFSSDSDIWSFGVVLWEIfSFGLQPYYGFSNQEVIEMVRKrqllpc 713
Cdd:cd06642  145 FGVAGQLTDTQIKR-NTFVGTPF-WMAPEVIKQSAYDFKADIWSLGITAIEL-AKGEPPNSDLHPMRVLFLIPK------ 215
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 223461072 714 seDCPPRM---YS-----LMTECWNEIPSRRPRFKDI 742
Cdd:cd06642  216 --NSPPTLegqHSkpfkeFVEACLNKDPRFRPTAKEL 250
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
498-742 1.08e-16

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: 80.93  E-value: 1.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 498 DHAQLVAIKTLK-DYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSphsdvgcs 576
Cdd:cd08220   23 DDNKLVIIKQIPvEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYAPGGTLFEYIQQRK-------- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 577 sdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGE-QLHVKISDLGLSREIYSadyyrvQSKSSLP 655
Cdd:cd08220   95 -------GSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKkRTVVKIGDFGISKILSS------KSKAYTV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 656 IR---WMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfgLQPYYGFSNQEVIEM-VRKRQLLPCSEDCPPRMYSLMTECWNE 731
Cdd:cd08220  162 VGtpcYISPELCEGKPYNQKSDIWALGCVLYELAS--LKRAFEAANLPALVLkIMRGTFAPISDRYSEELRHLILSMLHL 239
                        250
                 ....*....|.
gi 223461072 732 IPSRRPRFKDI 742
Cdd:cd08220  240 DPNKRPTLSEI 250
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
516-742 1.26e-16

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: 80.48  E-value: 1.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 516 QWTEFQQEaSLMaELHHPNIVCLLGAVTQEQP------VCMLFEYMNQGDLHEFLimrsphsDVGCSSDEDgTVKssldh 589
Cdd:cd14012   43 QLLEKELE-SLK-KLRHPNLVSYLAFSIERRGrsdgwkVYLLTEYAPGGSLSELL-------DSVGSVPLD-TAR----- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 590 gdflHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLH---VKISDLGLSREIYSADyYRVQSKSSLPIRWMPPEAI-M 665
Cdd:cd14012  108 ----RWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGtgiVKLTDYSLGKTLLDMC-SRGSLDEFKQTYWLPPELAqG 182
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223461072 666 YGKFSSDSDIWSFGVVLWEIfSFGlqpyygfsnQEVIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14012  183 SKSPTRKTDVWDLGLLFLQM-LFG---------LDVLEKYTSPNPVLVSLDLSASLQDFLSKCLSLDPKKRPTALEL 249
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
478-744 1.90e-16

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: 80.39  E-value: 1.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 478 ELGECTFGKIYKGHLYLPGmdhaQLVAIKTLK--DYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYM 555
Cdd:cd08224    7 KIGKGQFSVVYRARCLLDG----RLVALKKVQifEMMDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVLELA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQGDLHEFLIMRSPHsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLG 635
Cdd:cd08224   83 DAGDLSRLIKHFKKQ-------------KRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 636 LSReIYSADYYRVQSKSSLPIrWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfgLQ-PYYGfSNQEVIEMVRKrqllpcS 714
Cdd:cd08224  150 LGR-FFSSKTTAAHSLVGTPY-YMSPERIREQGYDFKSDIWSLGCLLYEMAA--LQsPFYG-EKMNLYSLCKK------I 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 223461072 715 EDC-----PPRMYS-----LMTECWNEIPSRRPRFKDIHV 744
Cdd:cd08224  219 EKCeypplPADLYSqelrdLVAACIQPDPEKRPDISYVLD 258
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
476-717 2.12e-16

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: 80.03  E-value: 2.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGHlylpGMDHAQLVAIKTLKDYNNPQQW-TEF-QQEASLMAELHHPNIVCLLGAVTQEQPVCMLFE 553
Cdd:cd14162    5 GKTLGHGSYAVVKKAY----STKHKCKVAIKIVSKKKAPEDYlQKFlPREIEVIKGLKHPNLICFYEAIETTSRVYIIME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 554 YMNQGDLHEFLimrspHSDVGCSSDEDGTvkssldhgdFLHiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISD 633
Cdd:cd14162   81 LAENGDLLDYI-----RKNGALPEPQARR---------WFR---QLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITD 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 634 LGLSREIYSA-DYYRVQSKS---SLPirWMPPE---AIMYGKFSsdSDIWSFGVVLWEIFsFGLQPYYGfSNQEVI-EMV 705
Cdd:cd14162  144 FGFARGVMKTkDGKPKLSETycgSYA--YASPEilrGIPYDPFL--SDIWSMGVVLYTMV-YGRLPFDD-SNLKVLlKQV 217
                        250
                 ....*....|....*.
gi 223461072 706 RKRQLLP----CSEDC 717
Cdd:cd14162  218 QRRVVFPknptVSEEC 233
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
65-135 2.33e-16

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 74.52  E-value: 2.33e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223461072   65 NNITTSLGQTAELHCKVSGNPPPSIRWFKNDAPVVQEPRRISFRaTNYGSRLRIRNLDTTDTGYFQCVATN 135
Cdd:pfam13927   9 SSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSL-SGSNSTLTISNVTRSDAGTYTCVASN 78
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
476-718 2.45e-16

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: 80.81  E-value: 2.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGHLYLPgmdhAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYM 555
Cdd:cd07872   11 LEKLGEGTYATVFKGRSKLT----ENLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQgDLHEFLimrsphsdvgcssDEDGTVKSSLDHGDFLHiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLG 635
Cdd:cd07872   87 DK-DLKQYM-------------DDCGNIMSMHNVKIFLY---QILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 636 LSREiySADYYRVQSKSSLPIRWMPPEAIM-YGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRKRQLLPCS 714
Cdd:cd07872  150 LARA--KSVPTKTYSNEVVTLWYRPPDVLLgSSEYSTQIDMWGVGCIFFEMAS-GRPLFPGSTVEDELHLIFRLLGTPTE 226

                 ....
gi 223461072 715 EDCP 718
Cdd:cd07872  227 ETWP 230
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
476-718 2.87e-16

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: 80.43  E-value: 2.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYM 555
Cdd:cd07873    7 LDKLGEGTYATVYKGRSKLTD----NLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQgDLHEFLimrsphsdvgcssDEDGTVKSSLDHGDFLHiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLG 635
Cdd:cd07873   83 DK-DLKQYL-------------DDCGNSINMHNVKLFLF---QLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 636 LSR--EIYSADYyrvqsKSSLPIRWMPPEAIMYG--KFSSDSDIWSFGVVLWEIfSFGLQPYYGFSNQEVIEMVRKRQLL 711
Cdd:cd07873  146 LARakSIPTKTY-----SNEVVTLWYRPPDILLGstDYSTQIDMWGVGCIFYEM-STGRPLFPGSTVEEQLHFIFRILGT 219

                 ....*..
gi 223461072 712 PCSEDCP 718
Cdd:cd07873  220 PTEETWP 226
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
478-741 2.89e-16

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: 80.07  E-value: 2.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 478 ELGECTFGKIYKGHLYLPGMdhaqLVAIKTLkDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQ 557
Cdd:cd06643   12 ELGDGAFGKVYKAQNKETGI----LAAAKVI-DTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 558 GDLHEFLI-----MRSPHSDVGCssdedgtvKSSLDhgdflhiaiqiaaGMEYLSSHFFVHKDLAARNILIGEQLHVKIS 632
Cdd:cd06643   87 GAVDAVMLelerpLTEPQIRVVC--------KQTLE-------------ALVYLHENKIIHRDLKAGNILFTLDGDIKLA 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 633 DLGLSreiySADYYRVQSKSSL---PIrWMPPEAIMYgKFSSD------SDIWSFGVVLWEIFSfgLQPyygfSNQEVIE 703
Cdd:cd06643  146 DFGVS----AKNTRTLQRRDSFigtPY-WMAPEVVMC-ETSKDrpydykADVWSLGVTLIEMAQ--IEP----PHHELNP 213
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 223461072 704 MvrkRQLLPCSEDCPPRMYSlmtecwneiPSR-RPRFKD 741
Cdd:cd06643  214 M---RVLLKIAKSEPPTLAQ---------PSRwSPEFKD 240
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
476-685 2.93e-16

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: 80.85  E-value: 2.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYkghlYLPGMDHAQLVAIKTLKdYNNPQ---QWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLF 552
Cdd:cd06633   26 LHEIGHGSFGAVY----FATNSHTNEVVAIKKMS-YSGKQtneKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVM 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 EYM--NQGDLHEflIMRSPHSDVGCSSdedgtvkssLDHGdflhiAIQiaaGMEYLSSHFFVHKDLAARNILIGEQLHVK 630
Cdd:cd06633  101 EYClgSASDLLE--VHKKPLQEVEIAA---------ITHG-----ALQ---GLAYLHSHNMIHRDIKAGNILLTEPGQVK 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 223461072 631 ISDLGLSREIYSADyyrvqSKSSLPIrWMPPEAIMY---GKFSSDSDIWSFGVVLWEI 685
Cdd:cd06633  162 LADFGSASIASPAN-----SFVGTPY-WMAPEVILAmdeGQYDGKVDIWSLGITCIEL 213
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
476-742 3.24e-16

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


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 79.84  E-value: 3.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKdYNNpqqwTEFQQEASLMAELHHPNIVCLLGAVTQEQPvCMLFEYM 555
Cdd:cd14047   11 IELIGSGGFGQVFKAKHRIDG----KTYAIKRVK-LNN----EKAEREVKALAKLDHPNIVRYNGCWDGFDY-DPETSSS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQGDLHE---FLIMRSphsdvgCssdEDGTVKS--------SLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIG 624
Cdd:cd14047   81 NSSRSKTkclFIQMEF------C---EKGTLESwiekrngeKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 625 EQLHVKISDLGLsreIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQpyyGFSNQEVIEM 704
Cdd:cd14047  152 DTGKVKIGDFGL---VTSLKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCDS---AFEKSKFWTD 225
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 223461072 705 VRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14047  226 LRNGILPDIFDKRYKIEKTIIKKMLSKKPEDRPNASEI 263
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
479-736 4.34e-16

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: 79.83  E-value: 4.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLylpgmdHAQLVAIKTLkdynnpqqWTefQQEASLMAE--------LHHPNIVCLL-------GAVT 543
Cdd:cd14144    3 VGKGRYGEVWKGKW------RGEKVAVKIF--------FT--TEEASWFREteiyqtvlMRHENILGFIaadikgtGSWT 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 544 QeqpVCMLFEYMNQGDLHEFLIMrsphsdvgcssdedgtvkSSLDHGDFLHIAIQIAAGMEYLSSHFF--------VHKD 615
Cdd:cd14144   67 Q---LYLITDYHENGSLYDFLRG------------------NTLDTQSMLKLAYSAACGLAHLHTEIFgtqgkpaiAHRD 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 616 LAARNILIGEQLHVKISDLGL-------SREIYSADYYRVQSKsslpiRWMPPE----AIMYGKFSS--DSDIWSFGVVL 682
Cdd:cd14144  126 IKSKNILVKKNGTCCIADLGLavkfiseTNEVDLPPNTRVGTK-----RYMAPEvldeSLNRNHFDAykMADMYSFGLVL 200
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223461072 683 WEI----FSFGL-----QPYYGF--------SNQEVIEMVRKRQLLP---CSEDCPPRMYSLMTECWNEIPSRR 736
Cdd:cd14144  201 WEIarrcISGGIveeyqLPYYDAvpsdpsyeDMRRVVCVERRRPSIPnrwSSDEVLRTMSKLMSECWAHNPAAR 274
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
473-742 4.42e-16

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: 79.30  E-value: 4.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 473 VRFMEELGECTFGKIYKGHLYLPgmdhAQLVAIKTLKDYNNPQQWTE-FQQEASLMAELHHPNIVCLLGAVTQEQPVCML 551
Cdd:cd14069    3 WDLVQTLGEGAFGEVFLAVNRNT----EEAVAVKFVDMKRAPGDCPEnIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMNQGDLHEFLimrSPhsDVGCSSDEDgtvkssldHGDFLhiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKI 631
Cdd:cd14069   79 LEYASGGELFDKI---EP--DVGMPEDVA--------QFYFQ----QLMAGLKYLHSCGITHRDIKPENLLLDENDNLKI 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 632 SDLGLsreiysADYYRVQSKS--------SLPirWMPPEAIMYGKFSSD-SDIWSFGVVL---------WEIFSFGLQPY 693
Cdd:cd14069  142 SDFGL------ATVFRYKGKErllnkmcgTLP--YVAPELLAKKKYRAEpVDVWSCGIVLfamlagelpWDQPSDSCQEY 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 223461072 694 YGFSNQeviemvRKRQLLPCSEdCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14069  214 SDWKEN------KKTYLTPWKK-IDTAALSLLRKILTENPNKRITIEDI 255
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
522-717 5.24e-16

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: 78.84  E-value: 5.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 522 QEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSPHSDvgcssdedGTVKssldhgdflHIAIQIAA 601
Cdd:cd05578   49 NELEILQELEHPFLVNLWYSFQDEEDMYMVVDLLLGGDLRYHLQQKVKFSE--------ETVK---------FYICEIVL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 602 GMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSReIYSADYYrVQSKSSLPIrWMPPEAIMYGKFSSDSDIWSFGVV 681
Cdd:cd05578  112 ALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIAT-KLTDGTL-ATSTSGTKP-YMAPEVFMRAGYSFAVDWWSLGVT 188
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 223461072 682 LWEiFSFGLQPYYGFSN---QEVIEM-VRKRQLLPC--SEDC 717
Cdd:cd05578  189 AYE-MLRGKRPYEIHSRtsiEEIRAKfETASVLYPAgwSEEA 229
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
476-718 6.00e-16

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: 79.28  E-value: 6.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYM 555
Cdd:cd07871   10 LDKLGEGTYATVFKGRSKLTE----NLVALKEIRLEHEEGAPCTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVFEYL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQgDLHEFLimrsphsdvgcssDEDGTVKSSLDHGDFLhiaIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLG 635
Cdd:cd07871   86 DS-DLKQYL-------------DNCGNLMSMHNVKIFM---FQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 636 LSR--EIYSADYyrvqSKSSLPIRWMPPEAIM-YGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRKRQLLP 712
Cdd:cd07871  149 LARakSVPTKTY----SNEVVTLWYRPPDVLLgSTEYSTPIDMWGVGCILYEMAT-GRPMFPGSTVKEELHLIFRLLGTP 223

                 ....*.
gi 223461072 713 CSEDCP 718
Cdd:cd07871  224 TEETWP 229
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
477-705 6.51e-16

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: 78.81  E-value: 6.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLYLPGMDHAQLVaIKTlkdyNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMN 556
Cdd:cd14190   10 EVLGGGKFGKVHTCTEKRTGLKLAAKV-INK----QNSKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLImrsphsdvgcssDEDgtvkSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNIL-IGEQLH-VKISDL 634
Cdd:cd14190   85 GGELFERIV------------DED----YHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILcVNRTGHqVKIIDF 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223461072 635 GLSREIYSADYYRVQSKSSlpiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMV 705
Cdd:cd14190  149 GLARRYNPREKLKVNFGTP---EFLSPEVVNYDQVSFPTDMWSMGVITYMLLS-GLSPFLGDDDTETLNNV 215
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
480-692 7.04e-16

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 79.64  E-value: 7.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 480 GECTFGKIYKGHLyLPGMDhAQLVAIKTLKdyNNPQQWTEFQQ----EASLMAELHHPNIVCLLGAV--TQEQPVCMLFE 553
Cdd:cd07842    9 GRGTYGRVYKAKR-KNGKD-GKEYAIKKFK--GDKEQYTGISQsacrEIALLRELKHENVVSLVEVFleHADKSVYLLFD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 554 YMNqgdlHEFLIMRSPHSDVGCSSDEDGTVKSsldhgdflhIAIQIAAGMEYLSSHFFVHKDLAARNILI----GEQLHV 629
Cdd:cd07842   85 YAE----HDLWQIIKFHRQAKRVSIPPSMVKS---------LLWQILNGIHYLHSNWVLHRDLKPANILVmgegPERGVV 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223461072 630 KISDLGLSREIYSAdyyrVQSKSSL-----PIRWMPPEAIMYGK-FSSDSDIWSFGVVLWEIFSfgLQP 692
Cdd:cd07842  152 KIGDLGLARLFNAP----LKPLADLdpvvvTIWYRAPELLLGARhYTKAIDIWAIGCIFAELLT--LEP 214
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
477-716 8.34e-16

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: 78.42  E-value: 8.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLYLPGMdhaqLVAIKTLKdYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMN 556
Cdd:cd14193   10 EILGGGRFGQVHKCEEKSSGL----KLAAKIIK-ARSQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLImrsphsdvgcssDEDGTVkSSLDHGDFLHiaiQIAAGMEYLSSHFFVHKDLAARNILI--GEQLHVKISDL 634
Cdd:cd14193   85 GGELFDRII------------DENYNL-TELDTILFIK---QICEGIQYMHQMYILHLDLKPENILCvsREANQVKIIDF 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 635 GLSREIYSADYYRVQSKSSlpiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEmvrkrQLLPCS 714
Cdd:cd14193  149 GLARRYKPREKLRVNFGTP---EFLAPEVVNYEFVSFPTDMWSLGVIAYMLLS-GLSPFLGEDDNETLN-----NILACQ 219

                 ..
gi 223461072 715 ED 716
Cdd:cd14193  220 WD 221
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
479-742 8.41e-16

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: 78.20  E-value: 8.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKghlyLPGMDHAQLVAIKTLKDYN-NPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQ 557
Cdd:cd08530    8 LGKGSYGSVYK----VKRLSDNQVYALKEVNLGSlSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEYAPF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 558 GDLHEfLIMRSPHSdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLS 637
Cdd:cd08530   84 GDLSK-LISKRKKK------------RRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGIS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 638 ReIYSADYYRVQSKSSLpirWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLqPYYGFSNQEVIEMVRKRQLLPcsedc 717
Cdd:cd08530  151 K-VLKKNLAKTQIGTPL---YAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRP-PFEARTMQELRYKVCRGKFPP----- 220
                        250       260       270
                 ....*....|....*....|....*....|
gi 223461072 718 PPRMYS-----LMTECWNEIPSRRPRFKDI 742
Cdd:cd08530  221 IPPVYSqdlqqIIRSLLQVNPKKRPSCDKL 250
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
471-740 9.20e-16

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: 78.54  E-value: 9.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 471 SAVRFMEELGECTFGKIYKghlylpgMDH---AQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQP 547
Cdd:cd06605    1 DDLEYLGELGEGNGGVVSK-------VRHrpsGQIMAVKVIRLEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 548 VCMLFEYMNQGDLHEFL--IMRSPHSDVGcssdedgtvkssldhgdflHIAIQIAAGMEYL-SSHFFVHKDLAARNILIG 624
Cdd:cd06605   74 ISICMEYMDGGSLDKILkeVGRIPERILG-------------------KIAVAVVKGLIYLhEKHKIIHRDVKPSNILVN 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 625 EQLHVKISDLGLSREIysadyyrVQS--KSSLPIR-WMPPEAIMYGKFSSDSDIWSFGVVLWEIfSFGLQPyYGFSNQEV 701
Cdd:cd06605  135 SRGQVKLCDFGVSGQL-------VDSlaKTFVGTRsYMAPERISGGKYTVKSDIWSLGLSLVEL-ATGRFP-YPPPNAKP 205
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 223461072 702 IEMVrkRQLLPCSEDCPP-----RMYS-----LMTECWNEIPSRRPRFK 740
Cdd:cd06605  206 SMMI--FELLSYIVDEPPpllpsGKFSpdfqdFVSQCLQKDPTERPSYK 252
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
478-718 1.11e-15

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: 78.54  E-value: 1.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 478 ELGECTFGKIYKGHLYLPGmdhAQLVAIKTLKDYNNPQ--QWTEFQQEASL--MAELHHPNIV-----CLLGAVTQEQPV 548
Cdd:cd07862    8 EIGEGAYGKVFKARDLKNG---GRFVALKRVRVQTGEEgmPLSTIREVAVLrhLETFEHPNVVrlfdvCTVSRTDRETKL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 549 CMLFEYMNQgDLHEFLiMRSPHSDVGCSSDEDgtvkssldhgdflhIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLH 628
Cdd:cd07862   85 TLVFEHVDQ-DLTTYL-DKVPEPGVPTETIKD--------------MMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQ 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 629 VKISDLGLSReIYSadyYRVQSKSSLPIRWM-PPEAIMYGKFSSDSDIWSFGVVLWEIFSfgLQPYY-GFSNQEVIEMVR 706
Cdd:cd07862  149 IKLADFGLAR-IYS---FQMALTSVVVTLWYrAPEVLLQSSYATPVDLWSVGCIFAEMFR--RKPLFrGSSDVDQLGKIL 222
                        250
                 ....*....|..
gi 223461072 707 KRQLLPCSEDCP 718
Cdd:cd07862  223 DVIGLPGEEDWP 234
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
513-742 1.38e-15

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: 77.53  E-value: 1.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 513 NPQQWT-----EFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLimrspHSDVGCSsdedgtvkssL 587
Cdd:cd14057   27 KVRDVTtrisrDFNEEYPRLRIFSHPNVLPVLGACNSPPNLVVISQYMPYGSLYNVL-----HEGTGVV----------V 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 588 DHGDFLHIAIQIAAGMEYLSS--HFFVHKDLAARNILIGEQLHVKIS--DLGLSreiysadyYRVQSKSSLPIrWMPPEA 663
Cdd:cd14057   92 DQSQAVKFALDIARGMAFLHTlePLIPRHHLNSKHVMIDEDMTARINmaDVKFS--------FQEPGKMYNPA-WMAPEA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 664 IMygKFSSD-----SDIWSFGVVLWEIFSFGLqPYYGFSNQEVIEMVRKRQLLPcseDCPP----RMYSLMTECWNEIPS 734
Cdd:cd14057  163 LQ--KKPEDinrrsADMWSFAILLWELVTREV-PFADLSNMEIGMKIALEGLRV---TIPPgispHMCKLMKICMNEDPG 236

                 ....*...
gi 223461072 735 RRPRFKDI 742
Cdd:cd14057  237 KRPKFDMI 244
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
470-743 1.56e-15

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: 77.76  E-value: 1.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 470 LSAVRFMEELGECTFGKIYKGHLYLpgmdHAQLVAIKTLKDYN--NPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQP 547
Cdd:cd08228    1 LANFQIEKKIGRGQFSEVYRATCLL----DRKPVALKKVQIFEmmDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 548 VCMLFEYMNQGDLHEFLIMRSPHsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQL 627
Cdd:cd08228   77 LNIVLELADAGDLSQMIKYFKKQ-------------KRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATG 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 628 HVKISDLGLSReIYSADYYRVQSKSSLPIrWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGlQPYYG-----FSNQEVI 702
Cdd:cd08228  144 VVKLGDLGLGR-FFSSKTTAAHSLVGTPY-YMSPERIHENGYNFKSDIWSLGCLLYEMAALQ-SPFYGdkmnlFSLCQKI 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 223461072 703 EMVrKRQLLPcSEDCPPRMYSLMTECWNEIPSRRPRFKDIH 743
Cdd:cd08228  221 EQC-DYPPLP-TEHYSEKLRELVSMCIYPDPDQRPDIGYVH 259
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
479-710 1.64e-15

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: 78.60  E-value: 1.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIY---KghlyLPGMDHAQLVAIKTLKDYN---NPQQWTEFqqEASLMAELHHPNIVCLLGAVTQEQPVCMLF 552
Cdd:cd05582    3 LGQGSFGKVFlvrK----ITGPDAGTLYAMKVLKKATlkvRDRVRTKM--ERDILADVNHPFIVKLHYAFQTEGKLYLIL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 EYMNQGDLHEFLimrsphSDVGCSSDEDgtVKSSLdhgdflhiaIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKIS 632
Cdd:cd05582   77 DFLRGGDLFTRL------SKEVMFTEED--VKFYL---------AELALALDHLHSLGIIYRDLKPENILLDEDGHIKLT 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223461072 633 DLGLSREiySADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRKRQL 710
Cdd:cd05582  140 DFGLSKE--SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GSLPFQGKDRKETMTMILKAKL 214
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
513-742 1.92e-15

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


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 77.46  E-value: 1.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 513 NPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLheflimrsphSDVGCSSDEDGTVkssLDHGDF 592
Cdd:cd08222   42 QPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIVTEYCEGGDL----------DDKISEYKKSGTT---IDENQI 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 593 LHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLhVKISDLGLSREIY-SAD---------YYrvqsksslpirwMPPE 662
Cdd:cd08222  109 LDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNNV-IKVGDFGISRILMgTSDlattftgtpYY------------MSPE 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 663 AIMYGKFSSDSDIWSFGVVLWEIFSFGlqpyYGFSNQEVIEMVRKrqllPCSEDCP--PRMYS-----LMTECWNEIPSR 735
Cdd:cd08222  176 VLKHEGYNSKSDIWSLGCILYEMCCLK----HAFDGQNLLSVMYK----IVEGETPslPDKYSkelnaIYSRMLNKDPAL 247

                 ....*..
gi 223461072 736 RPRFKDI 742
Cdd:cd08222  248 RPSAAEI 254
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
477-742 1.98e-15

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: 77.28  E-value: 1.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLYLPGMDHAQLVA----IKTLKDYNNPQQWT---EFQQEASLMAELHHPNIVCLLGAVTQEQPVC 549
Cdd:cd05077    5 EHLGRGTRTQIYAGILNYKDDDEDEGYSyekeIKVILKVLDPSHRDislAFFETASMMRQVSHKHIVLLYGVCVRDVENI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 550 MLFEYMNQGDLHEFLIMRSphsdvgcssdedgtvkSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQ--- 626
Cdd:cd05077   85 MVEEFVEFGPLDLFMHRKS----------------DVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNILLAREgid 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 627 ----LHVKISDLGLSREIYSadyyRVQSKSSLPirWMPPEAIMYGK-FSSDSDIWSFGVVLWEIFSFGLQPyygFSNQEV 701
Cdd:cd05077  149 gecgPFIKLSDPGIPITVLS----RQECVERIP--WIAPECVEDSKnLSIAADKWSFGTTLWEICYNGEIP---LKDKTL 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 223461072 702 IEMVR--KRQLLPCSEDCpPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05077  220 AEKERfyEGQCMLVTPSC-KELADLMTHCMNYDPNQRPFFRAI 261
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
478-686 2.26e-15

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: 77.70  E-value: 2.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 478 ELGECTFGKIYKGHlylpGMDHAQLVAIKTLKDYNNPQQW-TEFQQEASLMAELH---HPNIV-----CLLGAVTQEQPV 548
Cdd:cd07863    7 EIGVGAYGTVYKAR----DPHSGHFVALKSVRVQTNEDGLpLSTVREVALLKRLEafdHPNIVrlmdvCATSRTDRETKV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 549 CMLFEYMNQgDLHEFLIMRSPHsdvGCSSDedgTVKssldhgDFLHiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLH 628
Cdd:cd07863   83 TLVFEHVDQ-DLRTYLDKVPPP---GLPAE---TIK------DLMR---QFLRGLDFLHANCIVHRDLKPENILVTSGGQ 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 223461072 629 VKISDLGLSReIYSadYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIF 686
Cdd:cd07863  147 VKLADFGLAR-IYS--CQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMF 201
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
520-742 2.59e-15

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: 77.26  E-value: 2.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 520 FQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLimrsphsdvgcsSDEDGTVKSSLDhgdfLHIAIQI 599
Cdd:cd05076   62 FFETASLMSQVSHTHLVFVHGVCVRGSENIMVEEFVEHGPLDVWL------------RKEKGHVPMAWK----FVVARQL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 600 AAGMEYLSSHFFVHKDLAARNILI-------GEQLHVKISDLG-----LSREiysadyYRVQSksslpIRWMPPEAIMYG 667
Cdd:cd05076  126 ASALSYLENKNLVHGNVCAKNILLarlgleeGTSPFIKLSDPGvglgvLSRE------ERVER-----IPWIAPECVPGG 194
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223461072 668 -KFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPcsEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd05076  195 nSLSTAADKWGFGATLLEICFNGEAPLQSRTPSEKERFYQRQHRLP--EPSCPELATLISQCLTYEPTQRPSFRTI 268
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
478-737 2.65e-15

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: 77.38  E-value: 2.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 478 ELGECTFGKIYKGHLYLPGMdhaqLVAIKTLkDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQ 557
Cdd:cd06644   19 ELGDGAFGKVYKAKNKETGA----LAAAKVI-ETKSEEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCPG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 558 GDLHEFLI-----MRSPHSDVGCSsdedgtvkssldhgdflhiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKIS 632
Cdd:cd06644   94 GAVDAIMLeldrgLTEPQIQVICR---------------------QMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 633 DLGLSreiySADYYRVQSKSSL---PIrWMPPEAIMY-----GKFSSDSDIWSFGVVLWEIFSFGlQPYYGFSNQEVIEM 704
Cdd:cd06644  153 DFGVS----AKNVKTLQRRDSFigtPY-WMAPEVVMCetmkdTPYDYKADIWSLGITLIEMAQIE-PPHHELNPMRVLLK 226
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 223461072 705 VRKRQllPCSEDCP----PRMYSLMTECWNEIPSRRP 737
Cdd:cd06644  227 IAKSE--PPTLSQPskwsMEFRDFLKTALDKHPETRP 261
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
523-741 2.98e-15

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: 77.18  E-value: 2.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 523 EASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLimrsphSDVGcssdedgtvKSSLDHGDFLHIAIQIAAG 602
Cdd:cd05577   43 EKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDLKYHI------YNVG---------TRGFSEARAIFYAAEIICG 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 603 MEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSreiysadyyrVQSKSSLPIR-------WMPPEAIMYG-KFSSDSD 674
Cdd:cd05577  108 LEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLA----------VEFKGGKKIKgrvgthgYMAPEVLQKEvAYDFSVD 177
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223461072 675 IWSFGVVLWEIFSfGLQPYYGF----SNQEVIEMVrKRQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKD 741
Cdd:cd05577  178 WFALGCMLYEMIA-GRSPFRQRkekvDKEELKRRT-LEMAVEYPDSFSPEARSLCEGLLQKDPERRLGCRG 246
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
475-706 3.10e-15

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: 77.21  E-value: 3.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYK------GHLYLpgmdhAQLVAIKTLKdynnpQQWTefQQEASLMAELHHPNIVCLLGAVTQEQPV 548
Cdd:cd14104    4 IAEELGRGQFGIVHRcvetssKKTYM-----AKFVKVKGAD-----QVLV--KKEISILNIARHRNILRLHESFESHEEL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 549 CMLFEYMNQGDLHEFLimrsphsdvgcssdedGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQL- 627
Cdd:cd14104   72 VMIFEFISGVDIFERI----------------TTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRg 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 628 -HVKISDLGLSREIYSADYYRVQSKSSlpiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVR 706
Cdd:cd14104  136 sYIKIIEFGQSRQLKPGDKFRLQYTSA---EFYAPEVHQHESVSTATDMWSLGCLVYVLLS-GINPFEAETNQQTIENIR 211
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
477-705 3.56e-15

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: 76.76  E-value: 3.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLYLPGMDHA-QLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYM 555
Cdd:cd14105   11 EELGSGQFAVVKKCREKSTGLEYAaKFIKKRRSKASRRGVSREDIEREVSILRQVLHPNIITLHDVFENKTDVVLILELV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQGDLHEFLIMRSphsdvgCSSDEDGTVkssldhgdFLHiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQL----HVKI 631
Cdd:cd14105   91 AGGELFDFLAEKE------SLSEEEATE--------FLK---QILDGVNYLHTKNIAHFDLKPENIMLLDKNvpipRIKL 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223461072 632 SDLGLSREIYSADYYRvqSKSSLPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMV 705
Cdd:cd14105  154 IDFGLAHKIEDGNEFK--NIFGTP-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLANI 223
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
475-742 4.08e-15

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: 76.43  E-value: 4.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYK------GhlylpgmdhaQLVAIKTLkDYNNPQQwTEFQQ---EASLMAELHHPNIVCLLGAV--T 543
Cdd:cd08217    4 VLETIGKGSFGTVRKvrrksdG----------KILVWKEI-DYGKMSE-KEKQQlvsEVNILRELKHPNIVRYYDRIvdR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 544 QEQPVCMLFEYMNQGDLHEfLIMRsphsdvgCSSDedgtvKSSLDHGDFLHIAIQIAAGMEY-----LSSHFFVHKDLAA 618
Cdd:cd08217   72 ANTTLYIVMEYCEGGDLAQ-LIKK-------CKKE-----NQYIPEEFIWKIFTQLLLALYEchnrsVGGGKILHRDLKP 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 619 RNILIGEQLHVKISDLGLSREIYSAD----------YYrvqsksslpirwMPPEAIMYGKFSSDSDIWSFGVVLWEIFSf 688
Cdd:cd08217  139 ANIFLDSDNNVKLGDFGLARVLSHDSsfaktyvgtpYY------------MSPELLNEQSYDEKSDIWSLGCLIYELCA- 205
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 689 gLQ-PYYGFSNQEVIEMVRKRQLLPCsedcpPRMYS-----LMTECWNEIPSRRPRFKDI 742
Cdd:cd08217  206 -LHpPFQAANQLELAKKIKEGKFPRI-----PSRYSselneVIKSMLNVDPDKRPSVEEL 259
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
476-687 4.47e-15

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: 76.65  E-value: 4.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKdyNNPQQWTEFQ--QEASLMAELHHPNIVCLLGAVTQEQPVCMLFE 553
Cdd:cd07844    5 LDKLGEGSYATVYKGRSKLTG----QLVALKEIR--LEHEEGAPFTaiREASLLKDLKHANIVTLHDIIHTKKTLTLVFE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 554 YMnQGDLHEFLImrsphsdvgcssdedgtvksslDHGDFLHIA------IQIAAGMEYLSSHFFVHKDLAARNILIGEQL 627
Cdd:cd07844   79 YL-DTDLKQYMD----------------------DCGGGLSMHnvrlflFQLLRGLAYCHQRRVLHRDLKPQNLLISERG 135
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223461072 628 HVKISDLGLSR------EIYSAD----YYRvqsksslpirwmPPEAIM-YGKFSSDSDIWSFGVVLWEIFS 687
Cdd:cd07844  136 ELKLADFGLARaksvpsKTYSNEvvtlWYR------------PPDVLLgSTEYSTSLDMWGVGCIFYEMAT 194
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
470-686 4.66e-15

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: 76.97  E-value: 4.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 470 LSAVRFMEELGECTFGKIYKGHLYLPGmdhaQLVAIK--TLKDYNNPQQWTEfQQEASLMAELHHPNIVCLLGAVTQEQP 547
Cdd:cd07866    7 LRDYEILGKLGEGTFGEVYKARQIKTG----RVVALKkiLMHNEKDGFPITA-LREIKILKKLKHPNVVPLIDMAVERPD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 548 --------VCMLFEYMNQgDLHEFLimrsphsdvgcssdEDGTVKssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAAR 619
Cdd:cd07866   82 kskrkrgsVYMVTPYMDH-DLSGLL--------------ENPSVK--LTESQIKCYMLQLLEGINYLHENHILHRDIKAA 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 620 NILIGEQLHVKISDLGLSREIYSADYyrvQSKSSLPI-----------RWM-PPEAIMYGK-FSSDSDIWSFGVVLWEIF 686
Cdd:cd07866  145 NILIDNQGILKIADFGLARPYDGPPP---NPKGGGGGgtrkytnlvvtRWYrPPELLLGERrYTTAVDIWGIGCVFAEMF 221
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
471-739 5.38e-15

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: 76.43  E-value: 5.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 471 SAVRFMEELGECTFGKIYKghlylpgMDHAQLVAIKTLKDYNNPQQWTEFQQ---EASLMAELHHPNIVCLLGAVTQEQP 547
Cdd:cd06622    1 DEIEVLDELGKGNYGSVYK-------VLHRPTGVTMAMKEIRLELDESKFNQiimELDILHKAVSPYIVDFYGAFFIEGA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 548 VCMLFEYMNQGDLHEFLimrsphsdvgcssdEDGTVKSSLDHGDFLHIAIQIAAGMEYL-SSHFFVHKDLAARNILIGEQ 626
Cdd:cd06622   74 VYMCMEYMDAGSLDKLY--------------AGGVATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGN 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 627 LHVKISDLGLSREIysadyyrVQSKSSLPI---RWMPPEAIMYG------KFSSDSDIWSFGVVLWEIfSFGLQPYYGFS 697
Cdd:cd06622  140 GQVKLCDFGVSGNL-------VASLAKTNIgcqSYMAPERIKSGgpnqnpTYTVQSDVWSLGLSILEM-ALGRYPYPPET 211
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 223461072 698 NQEVIEmvrkrQLLPCSEDCPPRM---YS-----LMTECWNEIPSRRPRF 739
Cdd:cd06622  212 YANIFA-----QLSAIVDGDPPTLpsgYSddaqdFVAKCLNKIPNRRPTY 256
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
479-683 5.56e-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: 75.77  E-value: 5.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGmdhaQLVAIKTL--KDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMN 556
Cdd:cd14079   10 LGVGSFGKVKLAEHELTG----HKVAVKILnrQKIKSLDMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVMEYVS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLIMrsphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGL 636
Cdd:cd14079   86 GGELFDYIVQ-----------------KGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGL 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 223461072 637 SREIYSADYYRVQSKSslPiRWMPPEAIMyGKF--SSDSDIWSFGVVLW 683
Cdd:cd14079  149 SNIMRDGEFLKTSCGS--P-NYAAPEVIS-GKLyaGPEVDVWSCGVILY 193
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
468-680 7.21e-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: 75.80  E-value: 7.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 468 LPLSAVRF--MEELGECTFGKIYKGHLylpgMDHAQLVAIKTLKdyNNPQQWTEFQQEASLMAEL-HHPNIVCLLGAVTQ 544
Cdd:cd06608    1 LPDPAGIFelVEVIGEGTYGKVYKARH----KKTGQLAAIKIMD--IIEDEEEEIKLEINILRKFsNHPNIATFYGAFIK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 545 EQPVCMlfeymnQGDLheFLIMRspHSDVGCSSDedgTVKSSLDHGDFL---HIAI---QIAAGMEYLSSHFFVHKDLAA 618
Cdd:cd06608   75 KDPPGG------DDQL--WLVME--YCGGGSVTD---LVKGLRKKGKRLkeeWIAYilrETLRGLAYLHENKVIHRDIKG 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223461072 619 RNILIGEQLHVKISDLGLSReiysadyyrvQSKSSLPIR--------WMPPEAIMYGK-----FSSDSDIWSFGV 680
Cdd:cd06608  142 QNILLTEEAEVKLVDFGVSA----------QLDSTLGRRntfigtpyWMAPEVIACDQqpdasYDARCDVWSLGI 206
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
477-702 7.38e-15

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: 75.76  E-value: 7.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLYLPGMDHAQlvaiKTLKDYNNPQQW-----TEFQQEASLMAELHHPNIVCLLGAVTQEQPVCML 551
Cdd:cd14196   11 EELGSGQFAIVKKCREKSTGLEYAA----KFIKKRQSRASRrgvsrEEIEREVSILRQVLHPNIITLHDVYENRTDVVLI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMNQGDLHEFLIMrsphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQL---- 627
Cdd:cd14196   87 LELVSGGELFDFLAQ-----------------KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipip 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223461072 628 HVKISDLGLSREIysADYYRVQSKSSLPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVI 702
Cdd:cd14196  150 HIKLIDFGLAHEI--EDGVEFKNIFGTP-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETL 220
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
479-706 8.24e-15

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: 76.89  E-value: 8.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGmdhaQLVAIKTLKD----YNNPQQWTEFQQEASLMAeLHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd05619   13 LGKGSFGKVFLAELKGTN----QFFAIKALKKdvvlMDDDVECTMVEKRVLSLA-WEHPFLTHLFCTFQTKENLFFVMEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQGDLheFLIMRSPHsdvgcssdedgtvKSSLDHGDFLhiAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd05619   88 LNGGDL--MFHIQSCH-------------KFDLPRATFY--AAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADF 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223461072 635 GLSREIYSADyYRVQSKSSLPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVIEMVR 706
Cdd:cd05619  151 GMCKENMLGD-AKTSTFCGTP-DYIAPEILLGQKYNTSVDWWSFGVLLYEML-IGQSPFHGQDEEELFQSIR 219
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
474-742 9.29e-15

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: 75.34  E-value: 9.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 474 RFMEELGECTFGKIYKGHLYLPGMDhaqlVAIKTLKDYN-NPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLF 552
Cdd:cd13983    4 KFNEVLGRGSFKTVYRAFDTEEGIE----VAWNEIKLRKlPKAERQRFKQEIEILKSLKHPNIIKFYDSWESKSKKEVIF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 --EYMNQGDLHEFlIMRSPHSDVGcssdedgTVKSsldhgdflhIAIQIAAGMEYLSSHF--FVHKDLAARNILI-GEQL 627
Cdd:cd13983   80 itELMTSGTLKQY-LKRFKRLKLK-------VIKS---------WCRQILEGLNYLHTRDppIIHRDLKCDNIFInGNTG 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 628 HVKISDLGLSREIysaDYYRVQSKSSLPiRWMPPEaiMY-GKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSN-QEVIEMV 705
Cdd:cd13983  143 EVKIGDLGLATLL---RQSFAKSVIGTP-EFMAPE--MYeEHYDEKVDIYAFGMCLLEMAT-GEYPYSECTNaAQIYKKV 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 223461072 706 RKrQLLPCS----EDcpPRMYSLMTECWnEIPSRRPRFKDI 742
Cdd:cd13983  216 TS-GIKPESlskvKD--PELKDFIEKCL-KPPDERPSAREL 252
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
477-705 1.35e-14

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: 75.06  E-value: 1.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLYLPGMDHA-QLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYM 555
Cdd:cd14194   11 EELGSGQFAVVKKCREKSTGLQYAaKFIKKRRTKSSRRGVSREDIEREVSILKEIQHPNVITLHEVYENKTDVILILELV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQGDLHEFLIMRSPhsdvgcSSDEDGTvkssldhgDFLHiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQ----LHVKI 631
Cdd:cd14194   91 AGGELFDFLAEKES------LTEEEAT--------EFLK---QILNGVYYLHSLQIAHFDLKPENIMLLDRnvpkPRIKI 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223461072 632 SDLGLSREIYSADYYRvqSKSSLPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMV 705
Cdd:cd14194  154 IDFGLAHKIDFGNEFK--NIFGTP-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLANV 223
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
466-685 1.83e-14

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: 75.47  E-value: 1.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 466 KELPLSAVRFMEELGECTFGKIYKGHlylpGMDHAQLVAIKTLKdYNNPQ---QWTEFQQEASLMAELHHPNIVCLLGAV 542
Cdd:cd06635   20 KEDPEKLFSDLREIGHGSFGAVYFAR----DVRTSEVVAIKKMS-YSGKQsneKWQDIIKEVKFLQRIKHPNSIEYKGCY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 543 TQEQPVCMLFEYM--NQGDLHEflIMRSPHSDVGCSSdedgtvkssLDHGdflhiAIQiaaGMEYLSSHFFVHKDLAARN 620
Cdd:cd06635   95 LREHTAWLVMEYClgSASDLLE--VHKKPLQEIEIAA---------ITHG-----ALQ---GLAYLHSHNMIHRDIKAGN 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223461072 621 ILIGEQLHVKISDLGLSREIYSADYYrvqskSSLPIrWMPPEAIMY---GKFSSDSDIWSFGVVLWEI 685
Cdd:cd06635  156 ILLTEPGQVKLADFGSASIASPANSF-----VGTPY-WMAPEVILAmdeGQYDGKVDVWSLGITCIEL 217
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
479-711 1.87e-14

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: 74.57  E-value: 1.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGMDHAqLVAIKtlKDY-NNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQ 557
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFA-LKCVK--KRHiVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 558 GDLheFLIMRsphsDVGCSSDedgtvksslDHGDFLhIAiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLS 637
Cdd:cd05572   78 GEL--WTILR----DRGLFDE---------YTARFY-TA-CVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFA 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223461072 638 REIYSadYYRVQSKSSLPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPyygFSNQEVIEMVRKRQLL 711
Cdd:cd05572  141 KKLGS--GRKTWTFCGTP-EYVAPEIILNKGYDFSVDYWSLGILLYELLT-GRPP---FGGDDEDPMKIYNIIL 207
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
474-683 2.09e-14

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: 74.41  E-value: 2.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 474 RFMEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQWTEFQQ--------------EASLMAELHHPNIVCLL 539
Cdd:cd14077    4 EFVKTIGAGSMGKVKLAKHIRTG----EKCAIKIIPRASNAGLKKEREKrlekeisrdirtirEAALSSLLNHPHICRLR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 540 GAVTQEQPVCMLFEYMNQGDLHEFLIMRSPhsdvgcsSDEDGTVKssldhgdflhIAIQIAAGMEYLSSHFFVHKDLAAR 619
Cdd:cd14077   80 DFLRTPNHYYMLFEYVDGGQLLDYIISHGK-------LKEKQARK----------FARQIASALDYLHRNSIVHRDLKIE 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223461072 620 NILIGEQLHVKISDLGLSrEIYSADYYRVQSKSSLpiRWMPPEAIMYGKFSS-DSDIWSFGVVLW 683
Cdd:cd14077  143 NILISKSGNIKIIDFGLS-NLYDPRRLLRTFCGSL--YFAAPELLQAQPYTGpEVDVWSFGVVLY 204
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
469-723 2.69e-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: 2.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 469 PLSAVRFMEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQwtEFQQEASLMAEL-HHPNIVCLLGAVTQEQP 547
Cdd:cd06636   14 PAGIFELVEVVGNGTYGQVYKGRHVKTG----QLAAIKVMDVTEDEEE--EIKLEINMLKKYsHHRNIATYYGAFIKKSP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 548 ------VCMLFEYMNQGDLHEFLimrsphsdvgcssdeDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNI 621
Cdd:cd06636   88 pghddqLWLVMEFCGAGSVTDLV---------------KNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 622 LIGEQLHVKISDLGLSREIySADYYRVQSKSSLPIrWMPPEAIMY-----GKFSSDSDIWSFGVVLWEIfSFGLQPyygf 696
Cdd:cd06636  153 LLTENAEVKLVDFGVSAQL-DRTVGRRNTFIGTPY-WMAPEVIACdenpdATYDYRSDIWSLGITAIEM-AEGAPP---- 225
                        250       260
                 ....*....|....*....|....*..
gi 223461072 697 snqeVIEMVRKRQLLPCSEDCPPRMYS 723
Cdd:cd06636  226 ----LCDMHPMRALFLIPRNPPPKLKS 248
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
521-693 2.89e-14

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: 73.93  E-value: 2.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 521 QQEASLMAELHHPNIVCLLGAV--TQEQPVCMLFEYMNQGDlheflIMRSPhsdvgcsSDEdgtvksSLDHGDFLHIAIQ 598
Cdd:cd14118   62 YREIAILKKLDHPNVVKLVEVLddPNEDNLYMVFELVDKGA-----VMEVP-------TDN------PLSEETARSYFRD 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 599 IAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSADyyRVQSKSSLPIRWMPPEAIMYG--KFSSDS-DI 675
Cdd:cd14118  124 IVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFGVSNEFEGDD--ALLSSTAGTPAFMAPEALSESrkKFSGKAlDI 201
                        170
                 ....*....|....*...
gi 223461072 676 WSFGVVLWeIFSFGLQPY 693
Cdd:cd14118  202 WAMGVTLY-CFVFGRCPF 218
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
473-737 3.06e-14

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: 74.14  E-value: 3.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 473 VRFMEELGECTFGKIYKGhLYLPGmdhAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLF 552
Cdd:cd06619    3 IQYQEILGHGNGGTVYKA-YHLLT---RRILAVKVIPLDITVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 EYMNQGDLHEFliMRSPHSDVGcssdedgtvkssldhgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKIS 632
Cdd:cd06619   79 EFMDGGSLDVY--RKIPEHVLG-------------------RIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLC 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 633 DLGLSREIYS--ADYYrVQSKSslpirWMPPEAIMYGKFSSDSDIWSFGVVLWEIfSFGLQPYYGFSNQEVIEMvrKRQL 710
Cdd:cd06619  138 DFGVSTQLVNsiAKTY-VGTNA-----YMAPERISGEQYGIHSDVWSLGISFMEL-ALGRFPYPQIQKNQGSLM--PLQL 208
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 223461072 711 LPC--SEDCP--------PRMYSLMTECWNEIPSRRP 737
Cdd:cd06619  209 LQCivDEDPPvlpvgqfsEKFVHFITQCMRKQPKERP 245
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
477-702 3.34e-14

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: 73.88  E-value: 3.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLYLPGMDHA-QLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYM 555
Cdd:cd14195   11 EELGSGQFAIVRKCREKGTGKEYAaKFIKKRRLSSSRRGVSREEIEREVNILREIQHPNIITLHDIFENKTDVVLILELV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQGDLHEFLimrsphsdvgcssdedgTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQ----LHVKI 631
Cdd:cd14195   91 SGGELFDFL-----------------AEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKnvpnPRIKL 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223461072 632 SDLGLSREIYSADYYRvqSKSSLPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVI 702
Cdd:cd14195  154 IDFGIAHKIEAGNEFK--NIFGTP-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGETKQETL 220
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
469-692 3.58e-14

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: 73.93  E-value: 3.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 469 PLSAVRFMEELGECTFGKIYKGHlylpGMDHAQLVAIKTLKdYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPV 548
Cdd:cd06645    9 PQEDFELIQRIGSGTYGDVYKAR----NVNTGELAAIKVIK-LEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 549 CMLFEYMNQGDLHEFLIMRSPHSDVGCSsdedgtvkssldhgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLH 628
Cdd:cd06645   84 WICMEFCGGGSLQDIYHVTGPLSESQIA-----------------YVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGH 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223461072 629 VKISDLGLSREIySADYYRVQSKSSLPIrWMPPEAIMY---GKFSSDSDIWSFGVVLWEIFSfgLQP 692
Cdd:cd06645  147 VKLADFGVSAQI-TATIAKRKSFIGTPY-WMAPEVAAVerkGGYNQLCDIWAVGITAIELAE--LQP 209
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
484-687 3.61e-14

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: 74.29  E-value: 3.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 484 FGKIYKGHLylpgmdHAQLVAIKTLkdynNPQQWTEFQQEASLMAE--LHHPNIVCLLGAVTQEQPVCMLF----EYMNQ 557
Cdd:cd14053    8 FGAVWKAQY------LNRLVAVKIF----PLQEKQSWLTEREIYSLpgMKHENILQFIGAEKHGESLEAEYwlitEFHER 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 558 GDLHEFLimrspHSDVgcssdedgtvkssLDHGDFLHIAIQIAAGMEYLSS---HFF-------VHKDLAARNILIGEQL 627
Cdd:cd14053   78 GSLCDYL-----KGNV-------------ISWNELCKIAESMARGLAYLHEdipATNgghkpsiAHRDFKSKNVLLKSDL 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223461072 628 HVKISDLGLSReIYSADyyRVQSKSSLPI---RWMPPE----AImygKFSSDS----DIWSFGVVLWEIFS 687
Cdd:cd14053  140 TACIADFGLAL-KFEPG--KSCGDTHGQVgtrRYMAPEvlegAI---NFTRDAflriDMYAMGLVLWELLS 204
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
479-686 4.43e-14

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


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 74.33  E-value: 4.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHlylpGMDHAQLVAIKTLKdYNNPQQWTEFQ--QEASLMAELHHPNIVCLLGAVTQEQ--PVCMLFEY 554
Cdd:cd07845   15 IGEGTYGIVYRAR----DTTSGEIVALKKVR-MDNERDGIPISslREITLLLNLRHPNIVELKEVVVGKHldSIFLVMEY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQgDLHEFLI-MRSPHSDvgcssdedGTVKSsldhgdflhIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISD 633
Cdd:cd07845   90 CEQ-DLASLLDnMPTPFSE--------SQVKC---------LMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIAD 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 223461072 634 LGLSREIYSADYYRVQSKSSLPIRwmPPEaIMYG--KFSSDSDIWSFGVVLWEIF 686
Cdd:cd07845  152 FGLARTYGLPAKPMTPKVVTLWYR--APE-LLLGctTYTTAIDMWAVGCILAELL 203
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
476-737 4.79e-14

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: 73.61  E-value: 4.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKghLYLPGmdHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQP--VCMLFE 553
Cdd:cd06621    6 LSSLGEGAGGSVTK--CRLRN--TKTIFALKTITTDPNPDVQKQILRELEINKSCASPYIVKYYGAFLDEQDssIGIAME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 554 YMNQGDLheflimrsphsdvgcssdeDGTVKSSLDHGD------FLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQL 627
Cdd:cd06621   82 YCEGGSL-------------------DSIYKKVKKKGGrigekvLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKG 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 628 HVKISDLGLSREIYSA--------DYYrvqsksslpirwMPPEAIMYGKFSSDSDIWSFGVVLWEI----FSFglqPYYG 695
Cdd:cd06621  143 QVKLCDFGVSGELVNSlagtftgtSYY------------MAPERIQGGPYSITSDVWSLGLTLLEVaqnrFPF---PPEG 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 223461072 696 FSNQEVIEMVRK--RQLLPCSEDCP--PRMYS-----LMTECWNEIPSRRP 737
Cdd:cd06621  208 EPPLGPIELLSYivNMPNPELKDEPenGIKWSesfkdFIEKCLEKDGTRRP 258
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
479-742 4.86e-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: 73.06  E-value: 4.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGhlylpgMDHAQL--VAIKTLKDY---NNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQE--QPVCML 551
Cdd:cd14119    1 LGEGSYGKVKEV------LDTETLcrRAVKILKKRklrRIPNGEANVKREIQILRRLNHRNVIKLVDVLYNEekQKLYMV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMNqGDLHEfLIMRSPhsdvgcssdeDGTVKSSLDHGDFLhiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKI 631
Cdd:cd14119   75 MEYCV-GGLQE-MLDSAP----------DKRLPIWQAHGYFV----QLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKI 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 632 SDLGLSREI--YSADyYRVQSKSSLPiRWMPPEaIMYGKFSSDS---DIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVR 706
Cdd:cd14119  139 SDFGVAEALdlFAED-DTCTTSQGSP-AFQPPE-IANGQDSFSGfkvDIWSAGVTLYNMTT-GKYPFEGDNIYKLFENIG 214
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 223461072 707 KRQL-LPcsEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14119  215 KGEYtIP--DDVDPDLQDLLRGMLEKDPEKRFTIEQI 249
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
479-687 5.60e-14

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: 73.55  E-value: 5.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLylpgmdHAQLVAIKTLkdynnPQQWTE-FQQEASLMA--ELHHPNIVCLLGA---VTQEQPV--CM 550
Cdd:cd14054    3 IGQGRYGTVWKGSL------DERPVAVKVF-----PARHRQnFQNEKDIYElpLMEHSNILRFIGAderPTADGRMeyLL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 551 LFEYMNQGDLHEFLIMrsphsdvgcssdedgtvkSSLDHGDFLHIAIQIAAGMEYLSSHF---------FVHKDLAARNI 621
Cdd:cd14054   72 VLEYAPKGSLCSYLRE------------------NTLDWMSSCRMALSLTRGLAYLHTDLrrgdqykpaIAHRDLNSRNV 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 622 LIGEQLHVKISDLGLSREIYSADYYRVQSKSSLP--------IRWMPPEaIMYG--------KFSSDSDIWSFGVVLWEI 685
Cdd:cd14054  134 LVKADGSCVICDFGLAMVLRGSSLVRGRPGAAENasisevgtLRYMAPE-VLEGavnlrdceSALKQVDVYALGLVLWEI 212

                 ..
gi 223461072 686 FS 687
Cdd:cd14054  213 AM 214
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
476-685 5.81e-14

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: 73.90  E-value: 5.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYkghlYLPGMDHAQLVAIKTLKdYNNPQ---QWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLF 552
Cdd:cd06634   20 LREIGHGSFGAVY----FARDVRNNEVVAIKKMS-YSGKQsneKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVM 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 EYM--NQGDLHEflIMRSPHSDVGCSSdedgtvkssLDHGdflhiAIQiaaGMEYLSSHFFVHKDLAARNILIGEQLHVK 630
Cdd:cd06634   95 EYClgSASDLLE--VHKKPLQEVEIAA---------ITHG-----ALQ---GLAYLHSHNMIHRDVKAGNILLTEPGLVK 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 223461072 631 ISDLGLSREIYSADYYrvqskSSLPIrWMPPEAIMY---GKFSSDSDIWSFGVVLWEI 685
Cdd:cd06634  156 LGDFGSASIMAPANSF-----VGTPY-WMAPEVILAmdeGQYDGKVDVWSLGITCIEL 207
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
477-685 6.61e-14

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: 72.85  E-value: 6.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGhLYLPGmdhaQLVAIKTLK-DYNNP----QQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCML 551
Cdd:cd06631    7 NVLGKGAYGTVYCG-LTSTG----QLIAVKQVElDTSDKekaeKEYEKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMNQGDLHEFLIMRSPhsdvgcssdedgtvkssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKI 631
Cdd:cd06631   82 MEFVPGGSIASILARFGA-----------------LEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKL 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 223461072 632 SDLGLSREIYSADYYRVQSKSSLPIR----WMPPEAIMYGKFSSDSDIWSFGVVLWEI 685
Cdd:cd06631  145 IDFGCAKRLCINLSSGSQSQLLKSMRgtpyWMAPEVINETGHGRKSDIWSIGCTVFEM 202
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
75-145 7.56e-14

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 67.35  E-value: 7.56e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223461072  75 AELHCKVSGNPPPSIRWFKNDAPVVQEPRRISFRATNyGSRLRIRNLDTTDTGYFQCVATNGKKVVSTTGV 145
Cdd:cd00096    1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELG-NGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
477-736 9.92e-14

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: 72.86  E-value: 9.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLylpgMDHAqlVAIKTLkDYNNPQQWtefQQEASLMAE--LHHPNIVCLLGA----VTQEQPVCM 550
Cdd:cd13998    1 EVIGKGRFGEVWKASL----KNEP--VAVKIF-SSRDKQSW---FREKEIYRTpmLKHENILQFIAAderdTALRTELWL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 551 LFEYMNQGDLHEFLimrSPHSdvgcssdedgtvkssLDHGDFLHIAIQIAAGMEYLSSHFF---------VHKDLAARNI 621
Cdd:cd13998   71 VTAFHPNGSL*DYL---SLHT---------------IDWVSLCRLALSVARGLAHLHSEIPgctqgkpaiAHRDLKSKNI 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 622 LIGEQLHVKISDLGLS-------REIYSADYYRVQSKsslpiRWMPPE----AIMYGKFSS--DSDIWSFGVVLWEIFS- 687
Cdd:cd13998  133 LVKNDGTCCIADFGLAvrlspstGEEDNANNGQVGTK-----RYMAPEvlegAINLRDFESfkRVDIYAMGLVLWEMASr 207
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223461072 688 ----FGLQPYYGFSNQEVI----------EMVRKRQLLPcseDCPPR---------MYSLMTECWNEIPSRR 736
Cdd:cd13998  208 ctdlFGIVEEYKPPFYSEVpnhpsfedmqEVVVRDKQRP---NIPNRwlshpglqsLAETIEECWDHDAEAR 276
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
522-693 1.00e-13

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: 72.69  E-value: 1.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 522 QEASLMAELHHPNIVCLLGAVT--QEQPVCMLFEYMNQGDlheflIMRSPhsdvgcssdedgTVKS-SLDHGDFLHIaiQ 598
Cdd:cd14199   74 QEIAILKKLDHPNVVKLVEVLDdpSEDHLYMVFELVKQGP-----VMEVP------------TLKPlSEDQARFYFQ--D 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 599 IAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSADYYrVQSKSSLPIrWMPPEAIMYGK--FSSDS-DI 675
Cdd:cd14199  135 LIKGIEYLHYQKIIHRDVKPSNLLVGEDGHIKIADFGVSNEFEGSDAL-LTNTVGTPA-FMAPETLSETRkiFSGKAlDV 212
                        170
                 ....*....|....*...
gi 223461072 676 WSFGVVLWeIFSFGLQPY 693
Cdd:cd14199  213 WAMGVTLY-CFVFGQCPF 229
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
473-736 1.00e-13

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: 72.86  E-value: 1.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 473 VRFMEELGECTFGKIYKGHLylpgmdHAQLVAIKTLKDYNNPQQWTEFQQEASLMaeLHHPNIVCLLGA-VTQEQPVCML 551
Cdd:cd14142    7 ITLVECIGKGRYGEVWRGQW------QGESVAVKIFSSRDEKSWFRETEIYNTVL--LRHENILGFIASdMTSRNSCTQL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 F---EYMNQGDLHEFLimrsphsdvgcssdedgtVKSSLDHGDFLHIAIQIAAGMEYLSSHFF--------VHKDLAARN 620
Cdd:cd14142   79 WlitHYHENGSLYDYL------------------QRTTLDHQEMLRLALSAASGLVHLHTEIFgtqgkpaiAHRDLKSKN 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 621 ILIGEQLHVKISDLGL-------SREIYSADYYRVQSKsslpiRWMPPE----AIMYGKFSS--DSDIWSFGVVLWEI-- 685
Cdd:cd14142  141 ILVKSNGQCCIADLGLavthsqeTNQLDVGNNPRVGTK-----RYMAPEvldeTINTDCFESykRVDIYAFGLVLWEVar 215
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223461072 686 --FSFGL-----QPYYGF-SNQEVIEMVRK-------RQLLP---CSEDCPPRMYSLMTECWNEIPSRR 736
Cdd:cd14142  216 rcVSGGIveeykPPFYDVvPSDPSFEDMRKvvcvdqqRPNIPnrwSSDPTLTAMAKLMKECWYQNPSAR 284
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
462-694 1.10e-13

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 73.31  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 462 KSKAKELPLSAVRFMEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYN--NPQQWTEFQQEASLMAELHHPNIVCLL 539
Cdd:PTZ00263   9 KPDTSSWKLSDFEMGETLGTGSFGRVRIAKHKGTG----EYYAIKCLKKREilKMKQVQHVAQEKSILMELSHPFIVNMM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 540 GAVTQEQPVCMLFEYMNQGDLheFLIMRSPHsdvgcssdedgtvKSSLDHGDFLHIAIQIAagMEYLSSHFFVHKDLAAR 619
Cdd:PTZ00263  85 CSFQDENRVYFLLEFVVGGEL--FTHLRKAG-------------RFPNDVAKFYHAELVLA--FEYLHSKDIIYRDLKPE 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223461072 620 NILIGEQLHVKISDLGLSREIYSadyyRVQSKSSLPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEiFSFGLQPYY 694
Cdd:PTZ00263 148 NLLLDNKGHVKVTDFGFAKKVPD----RTFTLCGTP-EYLAPEVIQSKGHGKAVDWWTMGVLLYE-FIAGYPPFF 216
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
501-685 1.23e-13

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


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 72.36  E-value: 1.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 501 QLVAIK--TLKDYNN--PQQWTefqQEASLMAEL-HHPNIVCLLGAVTQEQPVCMLFEYMnQGDLHEflIMRspHSDVGC 575
Cdd:cd07832   26 ETVALKkvALRKLEGgiPNQAL---REIKALQACqGHPYVVKLRDVFPHGTGFVLVFEYM-LSSLSE--VLR--DEERPL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 576 SSDEdgtVKSsldhgdflhIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSReIYSADYYRVQSkSSLP 655
Cdd:cd07832   98 TEAQ---VKR---------YMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLAR-LFSEEDPRLYS-HQVA 163
                        170       180       190
                 ....*....|....*....|....*....|...
gi 223461072 656 IRW-MPPEaIMYG--KFSSDSDIWSFGVVLWEI 685
Cdd:cd07832  164 TRWyRAPE-LLYGsrKYDEGVDLWAVGCIFAEL 195
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
484-710 1.26e-13

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: 72.13  E-value: 1.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 484 FGKIYKGHLYLPGmdhaQLVAIKTLK--DYNNPQQWTEFQQE-ASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDL 560
Cdd:cd05611    9 FGSVYLAKKRSTG----DYFAIKVLKksDMIAKNQVTNVKAErAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLNGGDC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 561 HEFLIMRSPhsdvgcsSDEDGTVKssldhgdflHIAiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSRei 640
Cdd:cd05611   85 ASLIKTLGG-------LPEDWAKQ---------YIA-EVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSR-- 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223461072 641 ysADYYRVQSK--SSLPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEiFSFGLQPYYGFSNQEVIEMVRKRQL 710
Cdd:cd05611  146 --NGLEKRHNKkfVGTP-DYLAPETILGVGDDKMSDWWSLGCVIFE-FLFGYPPFHAETPDAVFDNILSRRI 213
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
479-748 1.31e-13

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


Pssm-ID: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 72.22  E-value: 1.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLylpgmdHAQLVAIKTLKDYNNPQ---QWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYM 555
Cdd:cd14160    1 IGEGEIFEVYRVRI------GNRSYAVKLFKQEKKMQwkkHWKRFLSELEVLLLFQHPNILELAAYFTETEKFCLVYPYM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQGDLHEFLimrsphsdvGCSSDEdgtvkSSLDHGDFLHIAIQIAAGMEYLSSH---FFVHKDLAARNILIGEQLHVKIS 632
Cdd:cd14160   75 QNGTLFDRL---------QCHGVT-----KPLSWHERINILIGIAKAIHYLHNSqpcTVICGNISSANILLDDQMQPKLT 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 633 DLGLSR----EIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQ-----PYYGFSNQEVIE 703
Cdd:cd14160  141 DFALAHfrphLEDQSCTINMTTALHKHLWYMPEEYIRQGKLSVKTDVYSFGIVIMEVLT-GCKvvlddPKHLQLRDLLHE 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 223461072 704 MVRKRQLLPC-------SEDCPP----RMYSLMTECWNEIPSRRPRFKDIHVRLRS 748
Cdd:cd14160  220 LMEKRGLDSClsfldlkFPPCPRnfsaKLFRLAGRCTATKAKLRPDMDEVLQRLES 275
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
476-685 1.45e-13

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


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 71.71  E-value: 1.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYkghlYLPGMDHAQLVAIKTLkDYNNPQQ---WTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLF 552
Cdd:cd06607    6 LREIGHGSFGAVY----YARNKRTSEVVAIKKM-SYSGKQStekWQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 EYMnqgdlheflimrsphsdVGCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKIS 632
Cdd:cd06607   81 EYC-----------------LGSASDIVEVHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLA 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 223461072 633 DLGLSREIYSAdyyrvQSKSSLPIrWMPPEAIMY---GKFSSDSDIWSFGVVLWEI 685
Cdd:cd06607  144 DFGSASLVCPA-----NSFVGTPY-WMAPEVILAmdeGQYDGKVDVWSLGITCIEL 193
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
501-712 1.54e-13

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: 71.70  E-value: 1.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 501 QLVAIKTLkDYNNPQQWTEFQQEASLMAELHHPNIVCLLGA--VTQEQPVCMlfEYMNQGDLheflimrsphsdvgcssd 578
Cdd:cd06648   33 RQVAVKKM-DLRKQQRRELLFNEVVIMRDYQHPNIVEMYSSylVGDELWVVM--EFLEGGAL------------------ 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 579 EDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIySADYYRVQSKSSLPIrW 658
Cdd:cd06648   92 TDIVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQV-SKEVPRRKSLVGTPY-W 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 223461072 659 MPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYygFSNQEVIEMVRKRQLLP 712
Cdd:cd06648  170 MAPEVISRLPYGTEVDIWSLGIMVIEMVD-GEPPY--FNEPPLQAMKRIRDNEP 220
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
501-700 1.56e-13

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: 73.09  E-value: 1.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 501 QLVAIKTLK--DYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLImrspHSDVgcsSD 578
Cdd:cd05573   27 QVYAMKILRksDMLKREQIAHVRAERDILADADSPWIVRLHYAFQDEDHLYLVMEYMPGGDLMNLLI----KYDV---FP 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 579 EDgTVKssldhgdfLHIAiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSAD---YYRVQS----- 650
Cdd:cd05573  100 EE-TAR--------FYIA-ELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMNKSGdreSYLNDSvntlf 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223461072 651 -KSSLPIRW------------------MPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQE 700
Cdd:cd05573  170 qDNVLARRRphkqrrvraysavgtpdyIAPEVLRGTGYGPECDWWSLGVILYEML-YGFPPFYSDSLVE 237
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
504-687 1.64e-13

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


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 72.05  E-value: 1.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 504 AIKTLKDYNNPQQWTEFQQ----EASLMAELHHPNIVCLLGAVTQEQ-PVCMLFEYMNQ--GDLHEfliMRSphsdvgcs 576
Cdd:cd14001   32 AVKKINSKCDKGQRSLYQErlkeEAKILKSLNHPNIVGFRAFTKSEDgSLCLAMEYGGKslNDLIE---ERY-------- 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 577 SDEDGtvksSLDHGDFLHIAIQIAAGMEYLssHF---FVHKDLAARNILI-GEQLHVKISDLGLS------REIYS---A 643
Cdd:cd14001  101 EAGLG----PFPAATILKVALSIARALEYL--HNekkILHGDIKSGNVLIkGDFESVKLCDFGVSlpltenLEVDSdpkA 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 223461072 644 DYYRVQSksslpirWMPPEAIMYGKFSSD-SDIWSFGVVLWEIFS 687
Cdd:cd14001  175 QYVGTEP-------WKAKEALEEGGVITDkADIFAYGLVLWEMMT 212
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
476-724 1.65e-13

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: 72.42  E-value: 1.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKdyNNPQQWTEFQ--QEASLMAELHHPNIVCLLGAVTQEQPVCMLFE 553
Cdd:cd07869   10 LEKLGEGSYATVYKGKSKVNG----KLVALKVIR--LQEEEGTPFTaiREASLLKGLKHANIVLLHDIIHTKETLTLVFE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 554 YMnqgdlheflimrspHSDVGCSSDEDgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISD 633
Cdd:cd07869   84 YV--------------HTDLCQYMDKH---PGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLAD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 634 LGLSR--EIYSADYyrvqSKSSLPIRWMPPEAIM-YGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSN-QEVIEMVRKRQ 709
Cdd:cd07869  147 FGLARakSVPSHTY----SNEVVTLWYRPPDVLLgSTEYSTCLDMWGVGCIFVEMIQ-GVAAFPGMKDiQDQLERIFLVL 221
                        250
                 ....*....|....*
gi 223461072 710 LLPcSEDCPPRMYSL 724
Cdd:cd07869  222 GTP-NEDTWPGVHSL 235
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
483-686 1.84e-13

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: 72.15  E-value: 1.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 483 TFGKIYKGHLYLPGmdhaQLVAIK-TLKD--YNNpqqwtefqQEASLMAELHHPNIVCLLGA-VTQEQP-----VCMLFE 553
Cdd:cd14137   16 SFGVVYQAKLLETG----EVVAIKkVLQDkrYKN--------RELQIMRRLKHPNIVKLKYFfYSSGEKkdevyLNLVME 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 554 YMNQgDLHEFLIMRSphsdvgcssdedgTVKSSLDhgdFLHIAI---QIAAGMEYLSSHFFVHKDLAARNILIGEQLHV- 629
Cdd:cd14137   84 YMPE-TLYRVIRHYS-------------KNKQTIP---IIYVKLysyQLFRGLAYLHSLGICHRDIKPQNLLVDPETGVl 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223461072 630 KISDLG---------------LSReiysadYYRvqsksslpirwmPPEAImYG--KFSSDSDIWSFGVVLWEIF 686
Cdd:cd14137  147 KLCDFGsakrlvpgepnvsyiCSR------YYR------------APELI-FGatDYTTAIDIWSAGCVLAELL 201
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
477-736 1.92e-13

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: 71.56  E-value: 1.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHlylpGMDHAQLVAIKTLkdynNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMN 556
Cdd:cd14010    6 DEIGRGKHSVVYKGR----RKGTIEFVAIKCV----DKSKRPEVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLimrsphsdvgcSSDEdgtvksSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGL 636
Cdd:cd14010   78 GGDLETLL-----------RQDG------NLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 637 SREI----------YSADYYRVQSKSSLPIR----WMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVI 702
Cdd:cd14010  141 ARREgeilkelfgqFSDEGNVNKVSKKQAKRgtpyYMAPELFQGGVHSFASDLWALGCVLYEMF-TGKPPFVAESFTELV 219
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 223461072 703 EMVRKRQLLP----CSEDCPPRMYSLMTECWNEIPSRR 736
Cdd:cd14010  220 EKILNEDPPPpppkVSSKPSPDFKSLLKGLLEKDPAKR 257
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
469-693 1.92e-13

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: 71.50  E-value: 1.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 469 PLSAVRFMEELGECTFGKIYKGHLYLPGMDhaqlVAIKTLKDYNNPQQwTEFQQEASLMAELHHPNIVCLLGAVTQEQPV 548
Cdd:cd06647    5 PKKKYTRFEKIGQGASGTVYTAIDVATGQE----VAIKQMNLQQQPKK-ELIINEILVMRENKNPNIVNYLDSYLVGDEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 549 CMLFEYMNQGDLheflimrsphSDVgcssdedgTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLH 628
Cdd:cd06647   80 WVVMEYLAGGSL----------TDV--------VTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGS 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223461072 629 VKISDLGLSREIYSAdyyrvQSKSSLPI---RWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPY 693
Cdd:cd06647  142 VKLTDFGFCAQITPE-----QSKRSTMVgtpYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 203
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
479-745 2.03e-13

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


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 71.16  E-value: 2.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIykghLYLPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQG 558
Cdd:cd08219    8 VGEGSFGRA----LLVQHVNSDQKYAMKEIRLPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYCDGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 559 DLhefliMRSPHSDVGCSSDEDgtvkssldhgDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSR 638
Cdd:cd08219   84 DL-----MQKIKLQRGKLFPED----------TILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSAR 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 639 EIYSADYYRVQSKSSlPIrWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGlQPYYGFSNQEVIEMVRKRQLLPCSEDCP 718
Cdd:cd08219  149 LLTSPGAYACTYVGT-PY-YVPPEIWENMPYNNKSDIWSLGCILYELCTLK-HPFQANSWKNLILKVCQGSYKPLPSHYS 225
                        250       260
                 ....*....|....*....|....*..
gi 223461072 719 PRMYSLMTECWNEIPSRRPRFKDIHVR 745
Cdd:cd08219  226 YELRSLIKQMFKRNPRSRPSATTILSR 252
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
469-685 2.13e-13

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: 72.06  E-value: 2.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 469 PLSAVRFMEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQwtEFQQEASLMAEL-HHPNIVCLLGAVTQEQP 547
Cdd:cd06637    4 PAGIFELVELVGNGTYGQVYKGRHVKTG----QLAAIKVMDVTGDEEE--EIKQEINMLKKYsHHRNIATYYGAFIKKNP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 548 VCMlfeymnqgDLHEFLIMRSphsdVGCSSDED---GTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIG 624
Cdd:cd06637   78 PGM--------DDQLWLVMEF----CGAGSVTDlikNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLT 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223461072 625 EQLHVKISDLGLSREIySADYYRVQSKSSLPIrWMPPEAIMY-----GKFSSDSDIWSFGVVLWEI 685
Cdd:cd06637  146 ENAEVKLVDFGVSAQL-DRTVGRRNTFIGTPY-WMAPEVIACdenpdATYDFKSDLWSLGITAIEM 209
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
474-685 2.31e-13

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: 70.88  E-value: 2.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 474 RFMEELGECTFGKIYK------GHLYlpgmdhaqlvAIKTLKdynnpQQWTEFQQEASLMAEL-------HHPNIVCLLG 540
Cdd:cd13997    3 HELEQIGSGSFSEVFKvrskvdGCLY----------AVKKSK-----KPFRGPKERARALREVeahaalgQHPNIVRYYS 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 541 AVTQEQPVCMLFEYMNQGDLHEFLIMRSPhsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARN 620
Cdd:cd13997   68 SWEEGGHLYIQMELCENGSLQDALEELSP--------------ISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDN 133
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223461072 621 ILIGEQLHVKISDLGLSREIYSAdyYRVQSKSSlpiRWMPPEAIMYGKFSSDS-DIWSFGVVLWEI 685
Cdd:cd13997  134 IFISNKGTCKIGDFGLATRLETS--GDVEEGDS---RYLAPELLNENYTHLPKaDIFSLGVTVYEA 194
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
503-719 3.78e-13

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: 71.17  E-value: 3.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 503 VAIKTLkDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLimrsphSDVGCSSDEDGT 582
Cdd:cd06659   49 VAVKMM-DLRKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGALTDIV------SQTRLNEEQIAT 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 583 VKSSldhgdflhiaiqIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIySADYYRVQSKSSLPIrWMPPE 662
Cdd:cd06659  122 VCEA------------VLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQI-SKDVPKRKSLVGTPY-WMAPE 187
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 223461072 663 AIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYygFSNQEVIEMVRKRqllpcseDCPP 719
Cdd:cd06659  188 VISRCPYGTEVDIWSLGIMVIEMVD-GEPPY--FSDSPVQAMKRLR-------DSPP 234
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
454-693 4.39e-13

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: 70.91  E-value: 4.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 454 SMLNAYKPKSKAkelplsaVRFmEELGECTFGKIYKGhlylpgMDHA--QLVAIKTLKDYNNPQQwTEFQQEASLMAELH 531
Cdd:cd06654   11 SIVSVGDPKKKY-------TRF-EKIGQGASGTVYTA------MDVAtgQEVAIRQMNLQQQPKK-ELIINEILVMRENK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 532 HPNIVCLLGAVTQEQPVCMLFEYMNQGDLheflimrsphsdvgcssdEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFF 611
Cdd:cd06654   76 NPNIVNYLDSYLVGDELWVVMEYLAGGSL------------------TDVVTETCMDEGQIAAVCRECLQALEFLHSNQV 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 612 VHKDLAARNILIGEQLHVKISDLGLSREIYSAdyyrvQSKSSLPI---RWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSf 688
Cdd:cd06654  138 IHRDIKSDNILLGMDGSVKLTDFGFCAQITPE-----QSKRSTMVgtpYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIE- 211

                 ....*
gi 223461072 689 GLQPY 693
Cdd:cd06654  212 GEPPY 216
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
501-707 4.43e-13

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: 70.36  E-value: 4.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 501 QLVAIKTL--KDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMrsphsdvgcssd 578
Cdd:cd14081   27 QKVAIKIVnkEKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEYVSGGELFDYLVK------------ 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 579 edgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSreiysadyyRVQSKSSL---- 654
Cdd:cd14081   95 -----KGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMA---------SLQPEGSLlets 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 223461072 655 ---PiRWMPPEAIMYGKFSSD-SDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRK 707
Cdd:cd14081  161 cgsP-HYACPEVIKGEKYDGRkADIWSCGVILYALLV-GALPFDDDNLRQLLEKVKR 215
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
533-685 5.19e-13

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: 70.54  E-value: 5.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 533 PNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLimrSPHsdvGCSSDEDgtVKssldhgdflHIAIQIAAGMEYLSSHFFV 612
Cdd:cd05606   58 PFIVCMTYAFQTPDKLCFILDLMNGGDLHYHL---SQH---GVFSEAE--MR---------FYAAEVILGLEHMHNRFIV 120
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223461072 613 HKDLAARNILIGEQLHVKISDLGLsreiySADYYRVQSKSSLPIR-WMPPEAIMYG-KFSSDSDIWSFGVVLWEI 685
Cdd:cd05606  121 YRDLKPANILLDEHGHVRISDLGL-----ACDFSKKKPHASVGTHgYMAPEVLQKGvAYDSSADWFSLGCMLYKL 190
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
479-736 5.57e-13

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: 70.13  E-value: 5.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGmdhaQLVAIKTL-----KDYNNPQQwteFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFE 553
Cdd:cd14663    8 LGEGTFAKVKFARNTKTG----ESVAIKIIdkeqvAREGMVEQ---IKREIAIMKLLRHPNIVELHEVMATKTKIFFVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 554 YMNQGDLHEFLIMRSPhsdvgcssdedgtvkssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISD 633
Cdd:cd14663   81 LVTGGELFSKIAKNGR-----------------LKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISD 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 634 LGLS--REIYSADYYrVQSKSSLPiRWMPPEAIMY-GKFSSDSDIWSFGVVLWEIfsfgLQPYYGFSNQEVIEMVRK--R 708
Cdd:cd14663  144 FGLSalSEQFRQDGL-LHTTCGTP-NYVAPEVLARrGYDGAKADIWSCGVILFVL----LAGYLPFDDENLMALYRKimK 217
                        250       260
                 ....*....|....*....|....*...
gi 223461072 709 QLLPCSEDCPPRMYSLMTECWNEIPSRR 736
Cdd:cd14663  218 GEFEYPRWFSPGAKSLIKRILDPNPSTR 245
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
478-737 6.06e-13

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: 70.06  E-value: 6.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 478 ELGECTFGKIYKGHlylpgmDHA--QLVAIKTLKdYNNPQQWTEFQQEASLMAEL-HHPNIVCLLG-AVTQEQP---VCM 550
Cdd:cd13985    7 QLGEGGFSYVYLAH------DVNtgRRYALKRMY-FNDEEQLRVAIKEIEIMKRLcGHPNIVQYYDsAILSSEGrkeVLL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 551 LFEYMnQGDLHEFLIMRSPhsdvgcssdedgtvkSSLDHGDFLHIAIQIAAGMEYLSSHF--FVHKDLAARNILIGEQLH 628
Cdd:cd13985   80 LMEYC-PGSLVDILEKSPP---------------SPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGR 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 629 VKISDLG-LSREIYSadYYR----------VQSKSSLPIRwmPPEAI-MYGKF--SSDSDIWSFGVVLWEIFSFGLqPyy 694
Cdd:cd13985  144 FKLCDFGsATTEHYP--LERaeevniieeeIQKNTTPMYR--APEMIdLYSKKpiGEKADIWALGCLLYKLCFFKL-P-- 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 223461072 695 gFSNQEVIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRP 737
Cdd:cd13985  217 -FDESSKLAIVAGKYSIPEQPRYSPELHDLIRHMLTPDPAERP 258
CRD_FZ cd07066
CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential ...
170-297 6.75e-13

CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential component of a number of cell surface receptors, which are involved in multiple signal transduction pathways, particularly in modulating the activity of the Wnt proteins, which play a fundamental role in the early development of metazoans. CRD is also found in secreted frizzled related proteins (SFRPs), which lack the transmembrane segment found in the frizzled protein. The CRD domain is also present in the alpha-1 chain of mouse type XVIII collagen, in carboxypeptidase Z, several receptor tyrosine kinases, and the mosaic transmembrane serine protease corin. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. CRD domains have also been identified in multiple tandem copies in a Dictyostelium discoideum protein. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines.


Pssm-ID: 143549  Cd Length: 119  Bit Score: 65.99  E-value: 6.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 170 CQPYRGIACARFIGNRTVYMESLHMqgeiENQITAAFTMIGTSSHLSDKCSQFAIPSLCHYAFPYCDETSSVPKPrdLCR 249
Cdd:cd07066    2 CEPIPLPLCRGLPYNTTRFPNLLGH----ESQEEAEQELESFTPLVNSGCHPDLRFFLCSLYFPECTPDGDRPIP--PCR 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 223461072 250 DECE-VLENvlCQTEYIFARsnpmiLMRLKLPNCEDLpqPESPEAANCI 297
Cdd:cd07066   76 SLCEeVRDS--CEPLMLAFG-----FPWPEPLDCDRF--PDSNEEGLCI 115
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
60-148 7.73e-13

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 64.72  E-value: 7.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  60 LDEPMNNITTsLGQTAELHCKVSGNPPPSIRWFKNDA--PVvqepRRISFRATNygsRLRIRNLDTTDTGYFQCVATNGK 137
Cdd:cd05725    1 VKRPQNQVVL-VDDSAEFQCEVGGDPVPTVRWRKEDGelPK----GRYEILDDH---SLKIRKVTAGDMGSYTCVAENMV 72
                         90
                 ....*....|.
gi 223461072 138 KVVSTTGVLFV 148
Cdd:cd05725   73 GKIEASATLTV 83
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
475-687 9.88e-13

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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: 69.65  E-value: 9.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYKGhlylpgMDHA--QLVAIKTLKD-YNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCML 551
Cdd:cd07833    5 VLGVVGEGAYGVVLKC------RNKAtgEIVAIKKFKEsEDDEDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMNQGDLHefLIMRSPHsdvGCSSDedgTVKSSLdhgdflhiaIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKI 631
Cdd:cd07833   79 FEYVERTLLE--LLEASPG---GLPPD---AVRSYI---------WQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKL 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223461072 632 SDLGLSREIysadyyrvQSKSSLPI------RWM-PPE----AIMYGKfssDSDIWSFGVVLWEIFS 687
Cdd:cd07833  142 CDFGFARAL--------TARPASPLtdyvatRWYrAPEllvgDTNYGK---PVDVWAIGCIMAELLD 197
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
501-693 1.10e-12

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: 69.26  E-value: 1.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 501 QLVAIKTLK---DYNNPQQWTE-FQQEASLMAELHHPNIV---CLLgaVTQEQPVCMLFEYMNQGDLHEFLIMRSphsdv 573
Cdd:cd13994   21 VLYAVKEYRrrdDESKRKDYVKrLTSEYIISSKLHHPNIVkvlDLC--QDLHGKWCLVMEYCPGGDLFTLIEKAD----- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 574 gcssdedgtvksSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGlsreiySADYYRVQSKS- 652
Cdd:cd13994   94 ------------SLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFG------TAEVFGMPAEKe 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 223461072 653 ---------SLPirWMPPEAIMYGKFSSDS-DIWSFGVVLWEIFsFGLQPY 693
Cdd:cd13994  156 spmsaglcgSEP--YMAPEVFTSGSYDGRAvDVWSCGIVLFALF-TGRFPW 203
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
479-742 1.19e-12

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: 68.89  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKghlyLPGMDHAQLVAIKTL--KDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMN 556
Cdd:cd14188    9 LGKGGFAKCYE----MTDLTTNKVYAAKIIphSRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLIMRSphsdvgcssdedgtvksSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGL 636
Cdd:cd14188   85 RRSMAHILKARK-----------------VLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 637 SREIYSADYYRvQSKSSLPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVIEMVRK-RQLLPCSE 715
Cdd:cd14188  148 AARLEPLEHRR-RTICGTP-NYLSPEVLNKQGHGCESDIWALGCVMYTML-LGRPPFETTNLKETYRCIREaRYSLPSSL 224
                        250       260
                 ....*....|....*....|....*..
gi 223461072 716 DCPPRmySLMTECWNEIPSRRPRFKDI 742
Cdd:cd14188  225 LAPAK--HLIASMLSKNPEDRPSLDEI 249
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
579-710 1.22e-12

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: 69.11  E-value: 1.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 579 EDGTVKSSLDHGDFL------HIAIQIAAGMEYLSSHFFVHKDLAARNILI-------GEQLHVKISDLGLSREIYSADY 645
Cdd:cd14097   83 EDGELKELLLRKGFFsenetrHIIQSLASAVAYLHKNDIVHRDLKLENILVkssiidnNDKLNIKVTDFGLSVQKYGLGE 162
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223461072 646 YRVQSKSSLPIrWMPPEAIMYGKFSSDSDIWSFGVVLWeIFSFGLQPYYGFSNQEVIEMVRKRQL 710
Cdd:cd14097  163 DMLQETCGTPI-YMAPEVISAHGYSQQCDIWSIGVIMY-MLLCGEPPFVAKSEEKLFEEIRKGDL 225
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
473-694 1.47e-12

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


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 69.14  E-value: 1.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 473 VRFMEELGECTFGKI----YKghlylpgmDHAQLVAIKTLKDynnpQQWTEFQQ------EASLMAELHHPNIVCLLGAV 542
Cdd:cd05580    3 FEFLKTLGTGSFGRVrlvkHK--------DSGKYYALKILKK----AKIIKLKQvehvlnEKRILSEVRHPFIVNLLGSF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 543 TQEQPVCMLFEYMNQGDLheFLIMRSPHsdvgcssdedgtvKSSLDHGDFLhiAIQIAAGMEYLSSHFFVHKDLAARNIL 622
Cdd:cd05580   71 QDDRNLYMVMEYVPGGEL--FSLLRRSG-------------RFPNDVAKFY--AAEVVLALEYLHSLDIVYRDLKPENLL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 623 IGEQLHVKISDLGLSREI----YS----ADYyrvqsksslpirwMPPEAIM---YGKfssDSDIWSFGVVLWEIFSfGLQ 691
Cdd:cd05580  134 LDSDGHIKITDFGFAKRVkdrtYTlcgtPEY-------------LAPEIILskgHGK---AVDWWALGILIYEMLA-GYP 196

                 ...
gi 223461072 692 PYY 694
Cdd:cd05580  197 PFF 199
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
489-742 1.57e-12

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: 68.73  E-value: 1.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 489 KGHLYLPGMDHAQLVAIKTLKDyNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLImrs 568
Cdd:cd14045   19 KKPFTQTGIYDGRTVAIKKIAK-KSFTLSKRIRKEVKQVRELDHPNLCKFIGGCIEVPNVAIITEYCPKGSLNDVLL--- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 569 phsdvgcssDEDgtvkSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLS---REIYSADY 645
Cdd:cd14045   95 ---------NED----IPLNWGFRFSFATDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADYGLTtyrKEDGSENA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 646 YRVQSKssLPIRWMPPEA--IMYGKFSSDSDIWSFGVVLWEIFSFG-LQPYYGFSNQEVIEMVRKRQLLPCSED---CPP 719
Cdd:cd14045  162 SGYQQR--LMQVYLPPENhsNTDTEPTQATDVYSYAIILLEIATRNdPVPEDDYSLDEAWCPPLPELISGKTENscpCPA 239
                        250       260
                 ....*....|....*....|...
gi 223461072 720 RMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14045  240 DYVELIRRCRKNNPAQRPTFEQI 262
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
479-737 1.59e-12

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: 69.07  E-value: 1.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGmdhaQLVAIK-------TLKDYnnpqqwTEFQQEASLMAELHHPNIVCLLGAvTQEQPVCML 551
Cdd:cd14049   14 LGKGGYGKVYKVRNKLDG----QYYAIKkilikkvTKRDC------MKVLREVKVLAGLQHPNIVGYHTA-WMEHVQLML 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMN--QGDLHEFLIMRSPHsdvGCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILI-GEQLH 628
Cdd:cd14049   83 YIQMQlcELSLWDWIVERNKR---PCEEEFKSAPYTPVDVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLhGSDIH 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 629 VKISDLGLS-REIY--SADYYRVQSKSSL-------PIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFsfglQPY-YGFS 697
Cdd:cd14049  160 VRIGDFGLAcPDILqdGNDSTTMSRLNGLthtsgvgTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF----QPFgTEME 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 223461072 698 NQEVIEMVRKRQlLPCSEDCPPRMYS-LMTECWNEIPSRRP 737
Cdd:cd14049  236 RAEVLTQLRNGQ-IPKSLCKRWPVQAkYIKLLTSTEPSERP 275
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
508-742 1.72e-12

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: 68.76  E-value: 1.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 508 LKDYNNPQQWTEFQQEASL--MAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLimrsphSDVgcSSDEDGTVks 585
Cdd:cd14044   36 LKDLKNNEGNFTEKQKIELnkLLQIDYYNLTKFYGTVKLDTMIFGVIEYCERGSLRDVL------NDK--ISYPDGTF-- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 586 sLDHGDFLHIAIQIAAGMEYL-SSHFFVHKDLAARNILIGEQLHVKISDLGlsreiysadyyrvqSKSSLPIR---WMPP 661
Cdd:cd14044  106 -MDWEFKISVMYDIAKGMSYLhSSKTEVHGRLKSTNCVVDSRMVVKITDFG--------------CNSILPPSkdlWTAP 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 662 EAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVIEMVRKRQL------------LPCSEDCPPRMYSLMTECW 729
Cdd:cd14044  171 EHLRQAGTSQKGDVYSYGIIAQEII-LRKETFYTAACSDRKEKIYRVQNpkgmkpfrpdlnLESAGEREREVYGLVKNCW 249
                        250
                 ....*....|...
gi 223461072 730 NEIPSRRPRFKDI 742
Cdd:cd14044  250 EEDPEKRPDFKKI 262
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
479-683 1.96e-12

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


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 68.35  E-value: 1.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGMDhaqlVAIKTL--KDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMN 556
Cdd:cd14186    9 LGKGSFACVYRARSLHTGLE----VAIKMIdkKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEMCH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLIMRsphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGL 636
Cdd:cd14186   85 NGEMSRYLKNR----------------KKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGL 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 223461072 637 SREIYSADyYRVQSKSSLPiRWMPPEAIMYGKFSSDSDIWSFGVVLW 683
Cdd:cd14186  149 ATQLKMPH-EKHFTMCGTP-NYISPEIATRSAHGLESDVWSLGCMFY 193
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
526-686 2.01e-12

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: 69.48  E-value: 2.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 526 LMAELHHPNIVCLLGAVTQEQP-----VCMLFEYMnQGDLHEflIMRSPHsdvgcssdedgtvKSSLDHGDFlhIAIQIA 600
Cdd:cd07834   52 ILRHLKHENIIGLLDILRPPSPeefndVYIVTELM-ETDLHK--VIKSPQ-------------PLTDDHIQY--FLYQIL 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 601 AGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSAD------------YYRvqsksslpirwmPPEAIM-YG 667
Cdd:cd07834  114 RGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLARGVDPDEdkgflteyvvtrWYR------------APELLLsSK 181
                        170
                 ....*....|....*....
gi 223461072 668 KFSSDSDIWSFGVVLWEIF 686
Cdd:cd07834  182 KYTKAIDIWSVGCIFAELL 200
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
470-737 2.26e-12

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: 68.90  E-value: 2.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 470 LSAVRFMEELGECTFGKIYKGHLYLPGMdhaqLVAIKTLK--DYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQP 547
Cdd:cd08229   23 LANFRIEKKIGRGQFSEVYRATCLLDGV----PVALKKVQifDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 548 VCMLFEYMNQGDLHEFLIMRSPHsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQL 627
Cdd:cd08229   99 LNIVLELADAGDLSRMIKHFKKQ-------------KRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 628 HVKISDLGLSReIYSADYYRVQSKSSLPIrWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGlQPYYGfSNQEVIEMVRK 707
Cdd:cd08229  166 VVKLGDLGLGR-FFSSKTTAAHSLVGTPY-YMSPERIHENGYNFKSDIWSLGCLLYEMAALQ-SPFYG-DKMNLYSLCKK 241
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 223461072 708 RQllPCseDCPP--------RMYSLMTECWNEIPSRRP 737
Cdd:cd08229  242 IE--QC--DYPPlpsdhyseELRQLVNMCINPDPEKRP 275
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
479-695 2.33e-12

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: 68.62  E-value: 2.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYK------GHLY-LPGMDHAQLVAIKtlkdynnpqQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCML 551
Cdd:cd05612    9 IGTGTFGRVHLvrdrisEHYYaLKVMAIPEVIRLK---------QEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYML 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMNQGDLHEFLIMRsphsdvgcssdedGTVKSSLdhGDFLhiAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKI 631
Cdd:cd05612   80 MEYVPGGELFSYLRNS-------------GRFSNST--GLFY--ASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKL 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223461072 632 SDLGLSREIYSadyyRVQSKSSLPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYG 695
Cdd:cd05612  143 TDFGFAKKLRD----RTWTLCGTP-EYLAPEVIQSKGHNKAVDWWALGILIYEMLV-GYPPFFD 200
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
454-693 2.51e-12

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: 68.59  E-value: 2.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 454 SMLNAYKPKSKAkelplsaVRFmEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQwTEFQQEASLMAELHHP 533
Cdd:cd06656   10 SIVSVGDPKKKY-------TRF-EKIGQGASGTVYTAIDIATG----QEVAIKQMNLQQQPKK-ELIINEILVMRENKNP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 534 NIVCLLGAVTQEQPVCMLFEYMNQGDLheflimrsphsdvgcssdEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVH 613
Cdd:cd06656   77 NIVNYLDSYLVGDELWVVMEYLAGGSL------------------TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIH 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 614 KDLAARNILIGEQLHVKISDLGLSREIYSAdyyrvQSKSSLPI---RWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGL 690
Cdd:cd06656  139 RDIKSDNILLGMDGSVKLTDFGFCAQITPE-----QSKRSTMVgtpYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GE 212

                 ...
gi 223461072 691 QPY 693
Cdd:cd06656  213 PPY 215
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
503-717 2.97e-12

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: 67.80  E-value: 2.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 503 VAIKTL-KDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRsphsdvGCSSDEDG 581
Cdd:cd14071   28 VAIKIIdKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYASNGEIFDYLAQH------GRMSEKEA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 582 TVKssldhgdFLhiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSrEIYSADYYRVQSKSSLPirWMPP 661
Cdd:cd14071  102 RKK-------FW----QILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFS-NFFKPGELLKTWCGSPP--YAAP 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 662 EAIMYGKFSS-DSDIWSFGVVLWeIFSFGLQPYYGFSNQEVIEMV---RKRQLLPCSEDC 717
Cdd:cd14071  168 EVFEGKEYEGpQLDIWSLGVVLY-VLVCGALPFDGSTLQTLRDRVlsgRFRIPFFMSTDC 226
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
477-693 3.09e-12

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: 68.60  E-value: 3.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQwTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMN 556
Cdd:cd06655   25 EKIGQGASGTVFTAIDVATG----QEVAIKQINLQKQPKK-ELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLheflimrsphsdvgcssdEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGL 636
Cdd:cd06655  100 GGSL------------------TDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGF 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 637 SREIYSAdyyrvQSKSSLPI---RWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPY 693
Cdd:cd06655  162 CAQITPE-----QSKRSTMVgtpYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 215
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
479-736 3.11e-12

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: 68.56  E-value: 3.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGMDHAQLVAIKTLKdYNNPQQWtefQQEASL--MAELHHPNIVCLLGA----VTQEQPVCMLF 552
Cdd:cd14055    3 VGKGRFAEVWKAKLKQNASGQYETVAVKIFP-YEEYASW---KNEKDIftDASLKHENILQFLTAeergVGLDRQYWLIT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 EYMNQGDLHEFLimrsphsdvgcssdedgtVKSSLDHGDFLHIAIQIAAGMEYLSSHFF---------VHKDLAARNILI 623
Cdd:cd14055   79 AYHENGSLQDYL------------------TRHILSWEDLCKMAGSLARGLAHLHSDRTpcgrpkipiAHRDLKSSNILV 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 624 GEQLHVKISDLGLSREI---YSADYYRVQSKSSLPiRWMPPEAImygkfssDS-------------DIWSFGVVLWEIFS 687
Cdd:cd14055  141 KNDGTCVLADFGLALRLdpsLSVDELANSGQVGTA-RYMAPEAL-------ESrvnledlesfkqiDVYSMALVLWEMAS 212
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223461072 688 F--------GLQPYYG--FSNQEVIEM-----VRKRQL--LPCSEDCPPRMYSL---MTECWNEIPSRR 736
Cdd:cd14055  213 RceasgevkPYELPFGskVRERPCVESmkdlvLRDRGRpeIPDSWLTHQGMCVLcdtITECWDHDPEAR 281
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
523-688 3.22e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 69.13  E-value: 3.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 523 EASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQgDLHEFLIMRSphsdvgcssdedgtvkSSLDHGDFLHIAIQIAAG 602
Cdd:PHA03209 107 EAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYSS-DLYTYLTKRS----------------RPLPIDQALIIEKQILEG 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 603 MEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSR-EIYSADYYRVQSKsslpIRWMPPEAIMYGKFSSDSDIWSFGVV 681
Cdd:PHA03209 170 LRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQfPVVAPAFLGLAGT----VETNAPEVLARDKYNSKADIWSAGIV 245

                 ....*..
gi 223461072 682 LWEIFSF 688
Cdd:PHA03209 246 LFEMLAY 252
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
469-692 3.54e-12

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: 67.75  E-value: 3.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 469 PLSAVRFMEELGECTFGKIYKGHlylpGMDHAQLVAIKTLKdYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPV 548
Cdd:cd06646    7 PQHDYELIQRVGSGTYGDVYKAR----NLHTGELAAVKIIK-LEPGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 549 CMLFEYMNQGDLHEFLIMRSPHSDVGCSsdedgtvkssldhgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLH 628
Cdd:cd06646   82 WICMEYCGGGSLQDIYHVTGPLSELQIA-----------------YVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGD 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223461072 629 VKISDLGLSREIySADYYRVQSKSSLPIrWMPPEAIMY---GKFSSDSDIWSFGVVLWEIFSfgLQP 692
Cdd:cd06646  145 VKLADFGVAAKI-TATIAKRKSFIGTPY-WMAPEVAAVeknGGYNQLCDIWAVGITAIELAE--LQP 207
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
479-736 4.66e-12

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: 68.11  E-value: 4.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGMDHAQLVAIKTL---KDynnpqQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYM 555
Cdd:cd05595    3 LGKGTFGKVILVREKATGRYYAMKILRKEViiaKD-----EVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQGDLHEFLIMRSPHSDvgcssdedgtvksslDHGDFLhiAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLG 635
Cdd:cd05595   78 NGGELFFHLSRERVFTE---------------DRARFY--GAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFG 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 636 LSREIYSaDYYRVQSKSSLPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRKRQL-LPcs 714
Cdd:cd05595  141 LCKEGIT-DGATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHERLFELILMEEIrFP-- 215
                        250       260
                 ....*....|....*....|..
gi 223461072 715 EDCPPRMYSLMTECWNEIPSRR 736
Cdd:cd05595  216 RTLSPEAKSLLAGLLKKDPKQR 237
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
474-707 5.52e-12

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: 67.30  E-value: 5.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 474 RFMEELGECTFGKIYKGHlylpGMDHAQLVAIKTLKD-YNNPQQWTEFQqEASLMAEL-HHPNIVCLLGAVTQEQPVC-- 549
Cdd:cd07831    2 KILGKIGEGTFSEVLKAQ----SRKTGKYYAIKCMKKhFKSLEQVNNLR-EIQALRRLsPHPNILRLIEVLFDRKTGRla 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 550 MLFEYMNQgDLHEFLIMRSPHSDvgcssdeDGTVKSSLdhgdflhiaIQIAAGMEYLSSHFFVHKDLAARNILIgEQLHV 629
Cdd:cd07831   77 LVFELMDM-NLYELIKGRKRPLP-------EKRVKNYM---------YQLLKSLDHMHRNGIFHRDIKPENILI-KDDIL 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 630 KISDLGLSREIYS----ADYyrvqskssLPIRWM-PPEAIMY-GKFSSDSDIWSFGVVLWEIFSfgLQPYYGFSNQevIE 703
Cdd:cd07831  139 KLADFGSCRGIYSkppyTEY--------ISTRWYrAPECLLTdGYYGPKMDIWAVGCVFFEILS--LFPLFPGTNE--LD 206

                 ....
gi 223461072 704 MVRK 707
Cdd:cd07831  207 QIAK 210
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
522-693 5.56e-12

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: 67.28  E-value: 5.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 522 QEASLMAELHHPNIVCLLGAVTQ--EQPVCMLFEYMNQGDlheflIMRSPhSDVGCSSDEDgtvkssldhgdfLHIAIQI 599
Cdd:cd14200   72 QEIAILKKLDHVNIVKLIEVLDDpaEDNLYMVFDLLRKGP-----VMEVP-SDKPFSEDQA------------RLYFRDI 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 600 AAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSADyYRVQSKSSLPIrWMPPEAIM-YGK-FSSDS-DIW 676
Cdd:cd14200  134 VLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIADFGVSNQFEGND-ALLSSTAGTPA-FMAPETLSdSGQsFSGKAlDVW 211
                        170
                 ....*....|....*..
gi 223461072 677 SFGVVLWeIFSFGLQPY 693
Cdd:cd14200  212 AMGVTLY-CFVYGKCPF 227
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
477-739 6.04e-12

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: 67.30  E-value: 6.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLylpgmdHAQlVAIKTLK-DYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYM 555
Cdd:cd14152    6 ELIGQGRWGKVHRGRW------HGE-VAIRLLEiDGNNQDHLKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAIITSFC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQGDLHEFLimRSPhsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIgEQLHVKISDLG 635
Cdd:cd14152   79 KGRTLYSFV--RDP--------------KTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFG 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 636 LSREIYSADYYRVQSKSSLPIRW---MPPEAIMY---GK------FSSDSDIWSFGVVLWEifsfgLQPY-YGFSNQEVI 702
Cdd:cd14152  142 LFGISGVVQEGRRENELKLPHDWlcyLAPEIVREmtpGKdedclpFSKAADVYAFGTIWYE-----LQARdWPLKNQPAE 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 223461072 703 EMVRK-------RQLLpCSEDCPPRMYSLMTECWNEIPSRRPRF 739
Cdd:cd14152  217 ALIWQigsgegmKQVL-TTISLGKEVTEILSACWAFDLEERPSF 259
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
479-740 6.24e-12

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: 66.76  E-value: 6.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGmdhaQLVAIKTLkDYNNPQQWT----EFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd14070   10 LGEGSFAKVREGLHAVTG----EKVAIKVI-DKKKAKKDSyvtkNLRREGRIQQMIRHPNITQLLDILETENSYYLVMEL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQGDLHEFLimrsphsdvgCSsdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd14070   85 CPGGNLMHRI----------YD-------KKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDF 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 635 GLSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFS----FGLQPyygFSNQEVIEMVRKRQL 710
Cdd:cd14070  148 GLSNCAGILGYSDPFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTgtlpFTVEP---FSLRALHQKMVDKEM 224
                        250       260       270
                 ....*....|....*....|....*....|
gi 223461072 711 LPCSEDCPPRMYSLMTECWNEIPSRRPRFK 740
Cdd:cd14070  225 NPLPTDLSPGAISFLRSLLEPDPLKRPNIK 254
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
504-742 7.38e-12

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: 67.21  E-value: 7.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 504 AIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAvTQEQPVCMLFEYMNQGDLheFLIMRSphsdvgCSSD--EDG 581
Cdd:cd14048   35 AVKRIRLPNNELAREKVLREVRALAKLDHPGIVRYFNA-WLERPPEGWQEKMDEVYL--YIQMQL------CRKEnlKDW 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 582 TVKS----SLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSR---------------EIYS 642
Cdd:cd14048  106 MNRRctmeSRELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLVTamdqgepeqtvltpmPAYA 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 643 ADYYRVQSKSslpirWMPPEAIMYGKFSSDSDIWSFGVVLWE-IFSFGLQpyygFSNQEVIEMVRKRQLLPCSEDCPPRM 721
Cdd:cd14048  186 KHTGQVGTRL-----YMSPEQIHGNQYSEKVDIFALGLILFElIYSFSTQ----MERIRTLTDVRKLKFPALFTNKYPEE 256
                        250       260
                 ....*....|....*....|.
gi 223461072 722 YSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14048  257 RDMVQQMLSPSPSERPEAHEV 277
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
502-685 8.37e-12

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: 66.68  E-value: 8.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 502 LVAIKTLKDYNNPQQWTE-----FQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSPHSDVgcs 576
Cdd:cd06630   27 LMAVKQVSFCRNSSSEQEevveaIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAGGSVASLLSKYGAFSEN--- 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 577 sdedgTVKSsldhgdFLHiaiQIAAGMEYLSSHFFVHKDLAARNILI---GEqlHVKISDLG----LSREIYSADYYRVQ 649
Cdd:cd06630  104 -----VIIN------YTL---QILRGLAYLHDNQIIHRDLKGANLLVdstGQ--RLRIADFGaaarLASKGTGAGEFQGQ 167
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 223461072 650 SKSSlpIRWMPPEAIMYGKFSSDSDIWSFGVVLWEI 685
Cdd:cd06630  168 LLGT--IAFMAPEVLRGEQYGRSCDVWSVGCVIIEM 201
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
475-737 8.48e-12

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: 66.42  E-value: 8.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYKGhlylPGMDHAQLVAIKTLKDYNNPQQWTE--FQQEASLMAELHHPNIVcllgavtqeqpvcMLF 552
Cdd:cd14164    4 LGTTIGEGSFSKVKLA----TSQKYCCKVAIKIVDRRRASPDFVQkfLPRELSILRRVNHPNIV-------------QMF 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 EYMNQGDLHEFLIMRSPHSDVGCSSDEDGTVKSSLDHGDFlhiaIQIAAGMEYLSSHFFVHKDLAARNILI-GEQLHVKI 631
Cdd:cd14164   67 ECIEVANGRLYIVMEAAATDLLQKIQEVHHIPKDLARDMF----AQMVGAVNYLHDMNIVHRDLKCENILLsADDRKIKI 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 632 SDLGLSREIysADYYRVQSKSSLPIRWMPPEAIMYGKFSSDS-DIWSFGVVLWEIFSfGLQPYYGfsnqEVIEMVRKRQ- 709
Cdd:cd14164  143 ADFGFARFV--EDYPELSTTFCGSRAYTPPEVILGTPYDPKKyDVWSLGVVLYVMVT-GTMPFDE----TNVRRLRLQQr 215
                        250       260       270
                 ....*....|....*....|....*....|
gi 223461072 710 --LLPCSEDCPPRMYSLMTECWNEIPSRRP 737
Cdd:cd14164  216 gvLYPSGVALEEPCRALIRTLLQFNPSTRP 245
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
476-737 9.04e-12

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: 66.76  E-value: 9.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGHLYLPGmdhAQLVAIKTLkDYNNP----------QQWTEFQQEASLMAE-LHHPNIVCLLGAVTQ 544
Cdd:cd08528    5 LELLGSGAFGCVYKVRKKSNG---QTLLALKEI-NMTNPafgrteqerdKSVGDIISEVNIIKEqLRHPNIVRYYKTFLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 545 EQPVCMLFEYMNQGDLHE-FLIMRSPHSDVgcssDEDgtvkssldhgDFLHIAIQIAAGMEYL-SSHFFVHKDLAARNIL 622
Cdd:cd08528   81 NDRLYIVMELIEGAPLGEhFSSLKEKNEHF----TED----------RIWNIFVQMVLALRYLhKEKQIVHRDLKPNNIM 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 623 IGEQLHVKISDLGLSREiYSADYYRVQSKSSLPIRWMpPEAIMYGKFSSDSDIWSFGVVLWEIFSfgLQPYYGFSNQEVI 702
Cdd:cd08528  147 LGEDDKVTITDFGLAKQ-KGPESSKMTSVVGTILYSC-PEIVQNEPYGEKADIWALGCILYQMCT--LQPPFYSTNMLTL 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 223461072 703 EM-VRKRQLLPCSEDcpprMYS-----LMTECWNEIPSRRP 737
Cdd:cd08528  223 ATkIVEAEYEPLPEG----MYSdditfVIRSCLTPDPEARP 259
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
503-684 9.39e-12

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 68.67  E-value: 9.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 503 VAIKTLK-DYNNPQQWTE-FQQEASLMAELHHPNIVcllgAVT---QEQPV---CMlfEYMNQGDLHEFLIMRSPhsdvg 574
Cdd:NF033483  35 VAVKVLRpDLARDPEFVArFRREAQSAASLSHPNIV----SVYdvgEDGGIpyiVM--EYVDGRTLKDYIREHGP----- 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 575 cssdedgtvkssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSRE------------IYS 642
Cdd:NF033483 104 ------------LSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARAlssttmtqtnsvLGT 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 223461072 643 ADYyrvqsksslpirwMPPEAIMYGKFSSDSDIWSFGVVLWE 684
Cdd:NF033483 172 VHY-------------LSPEQARGGTVDARSDIYSLGIVLYE 200
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
523-685 1.00e-11

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: 66.61  E-value: 1.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 523 EASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLhEFLI--MRSPHSDVGCSsdedgtvkssldhgdfLHIAIQIA 600
Cdd:cd05605   50 EKQILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGDL-KFHIynMGNPGFEEERA----------------VFYAAEIT 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 601 AGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSADYY--RVQSksslpIRWMPPEAIMYGKFSSDSDIWSF 678
Cdd:cd05605  113 CGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGETIrgRVGT-----VGYMAPEVVKNERYTFSPDWWGL 187

                 ....*..
gi 223461072 679 GVVLWEI 685
Cdd:cd05605  188 GCLIYEM 194
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
474-687 1.09e-11

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: 66.22  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 474 RFMEELGECTFGKIYKGHlylpGMDHAQLVAIKTLK-DYNNPQQWTE---FQQEASLMAELHHPNIVCLLGAV--TQEQP 547
Cdd:cd06652    5 RLGKLLGQGAFGRVYLCY----DADTGRELAVKQVQfDPESPETSKEvnaLECEIQLLKNLLHERIVQYYGCLrdPQERT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 548 VCMLFEYMNQGDLHEFLimrsphSDVGCSSdEDGTVKSSLdhgdflhiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQL 627
Cdd:cd06652   81 LSIFMEYMPGGSIKDQL------KSYGALT-ENVTRKYTR----------QILEGVHYLHSNMIVHRDIKGANILRDSVG 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223461072 628 HVKISDLGLSREIYSA--DYYRVQSKSSLPIrWMPPEAIMYGKFSSDSDIWSFGVVLWEIFS 687
Cdd:cd06652  144 NVKLGDFGASKRLQTIclSGTGMKSVTGTPY-WMSPEVISGEGYGRKADIWSVGCTVVEMLT 204
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
479-706 1.14e-11

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: 66.34  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGMDhaqlVAIKTLKDYNNPQQWTE--FQQEASLMAELHHPNIVCLLGAV-TQEQPVCMLFEYM 555
Cdd:cd14165    9 LGEGSYAKVKSAYSERLKCN----VAIKIIDKKKAPDDFVEkfLPRELEILARLNHKSIIKTYEIFeTSDGKVYIVMELG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQGDLHEFLIMR-SPHSDVGcssdedgtvkssldhGDFLHiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd14165   85 VQGDLLEFIKLRgALPEDVA---------------RKMFH---QLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDF 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223461072 635 GLSREIYSADYYRVQSKSSL--PIRWMPPEAIMYGKFSSD-SDIWSFGVVLWeIFSFGLQPYygfSNQEVIEMVR 706
Cdd:cd14165  147 GFSKRCLRDENGRIVLSKTFcgSAAYAAPEVLQGIPYDPRiYDIWSLGVILY-IMVCGSMPY---DDSNVKKMLK 217
PHA02988 PHA02988
hypothetical protein; Provisional
502-742 1.31e-11

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 66.30  E-value: 1.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 502 LVAIKTLK-DYNNPQQWTE-FQQEASLMAELHHPNIVCLLG---AVTQEQP-VCMLFEYMNQGDLHEFLIMrsphsdvgc 575
Cdd:PHA02988  45 EVIIRTFKkFHKGHKVLIDiTENEIKNLRRIDSNNILKIYGfiiDIVDDLPrLSLILEYCTRGYLREVLDK--------- 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 576 ssDEDGTVKSSLDhgdflhIAIQIAAGMEYLSSHFFV-HKDLAARNILIGEQLHVKISDLGLSREIYSADYYRVQSkssl 654
Cdd:PHA02988 116 --EKDLSFKTKLD------MAIDCCKGLYNLYKYTNKpYKNLTSVSFLVTENYKLKIICHGLEKILSSPPFKNVNF---- 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 655 pIRWMPPEAI--MYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEM-VRKRQLLPCSEDCPPRMYSLMTECWNE 731
Cdd:PHA02988 184 -MVYFSYKMLndIFSEYTIKDDIYSLGVVLWEIFT-GKIPFENLTTKEIYDLiINKNNSLKLPLDCPLEIKCIVEACTSH 261
                        250
                 ....*....|.
gi 223461072 732 IPSRRPRFKDI 742
Cdd:PHA02988 262 DSIKRPNIKEI 272
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
479-693 1.36e-11

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: 66.52  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHlylpGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVC-------LLGAVTQEQPVcML 551
Cdd:cd14038    2 LGTGGFGNVLRWI----NQETGEQVAIKQCRQELSPKNRERWCLEIQIMKRLNHPNVVAardvpegLQKLAPNDLPL-LA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMNQGDLHEFLIMRSphsdvGCSSDEDGTVKSSLDhgdflhiaiQIAAGMEYLSSHFFVHKDLAARNILI--GEQLHV 629
Cdd:cd14038   77 MEYCQGGDLRKYLNQFE-----NCCGLREGAILTLLS---------DISSALRYLHENRIIHRDLKPENIVLqqGEQRLI 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223461072 630 -KISDLGLSREIysaDYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPY 693
Cdd:cd14038  143 hKIIDLGYAKEL---DQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECIT-GFRPF 203
CRD_TK_ROR_related cd07469
Cysteine-rich domain of proteins similar to tyrosine kinase-like orphan receptors; The ...
168-300 1.45e-11

Cysteine-rich domain of proteins similar to tyrosine kinase-like orphan receptors; The cysteine-rich domain (CRD) is an essential part of the tyrosine kinase-like orphan receptor (Ror) proteins, a conserved family of tyrosine kinases that function in various processes, including neuronal and skeletal development, cell polarity, and cell movement. Ror proteins are receptors of Wnt proteins, which are key players in a number of fundamental cellular processes in embryogenesis and postnatal development. In different cellular contexts, Ror proteins can either activate or repress transcription of Wnt target genes, and can modulate Wnt signaling by sequestering Wnt ligands.


Pssm-ID: 143578  Cd Length: 147  Bit Score: 63.19  E-value: 1.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 168 GFCQPYRGIACARFIGNRTV--YMESLHMQGEIENQIT-AAFTMIGTSshLSDKCSQFAIPSLCHYAFPYCDETSSVPKP 244
Cdd:cd07469    3 GYCATYRGEVCRAYLSNDALvwFNSSYADPEGLNEQLTtGLWEELIKT--VSELCRPAAEKLLCNYAFPECHPSGVGPTP 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223461072 245 RDLCRDECEVLENVLCQTEYIFARSNPMI------LMRLKLPNCEDLP-QPESPEAanCIRIG 300
Cdd:cd07469   81 KPLCREDCLAVKELFCYKDWALIEENKQRgiylksRGHFTLPECESLPsIHADPPA--CSHIP 141
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
525-706 1.55e-11

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: 67.01  E-value: 1.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 525 SLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLimrsphSDVGCSSDEDgtvkssldhgdFLHIAIQIAAGME 604
Cdd:cd05633   60 SLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNGGDLHYHL------SQHGVFSEKE-----------MRFYATEIILGLE 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 605 YLSSHFFVHKDLAARNILIGEQLHVKISDLGLsreiySADYYRVQSKSSLPIR-WMPPEAIMYGK-FSSDSDIWSFGVVL 682
Cdd:cd05633  123 HMHNRFVVYRDLKPANILLDEHGHVRISDLGL-----ACDFSKKKPHASVGTHgYMAPEVLQKGTaYDSSADWFSLGCML 197
                        170       180
                 ....*....|....*....|....
gi 223461072 683 WEIFSfGLQPYYGFSNQEVIEMVR 706
Cdd:cd05633  198 FKLLR-GHSPFRQHKTKDKHEIDR 220
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
479-693 1.90e-11

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: 65.58  E-value: 1.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKG-HLYLPGMDHAQLVAIKTLK--DYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYM 555
Cdd:cd14076    9 LGEGEFGKVKLGwPLPKANHRSGVQVAIKLIRrdTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGIVLEFV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQGDLHEFLIMRSPHSD-VGCssdedgtvkssldhgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd14076   89 SGGELFDYILARRRLKDsVAC------------------RLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDF 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223461072 635 GLSREIYSADYYRVQSKSSLPIrWMPPEAIMYGKF--SSDSDIWSFGVVLWEIFSfGLQPY 693
Cdd:cd14076  151 GFANTFDHFNGDLMSTSCGSPC-YAAPELVVSDSMyaGRKADIWSCGVILYAMLA-GYLPF 209
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
481-687 2.20e-11

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: 65.63  E-value: 2.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 481 ECTFGKIYKGHlylpgmDHAQLVAIKTLK-DYNNPQQWTE--FQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQ 557
Cdd:cd14157    3 EGTFADIYKGY------RHGKQYVIKRLKeTECESPKSTErfFQTEVQICFRCCHPNILPLLGFCVESDCHCLIYPYMPN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 558 GDLHEFLimrsphsdvGCSSDEDgtvksSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLs 637
Cdd:cd14157   77 GSLQDRL---------QQQGGSH-----PLPWEQRLSISLGLLKAVQHLHNFGILHGNIKSSNVLLDGNLLPKLGHSGL- 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 223461072 638 rEIYSAD----YYRVQSK---SSLPirWMPPEAIMYGKFSSDSDIWSFGVVLWEIFS 687
Cdd:cd14157  142 -RLCPVDkksvYTMMKTKvlqISLA--YLPEDFVRHGQLTEKVDIFSCGVVLAEILT 195
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
469-685 2.21e-11

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: 65.78  E-value: 2.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 469 PLSAVRFMEELGECTFGKIYKghlyLPGMDHAQLVAIKTLKDYNNPQQwtEFQQEASLMAEL-HHPNIVCLLGAVTQEQP 547
Cdd:cd06639   20 PSDTWDIIETIGKGTYGKVYK----VTNKKDGSLAAVKILDPISDVDE--EIEAEYNILRSLpNHPNVVKFYGMFYKADQ 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 548 VC-----MLFEYMNQGDLHEFLimrspHSDVGCSSDEDGTVKSSLDHGDFLhiaiqiaaGMEYLSSHFFVHKDLAARNIL 622
Cdd:cd06639   94 YVggqlwLVLELCNGGSVTELV-----KGLLKCGQRLDEAMISYILYGALL--------GLQHLHNNRIIHRDVKGNNIL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223461072 623 IGEQLHVKISDLGLSREIYSADYYRVQSKSSlPIrWMPPEAIMYGK---FSSDS--DIWSFGVVLWEI 685
Cdd:cd06639  161 LTTEGGVKLVDFGVSAQLTSARLRRNTSVGT-PF-WMAPEVIACEQqydYSYDArcDVWSLGITAIEL 226
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
477-709 2.34e-11

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: 65.10  E-value: 2.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMN 556
Cdd:cd14078    9 ETIGSGGFAKVKLATHILTG----EKVAIKIMDKKALGDDLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLEYCP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLImrsphsdvgcssdedgtVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGL 636
Cdd:cd14078   85 GGELFDYIV-----------------AKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGL 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223461072 637 SREIYSADYYRVQSKSSLPIrWMPPEAIMyGK--FSSDSDIWSFGVVLWEIFSfGLQPyygFSNQEVIEMVRKRQ 709
Cdd:cd14078  148 CAKPKGGMDHHLETCCGSPA-YAAPELIQ-GKpyIGSEADVWSMGVLLYALLC-GFLP---FDDDNVMALYRKIQ 216
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
479-706 2.47e-11

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: 66.12  E-value: 2.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGmdhaQLVAIKTLKD----YNNPQQWTEFQQEASLMAeLHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd05620    3 LGKGSFGKVLLAELKGKG----EYFAVKALKKdvvlIDDDVECTMVEKRVLALA-WENPFLTHLYCTFQTKEHLFFVMEF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQGDLHeFLIMRsphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd05620   78 LNGGDLM-FHIQD----------------KGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADF 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223461072 635 GLSREIYSADyYRVQSKSSLPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVIEMVR 706
Cdd:cd05620  141 GMCKENVFGD-NRASTFCGTP-DYIAPEILQGLKYTFSVDWWSFGVLLYEML-IGQSPFHGDDEDELFESIR 209
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
58-148 3.09e-11

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 60.20  E-value: 3.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  58 LTLDEPMNnITTSLGQTAELHCKVSGNPPPSIRWFKNDAPV-VQEPRrisFRATNYGSrLRIRNLDTTDTGYFQCVATNG 136
Cdd:cd20952    1 IILQGPQN-QTVAVGGTVVLNCQATGEPVPTISWLKDGVPLlGKDER---ITTLENGS-LQIKGAEKSDTGEYTCVALNL 75
                         90
                 ....*....|..
gi 223461072 137 KKVVSTTGVLFV 148
Cdd:cd20952   76 SGEATWSAVLDV 87
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
479-693 3.27e-11

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: 65.16  E-value: 3.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKI--YKGHlylpgmDHAQLVAIKTLKDYNNP-----QQWtefQQEASLMAELHHPNIVC-------LLGAVTQ 544
Cdd:cd13989    1 LGSGGFGYVtlWKHQ------DTGEYVAIKKCRQELSPsdknrERW---CLEVQIMKKLNHPNVVSardvppeLEKLSPN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 545 EQPV-CMlfEYMNQGDLHEFLimRSPHSdvgCSSDEDGTVKSSLDHgdflhiaiqIAAGMEYLSSHFFVHKDLAARNILI 623
Cdd:cd13989   72 DLPLlAM--EYCSGGDLRKVL--NQPEN---CCGLKESEVRTLLSD---------ISSAISYLHENRIIHRDLKPENIVL 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 624 ----GEQLHvKISDLGLSREIysadyyrvqSKSSL------PIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPY 693
Cdd:cd13989  136 qqggGRVIY-KLIDLGYAKEL---------DQGSLctsfvgTLQYLAPELFESKKYTCTVDYWSFGTLAFECIT-GYRPF 204
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
476-712 3.81e-11

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: 65.24  E-value: 3.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGHLYLPGmdhaQLVAIKT----LKDYNNPqqwTEFQQEASLMAELHHPNIVCLLGAV--TQEQPVC 549
Cdd:cd07837    6 LEKIGEGTYGKVYKARDKNTG----KLVALKKtrleMEEEGVP---STALREVSLLQMLSQSIYIVRLLDVehVEENGKP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 550 ML---FEYMNQgDLHEFLIM--RSPHSDVgcssdEDGTVKSsldhgdFLHiaiQIAAGMEYLSSHFFVHKDLAARNILIG 624
Cdd:cd07837   79 LLylvFEYLDT-DLKKFIDSygRGPHNPL-----PAKTIQS------FMY---QLCKGVAHCHSHGVMHRDLKPQNLLVD 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 625 EQLHV-KISDLGLSREIysadyyrvqsksSLPIR----------WMPPEAIMYG-KFSSDSDIWSFGVvlweIFSfglqp 692
Cdd:cd07837  144 KQKGLlKIADLGLGRAF------------TIPIKsytheivtlwYRAPEVLLGStHYSTPVDMWSVGC----IFA----- 202
                        250       260
                 ....*....|....*....|
gi 223461072 693 yygfsnqeviEMVRKRQLLP 712
Cdd:cd07837  203 ----------EMSRKQPLFP 212
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
479-694 4.13e-11

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: 64.74  E-value: 4.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHlylpGMDHAQLVAIKTLKDyNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTqEQPVCMLFeyMNQ- 557
Cdd:cd06624   16 LGKGTFGVVYAAR----DLSTQVRIAIKEIPE-RDSREVQPLHEEIALHSRLSHKNIVQYLGSVS-EDGFFKIF--MEQv 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 558 --GDLHEFLImrsphSDVGCSSDEDGTVKssldhgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHV-KISDL 634
Cdd:cd06624   88 pgGSLSALLR-----SKWGPLKDNENTIG---------YYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTYSGVvKISDF 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223461072 635 GLSREIYSADYYRVQSKSSLpiRWMPPEAIMYGK--FSSDSDIWSFGVVLWEIFSfGLQPYY 694
Cdd:cd06624  154 GTSKRLAGINPCTETFTGTL--QYMAPEVIDKGQrgYGPPADIWSLGCTIIEMAT-GKPPFI 212
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
530-736 4.19e-11

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: 65.06  E-value: 4.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 530 LHHPNIVCLL-------GAVTQeqpVCMLFEYMNQGDLHEFLIMrsphsdvgcssdedgtvkSSLDHGDFLHIAIQIAAG 602
Cdd:cd14220   46 MRHENILGFIaadikgtGSWTQ---LYLITDYHENGSLYDFLKC------------------TTLDTRALLKLAYSAACG 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 603 MEYLSSHFF--------VHKDLAARNILIGEQLHVKISDLGLSREiYSADYYRVQSKSSLPI---RWMPP----EAIMYG 667
Cdd:cd14220  105 LCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGTCCIADLGLAVK-FNSDTNEVDVPLNTRVgtkRYMAPevldESLNKN 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 668 KFSS--DSDIWSFGVVLWEI----FSFGL-----QPYYGF-----SNQEVIEMVRKRQLLPC------SEDCPPRMYSLM 725
Cdd:cd14220  184 HFQAyiMADIYSFGLIIWEMarrcVTGGIveeyqLPYYDMvpsdpSYEDMREVVCVKRLRPTvsnrwnSDECLRAVLKLM 263
                        250
                 ....*....|.
gi 223461072 726 TECWNEIPSRR 736
Cdd:cd14220  264 SECWAHNPASR 274
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
523-710 4.21e-11

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: 65.38  E-value: 4.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 523 EASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLhEFLIMrsphsDVGCSSDEDGTVkssldhgdfLHIAIQIAAG 602
Cdd:cd05632   52 EKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNGGDL-KFHIY-----NMGNPGFEEERA---------LFYAAEILCG 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 603 MEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSslpIRWMPPEAIMYGKFSSDSDIWSFGVVL 682
Cdd:cd05632  117 LEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGESIRGRVGT---VGYMAPEVLNNQRYTLSPDYWGLGCLI 193
                        170       180
                 ....*....|....*....|....*...
gi 223461072 683 WEIFSfGLQPYYGFSNQEVIEMVRKRQL 710
Cdd:cd05632  194 YEMIE-GQSPFRGRKEKVKREEVDRRVL 220
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
523-702 4.25e-11

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: 64.65  E-value: 4.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 523 EASLMAELHHPNIVCLLGAVT-QEQPVCMLFEYMNQGDLHEFLimrsphSDVGCSSDEDGTVkssldhgdflhIAIQIAA 601
Cdd:cd13990   54 EYEIHKSLDHPRIVKLYDVFEiDTDSFCTVLEYCDGNDLDFYL------KQHKSIPEREARS-----------IIMQVVS 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 602 GMEYLSSHF--FVHKDLAARNILIGEQLH---VKISDLGLSR----EIYSADYYRVQSKSSLPIRWMPPEAIMYG----K 668
Cdd:cd13990  117 ALKYLNEIKppIIHYDLKPGNILLHSGNVsgeIKITDFGLSKimddESYNSDGMELTSQGAGTYWYLPPECFVVGktppK 196
                        170       180       190
                 ....*....|....*....|....*....|....
gi 223461072 669 FSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVI 702
Cdd:cd13990  197 ISSKVDVWSVGVIFYQML-YGRKPFGHNQSQEAI 229
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
475-705 4.43e-11

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: 65.49  E-value: 4.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIykghLYLPGMDHAQLVAIKTLKD--YNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLF 552
Cdd:cd05593   19 YLKLLGKGTFGKV----ILVREKASGKYYAMKILKKevIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 EYMNQGDLHEFLIMRSPHSDvgcssdedgtvksslDHGDFLhiAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKIS 632
Cdd:cd05593   95 EYVNGGELFFHLSRERVFSE---------------DRTRFY--GAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKIT 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223461072 633 DLGLSREIYSaDYYRVQSKSSLPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMV 705
Cdd:cd05593  158 DFGLCKEGIT-DAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 227
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
525-706 5.00e-11

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: 65.07  E-value: 5.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 525 SLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSPHSDvgcssdedgtvkssldhGDFLHIAIQIAAGME 604
Cdd:cd14223   55 SLVSTGDCPFIVCMSYAFHTPDKLSFILDLMNGGDLHYHLSQHGVFSE-----------------AEMRFYAAEIILGLE 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 605 YLSSHFFVHKDLAARNILIGEQLHVKISDLGLsreiySADYYRVQSKSSLPIR-WMPPEAIMYG-KFSSDSDIWSFGVVL 682
Cdd:cd14223  118 HMHSRFVVYRDLKPANILLDEFGHVRISDLGL-----ACDFSKKKPHASVGTHgYMAPEVLQKGvAYDSSADWFSLGCML 192
                        170       180
                 ....*....|....*....|....
gi 223461072 683 WEIFSfGLQPYYGFSNQEVIEMVR 706
Cdd:cd14223  193 FKLLR-GHSPFRQHKTKDKHEIDR 215
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
479-693 5.86e-11

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: 64.64  E-value: 5.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHlYLPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHH----PNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd05613    8 LGTGAYGKVFLVR-KVSGHDAGKLYAMKVLKKATIVQKAKTAEHTRTERQVLEHirqsPFLVTLHYAFQTDTKLHLILDY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQGDLHEFLIMRSPHSDvgcssdedgtvkssldHGDFLHIAiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd05613   87 INGGELFTHLSQRERFTE----------------NEVQIYIG-EIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDF 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223461072 635 GLSREIYSADYYRVQSKSSlPIRWMPPEAIMYGKFSSDS--DIWSFGVVLWEIFSfGLQPY 693
Cdd:cd05613  150 GLSKEFLLDENERAYSFCG-TIEYMAPEIVRGGDSGHDKavDWWSLGVLMYELLT-GASPF 208
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
496-737 6.37e-11

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 65.81  E-value: 6.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 496 GMDHAQLVAIKTLKdYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRsphsdvgc 575
Cdd:PTZ00267  89 GSDPKEKVVAKFVM-LNDERQAAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKQR-------- 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 576 ssdedgtVKSSLDHGDFLH--IAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSS 653
Cdd:PTZ00267 160 -------LKEHLPFQEYEVglLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSLDVASSFC 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 654 LPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGlQPYYGFSNQEVIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIP 733
Cdd:PTZ00267 233 GTPYYLAPELWERKRYSKKADMWSLGVILYELLTLH-RPFKGPSQREIMQQVLYGKYDPFPCPVSSGMKALLDPLLSKNP 311

                 ....
gi 223461072 734 SRRP 737
Cdd:PTZ00267 312 ALRP 315
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
477-736 6.70e-11

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: 64.39  E-value: 6.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLylpgmdHAQLVAIKTLKDYNNPQQWTEFQQEASLMaeLHHPNIVCLL-------GAVTQeqpVC 549
Cdd:cd14143    1 ESIGKGRFGEVWRGRW------RGEDVAVKIFSSREERSWFREAEIYQTVM--LRHENILGFIaadnkdnGTWTQ---LW 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 550 MLFEYMNQGDLHEFLimrsphsdvgcssdedgtVKSSLDHGDFLHIAIQIAAGMEYLSSHF--------FVHKDLAARNI 621
Cdd:cd14143   70 LVSDYHEHGSLFDYL------------------NRYTVTVEGMIKLALSIASGLAHLHMEIvgtqgkpaIAHRDLKSKNI 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 622 LIGEQLHVKISDLGL-------SREIYSADYYRVQSKsslpiRWMPPE----AIMYGKFSS--DSDIWSFGVVLWEIF-- 686
Cdd:cd14143  132 LVKKNGTCCIADLGLavrhdsaTDTIDIAPNHRVGTK-----RYMAPEvlddTINMKHFESfkRADIYALGLVFWEIArr 206
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223461072 687 -SFGLQ------PYYGF-SNQEVIEMVRKrqlLPCSEDCPP-------------RMYSLMTECWNEIPSRR 736
Cdd:cd14143  207 cSIGGIhedyqlPYYDLvPSDPSIEEMRK---VVCEQKLRPnipnrwqscealrVMAKIMRECWYANGAAR 274
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
479-635 6.90e-11

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


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 60.92  E-value: 6.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYkghlYLPGMDHAQLVAIKTLKDYNNPQ-QWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQ 557
Cdd:cd13968    1 MGEGASAKVF----WAEGECTTIGVAVKIGDDVNNEEgEDLESEMDILRRLKGLELNIPKVLVTEDVDGPNILLMELVKG 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223461072 558 GDLHEFlimrsphsdvgcssdedgTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLG 635
Cdd:cd13968   77 GTLIAY------------------TQEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
479-687 7.34e-11

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: 64.13  E-value: 7.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGmdhaQLVAIKTL--KDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMN 556
Cdd:cd05608    9 LGKGGFGEVSACQMRATG----KLYACKKLnkKRLKKRKGYEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLImrsphsdvgcSSDEDgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGL 636
Cdd:cd05608   85 GGDLRYHIY----------NVDEE---NPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGL 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 223461072 637 SREIySADYYRVQSKSSLPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFS 687
Cdd:cd05608  152 AVEL-KDGQTKTKGYAGTP-GFMAPELLLGEEYDYSVDYFTLGVTLYEMIA 200
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
523-736 8.72e-11

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: 63.89  E-value: 8.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 523 EASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLhEFLIMRsphsdVGcssdedgtvKSSLDHGDFLHIAIQIAAG 602
Cdd:cd05630   50 EKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGGDL-KFHIYH-----MG---------QAGFPEARAVFYAAEICCG 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 603 MEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSslpIRWMPPEAIMYGKFSSDSDIWSFGVVL 682
Cdd:cd05630  115 LEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKGRVGT---VGYMAPEVVKNERYTFSPDWWALGCLL 191
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 223461072 683 WEIFSfGLQPYY----GFSNQEVIEMVRKRQlLPCSEDCPPRMYSLMTECWNEIPSRR 736
Cdd:cd05630  192 YEMIA-GQSPFQqrkkKIKREEVERLVKEVP-EEYSEKFSPQARSLCSMLLCKDPAER 247
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
475-742 9.44e-11

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: 63.60  E-value: 9.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYKghlylpgMDHAQ---LVAIKTLKDYNNPQQWTEFQQEASL-MAELHHPNIVCLLGAVTQEQPVCM 550
Cdd:cd06617    5 VIEELGRGAYGVVDK-------MRHVPtgtIMAVKRIRATVNSQEQKRLLMDLDIsMRSVDCPYTVTFYGALFREGDVWI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 551 LFEYMNQGdLHEFLimrsphsdvgcssdedgtvKSSLDHG-----DFL-HIAIQIAAGMEYLSSHFFV-HKDLAARNILI 623
Cdd:cd06617   78 CMEVMDTS-LDKFY-------------------KKVYDKGltipeDILgKIAVSIVKALEYLHSKLSViHRDVKPSNVLI 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 624 GEQLHVKISDLGLSREIYSaDYYRVQSKSSLPirWMPPEAI---MYGK-FSSDSDIWSFGVVLWEIfSFGLQPYYGFSN- 698
Cdd:cd06617  138 NRNGQVKLCDFGISGYLVD-SVAKTIDAGCKP--YMAPERInpeLNQKgYDVKSDVWSLGITMIEL-ATGRFPYDSWKTp 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 223461072 699 -QEVIEMVrkrqllpcsEDCPPRM----YSL-----MTECWNEIPSRRPRFKDI 742
Cdd:cd06617  214 fQQLKQVV---------EEPSPQLpaekFSPefqdfVNKCLKKNYKERPNYPEL 258
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
475-709 1.05e-10

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


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 63.12  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYkghlyLPGMDHAQ-LVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFE 553
Cdd:cd14167    7 FREVLGTGAFSEVV-----LAEEKRTQkLVAIKCIAKKALEGKETSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 554 YMNQGDLHEFLIMRsphsdvGCSSDEDGTvkssldhgdflHIAIQIAAGMEYLSSHFFVHKDLAARNIL---IGEQLHVK 630
Cdd:cd14167   82 LVSGGELFDRIVEK------GFYTERDAS-----------KLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIM 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223461072 631 ISDLGLSREIYSADyyrVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWeIFSFGLQPYYGFSNQEVIEMVRKRQ 709
Cdd:cd14167  145 ISDFGLSKIEGSGS---VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDAKLFEQILKAE 219
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
484-707 1.43e-10

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: 62.67  E-value: 1.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 484 FGKIYKGHLYLPGMDHAQLV-AIKTLKDYNNPQQWTEFQ--QEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDL 560
Cdd:cd14116   13 LGKGKFGNVYLAREKQSKFIlALKVLFKAQLEKAGVEHQlrREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 561 HEFLimrsphsdVGCSSDEDGTVKSSLdhgdflhiaIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREI 640
Cdd:cd14116   93 YREL--------QKLSKFDEQRTATYI---------TELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHA 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223461072 641 YSAdyyrvqSKSSL--PIRWMPPEAIMYGKFSSDSDIWSFGVVLWEiFSFGLQPYYGFSNQEVIEMVRK 707
Cdd:cd14116  156 PSS------RRTTLcgTLDYLPPEMIEGRMHDEKVDLWSLGVLCYE-FLVGKPPFEANTYQETYKRISR 217
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
523-693 1.49e-10

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: 63.09  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 523 EASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLhEFLIMrsphsDVGcssdedgtvKSSLDHGDFLHIAIQIAAG 602
Cdd:cd05631   50 EKRILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGDL-KFHIY-----NMG---------NPGFDEQRAIFYAAELCCG 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 603 MEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSslpIRWMPPEAIMYGKFSSDSDIWSFGVVL 682
Cdd:cd05631  115 LEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPEGETVRGRVGT---VGYMAPEVINNEKYTFSPDWWGLGCLI 191
                        170
                 ....*....|.
gi 223461072 683 WEIFSfGLQPY 693
Cdd:cd05631  192 YEMIQ-GQSPF 201
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
66-135 1.65e-10

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 58.40  E-value: 1.65e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223461072  66 NITTSLGQTAELHCKVSGNPPPSIRWFKNDAPVVQEPRRISFratNY-GSRLRIRNLDTTDTGYFQCVATN 135
Cdd:cd05730   12 NATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEEKYSF---NEdGSEMTILDVDKLDEAEYTCIAEN 79
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
60-136 2.17e-10

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 57.84  E-value: 2.17e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223461072  60 LDEPmNNITTSLGQTAELHCKVSGNPPPSIRWFKNDAPVvqEPRRISFRATNYGSRLRIRNLDTTDTGYFQCVATNG 136
Cdd:cd04978    3 IIEP-PSLVLSPGETGELICEAEGNPQPTITWRLNGVPI--EPAPEDMRRTVDGRTLIFSNLQPNDTAVYQCNASNV 76
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
479-703 2.22e-10

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: 63.00  E-value: 2.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKI----YKGHlylpgmdhAQLVAIKTLKDynnpQQWTEFQQEASLMAE-------LHHPNIVCLLGAVTQEQP 547
Cdd:cd05570    3 LGKGSFGKVmlaeRKKT--------DELYAIKVLKK----EVIIEDDDVECTMTEkrvlalaNRHPFLTGLHACFQTEDR 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 548 VCMLFEYMNQGDLHeFLIMRSPhsdvgcssdedgtvKSSLDHGDFLhiAIQIAAGMEYLSSHFFVHKDLAARNILIGEQL 627
Cdd:cd05570   71 LYFVMEYVNGGDLM-FHIQRAR--------------RFTEERARFY--AAEICLALQFLHERGIIYRDLKLDNVLLDAEG 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 628 HVKISDLGLSRE-IYSA----------DYyrvqsksslpirwMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGF 696
Cdd:cd05570  134 HIKIADFGMCKEgIWGGnttstfcgtpDY-------------IAPEILREQDYGFSVDWWALGVLLYEMLA-GQSPFEGD 199

                 ....*..
gi 223461072 697 SNQEVIE 703
Cdd:cd05570  200 DEDELFE 206
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
475-707 2.27e-10

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: 62.70  E-value: 2.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQwTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd14166    7 FMEVLGSGAFSEVYLVKQRSTG----KLYALKCIKKSPLSRD-SSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQGDLHEFLIMRsphsdvGCSSDEDGTVkssldhgdflhIAIQIAAGMEYLSSHFFVHKDLAARNILI---GEQLHVKI 631
Cdd:cd14166   82 VSGGELFDRILER------GVYTEKDASR-----------VINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMI 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223461072 632 SDLGLSReiysADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRK 707
Cdd:cd14166  145 TDFGLSK----MEQNGIMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLC-GYPPFYEETESRLFEKIKE 215
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
474-701 2.81e-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: 62.70  E-value: 2.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 474 RFMEELGECTFGKI----YK--GHLYlpgmdhaqlvAIKTLKdynnpQQWTEFQQEA-SLMAE---------LHHPNIVC 537
Cdd:cd05589    2 RCIAVLGRGHFGKVllaeYKptGELF----------AIKALK-----KGDIIARDEVeSLMCEkrifetvnsARHPFLVN 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 538 LLGAVTQEQPVCMLFEYMNQGDLhefliMRSPHSDVgcsSDEDGTVkssldhgdflHIAIQIAAGMEYLSSHFFVHKDLA 617
Cdd:cd05589   67 LFACFQTPEHVCFVMEYAAGGDL-----MMHIHEDV---FSEPRAV----------FYAACVVLGLQFLHEHKIVYRDLK 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 618 ARNILIGEQLHVKISDLGLSRE-IYSADyyRVQSKSSLPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGF 696
Cdd:cd05589  129 LDNLLLDTEGYVKIADFGLCKEgMGFGD--RTSTFCGTP-EFLAPEVLTDTSYTRAVDWWGLGVLIYEML-VGESPFPGD 204

                 ....*
gi 223461072 697 SNQEV 701
Cdd:cd05589  205 DEEEV 209
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
475-705 2.85e-10

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: 62.71  E-value: 2.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYKGHLylPGMDhaQLVAIKTLKD----YNNPQQWTefQQEASLMAELHHPNIVCLLGAVTQEQP-VC 549
Cdd:cd05616    4 FLMVLGKGSFGKVMLAER--KGTD--ELYAVKILKKdvviQDDDVECT--MVEKRVLALSGKPPFLTQLHSCFQTMDrLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 550 MLFEYMNQGDL----HEFLIMRSPHSdvgcssdedgtvkssldhgdfLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGE 625
Cdd:cd05616   78 FVMEYVNGGDLmyhiQQVGRFKEPHA---------------------VFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDS 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 626 QLHVKISDLGLSREiYSADYYRVQSKSSLPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMV 705
Cdd:cd05616  137 EGHIKIADFGMCKE-NIWDGVTTKTFCGTP-DYIAPEIIAYQPYGKSVDWWAFGVLLYEMLA-GQAPFEGEDEDELFQSI 213
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
479-741 3.36e-10

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: 62.67  E-value: 3.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIykghLYLPGMDHAQLVAIKTLKD---YNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYM 555
Cdd:cd05604    4 IGKGSFGKV----LLAKRKRDGKYYAVKVLQKkviLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQGDLHeFLIMRsphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLG 635
Cdd:cd05604   80 NGGELF-FHLQR----------------ERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFG 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 636 LSREIYSadyyrvQSKSSLPI----RWMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVIEMVRKRQLL 711
Cdd:cd05604  143 LCKEGIS------NSDTTTTFcgtpEYLAPEVIRKQPYDNTVDWWCLGSVLYEML-YGLPPFYCRDTAEMYENILHKPLV 215
                        250       260       270
                 ....*....|....*....|....*....|
gi 223461072 712 pCSEDCPPRMYSLMTECWNEIPSRRPRFKD 741
Cdd:cd05604  216 -LRPGISLTAWSILEELLEKDRQLRLGAKE 244
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
523-710 3.61e-10

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 61.84  E-value: 3.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 523 EASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLhEFLIMrsphsDVGcssdedgtvKSSLDHGDFLHIAIQIAAG 602
Cdd:cd05607   52 EKEILEKVNSPFIVSLAYAFETKTHLCLVMSLMNGGDL-KYHIY-----NVG---------ERGIEMERVIFYSAQITCG 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 603 MEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSreiysadyyrVQSKSSLPIR-------WMPPEAIMYGKFSSDSDI 675
Cdd:cd05607  117 ILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLA----------VEVKEGKPITqragtngYMAPEILKEESYSYPVDW 186
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 223461072 676 WSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRKRQL 710
Cdd:cd05607  187 FAMGCSIYEMVA-GRTPFRDHKEKVSKEELKRRTL 220
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
521-742 3.77e-10

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: 61.68  E-value: 3.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 521 QQEASLMAELHHPNIVCLLGAVTQEQpvCMLFEYMN---QGDLHEFLIMRSphsdvGCSSDEDGTVKssldhgdflhIAI 597
Cdd:cd08223   47 EQEAKLLSKLKHPNIVSYKESFEGED--GFLYIVMGfceGGDLYTRLKEQK-----GVLLEERQVVE----------WFV 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 598 QIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSAD----------YYrvqsksslpirwMPPEAIMYG 667
Cdd:cd08223  110 QIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSdmattligtpYY------------MSPELFSNK 177
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223461072 668 KFSSDSDIWSFGVVLWEIFSFGlqpyYGFSNQEVIEMVRK---RQLLPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd08223  178 PYNHKSDVWALGCCVYEMATLK----HAFNAKDMNSLVYKileGKLPPMPKQYSPELGELIKAMLHQDPEKRPSVKRI 251
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
476-712 4.14e-10

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 61.76  E-value: 4.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLK----DYNNPQQWTefqQEASLMAELHHPNIVCLLGAVTQEQPVCML 551
Cdd:PLN00009   7 VEKIGEGTYGVVYKARDRVTN----ETIALKKIRleqeDEGVPSTAI---REISLLKEMQHGNIVRLQDVVHSEKRLYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMNQgDLHEFLimrsphsdvgcssdeDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLH-VK 630
Cdd:PLN00009  80 FEYLDL-DLKKHM---------------DSSPDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNaLK 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 631 ISDLGLSREIysadyyrvqsksSLPIR---------WMPPEAIMYGK--FSSDSDIWSFGVvlweIFSfglqpyygfsnq 699
Cdd:PLN00009 144 LADFGLARAF------------GIPVRtfthevvtlWYRAPEILLGSrhYSTPVDIWSVGC----IFA------------ 195
                        250
                 ....*....|...
gi 223461072 700 eviEMVRKRQLLP 712
Cdd:PLN00009 196 ---EMVNQKPLFP 205
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
522-690 5.12e-10

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 62.15  E-value: 5.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 522 QEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLheflimrsphsdvgcssdeDGTvksSLDHGDFL-HIAIQIA 600
Cdd:PLN00034 121 REIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSL-------------------EGT---HIADEQFLaDVARQIL 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 601 AGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIysADYYRVQSKSSLPIRWMPPEAI-------MYGKFSsdS 673
Cdd:PLN00034 179 SGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRIL--AQTMDPCNSSVGTIAYMSPERIntdlnhgAYDGYA--G 254
                        170       180
                 ....*....|....*....|.
gi 223461072 674 DIWSFGVVLWEI----FSFGL 690
Cdd:PLN00034 255 DIWSLGVSILEFylgrFPFGV 275
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
62-148 5.94e-10

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 56.81  E-value: 5.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  62 EPMNNITTSLGQTAELHCKVSGNPPPSIRWFKNDAPVVqEPRRISF-RATNYGSRLRIRNLDTTDTGYFQCVATNGKKVV 140
Cdd:cd20973    2 QTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIV-ESRRFQIdQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                 ....*...
gi 223461072 141 STTGVLFV 148
Cdd:cd20973   81 TCSAELTV 88
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
479-693 7.57e-10

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: 61.09  E-value: 7.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYkghLYlPGMDHAQLVAIKTLK---DYNNPQQWTefqQEASLMAELHHPNIVcllgaVTQEQPVCMLF--- 552
Cdd:cd14039    1 LGTGGFGNVC---LY-QNQETGEKIAIKSCRlelSVKNKDRWC---HEIQIMKKLNHPNVV-----KACDVPEEMNFlvn 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 -------EYMNQGDLHEFLimRSPHSDVGcssdedgtvkssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILI-- 623
Cdd:cd14039   69 dvpllamEYCSGGDLRKLL--NKPENCCG------------LKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLqe 134
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223461072 624 --GEQLHvKISDLGLSREIysaDYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEI------FSFGLQPY 693
Cdd:cd14039  135 inGKIVH-KIIDLGYAKDL---DQGSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECiagfrpFLHNLQPF 208
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
473-736 7.63e-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: 61.22  E-value: 7.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 473 VRFMEELGECTFGKIYKGHLylpgmdHAQLVAIKTLKDYNNPQQWTEFQQEASLMaeLHHPNIVCLL-------GAVTQe 545
Cdd:cd14219    7 IQMVKQIGKGRYGEVWMGKW------RGEKVAVKVFFTTEEASWFRETEIYQTVL--MRHENILGFIaadikgtGSWTQ- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 546 qpVCMLFEYMNQGDLHEFLimrsphsdvgcssdedgtVKSSLDHGDFLHIAIQIAAGMEYLSSHFF--------VHKDLA 617
Cdd:cd14219   78 --LYLITDYHENGSLYDYL------------------KSTTLDTKAMLKLAYSSVSGLCHLHTEIFstqgkpaiAHRDLK 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 618 ARNILIGEQLHVKISDLGL-------SREIYSADYYRVQSKsslpiRWMPPE----AIMYGKFSS--DSDIWSFGVVLWE 684
Cdd:cd14219  138 SKNILVKKNGTCCIADLGLavkfisdTNEVDIPPNTRVGTK-----RYMPPEvldeSLNRNHFQSyiMADMYSFGLILWE 212
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223461072 685 I----FSFGL-----QPYYGF-----SNQEVIEMVRKRQLLPC------SEDCPPRMYSLMTECWNEIPSRR 736
Cdd:cd14219  213 VarrcVSGGIveeyqLPYHDLvpsdpSYEDMREIVCIKRLRPSfpnrwsSDECLRQMGKLMTECWAHNPASR 284
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
477-737 7.74e-10

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: 60.90  E-value: 7.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLYLPGMDHA-QLVAIKTL--KDYNnpqqwtEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFE 553
Cdd:cd14086    7 EELGKGAFSVVRRCVQKSTGQEFAaKIINTKKLsaRDHQ------KLEREARICRLLKHPNIVRLHDSISEEGFHYLVFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 554 YMNQGDLHEFLIMRSPHSDVGCSsdedgtvkssldhgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLH---VK 630
Cdd:cd14086   81 LVTGGELFEDIVAREFYSEADAS-----------------HCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKgaaVK 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 631 ISDLGLSREIySADYYRVQSKSSLPIrWMPPEAIMYGKFSSDSDIWSFGVVLWeIFSFGLQPYYGFSNQEViemvrKRQL 710
Cdd:cd14086  144 LADFGLAIEV-QGDQQAWFGFAGTPG-YLSPEVLRKDPYGKPVDIWACGVILY-ILLVGYPPFWDEDQHRL-----YAQI 215
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 223461072 711 LPCSEDCPPRMYSLMT-ECWNEI-------PSRRP 737
Cdd:cd14086  216 KAGAYDYPSPEWDTVTpEAKDLInqmltvnPAKRI 250
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
533-719 7.98e-10

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: 60.88  E-value: 7.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 533 PNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLimrsphsdvgcssDEDGTVKSSLDHgdfLHIAIQIAAgMEYLSSHFFV 612
Cdd:cd05609   60 PFVVSMYCSFETKRHLCMVMEYVEGGDCATLL-------------KNIGPLPVDMAR---MYFAETVLA-LEYLHSYGIV 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 613 HKDLAARNILIGEQLHVKISDLGLSR--------EIYSA----DYYRVQSKS--SLPiRWMPPEAIMYGKFSSDSDIWSF 678
Cdd:cd05609  123 HRDLKPDNLLITSMGHIKLTDFGLSKiglmslttNLYEGhiekDTREFLDKQvcGTP-EYIAPEVILRQGYGKPVDWWAM 201
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 223461072 679 GVVLWEiFSFGLQPYYGFSNQEVIEMVRKRQLL-PCSEDCPP 719
Cdd:cd05609  202 GIILYE-FLVGCVPFFGDTPEELFGQVISDEIEwPEGDDALP 242
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
501-712 8.05e-10

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: 61.61  E-value: 8.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 501 QLVAIKTL-KDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQP------VCMLFEYMnQGDLHEflIMRsphsdv 573
Cdd:cd07855   31 QKVAIKKIpNAFDVVTTAKRTLRELKILRHFKHDNIIAIRDILRPKVPyadfkdVYVVLDLM-ESDLHH--IIH------ 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 574 gcsSDEDGTvkssLDHGD-FLHiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSAD----YYRV 648
Cdd:cd07855  102 ---SDQPLT----LEHIRyFLY---QLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPeehkYFMT 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223461072 649 QSKSSLPIRwmPPEAIM-YGKFSSDSDIWSFGVvlweIFSfglqpyygfsnqeviEMVRKRQLLP 712
Cdd:cd07855  172 EYVATRWYR--APELMLsLPEYTQAIDMWSVGC----IFA---------------EMLGRRQLFP 215
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
476-687 9.42e-10

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: 60.85  E-value: 9.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGHlylpGMDHAQLVAIKT-LKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd07847    6 LSKIGEGSYGVVFKCR----NRETGQIVAIKKfVESEDDPVIKKIALREIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQGDLHEflIMRSPHsdvGCssDEDGTVKssldhgdflhIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd07847   82 CDHTVLNE--LEKNPR---GV--PEHLIKK----------IIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDF 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223461072 635 GLSR-----EIYSADYyrvqskssLPIRWM-PPEAIM----YGkfsSDSDIWSFGVVLWEIFS 687
Cdd:cd07847  145 GFARiltgpGDDYTDY--------VATRWYrAPELLVgdtqYG---PPVDVWAIGCVFAELLT 196
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
477-683 1.00e-09

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


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 60.12  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLYLPGMDhaqlVAIKTL-KDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYM 555
Cdd:cd14082    9 EVLGSGQFGIVYGGKHRKTGRD----VAIKVIdKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NqGDLHEfLIMRSPHSDVgcssDEDGTvkssldhgDFLhiAIQIAAGMEYLSSHFFVHKDLAARNILI---GEQLHVKIS 632
Cdd:cd14082   85 H-GDMLE-MILSSEKGRL----PERIT--------KFL--VTQILVALRYLHSKNIVHCDLKPENVLLasaEPFPQVKLC 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 223461072 633 DLGLSREIYSADYYRvqSKSSLPIrWMPPEAIMYGKFSSDSDIWSFGVVLW 683
Cdd:cd14082  149 DFGFARIIGEKSFRR--SVVGTPA-YLAPEVLRNKGYNRSLDMWSVGVIIY 196
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
72-148 1.09e-09

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 55.93  E-value: 1.09e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223461072  72 GQTAELHCKVSGNPPPSIRWFKNDAPVVQEPRRISFRATNYGS-RLRIRNLDTTDTGYFQCVATNGKKVVSTTGVLFV 148
Cdd:cd05892   15 GDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNCGRiCLLIQNANKKDAGWYTVSAVNEAGVVSCNARLDV 92
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
484-710 1.11e-09

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: 61.05  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 484 FGKIYKGHlylpGMDHAQLVAIKTLK--DYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLH 561
Cdd:cd05610   17 FGKVYLGR----KKNNSKLYAVKVVKkaDMINKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVK 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 562 EFLIMRSphsdvgcSSDEDGTVKssldhgdflHIAiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLS---- 637
Cdd:cd05610   93 SLLHIYG-------YFDEEMAVK---------YIS-EVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSkvtl 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 638 -REI-------------YSADYYRVQSK-----SSL------PIR----------------------WMPPEAIMYGKFS 670
Cdd:cd05610  156 nRELnmmdilttpsmakPKNDYSRTPGQvlsliSSLgfntptPYRtpksvrrgaarvegerilgtpdYLAPELLLGKPHG 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 223461072 671 SDSDIWSFGVVLWEiFSFGLQPYYGFSNQEVIEMVRKRQL 710
Cdd:cd05610  236 PAVDWWALGVCLFE-FLTGIPPFNDETPQQVFQNILNRDI 274
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
469-730 1.13e-09

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: 60.41  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 469 PLSAVRFMEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQwtEFQQEASLMAELH-HPNIVCLLGA-----V 542
Cdd:cd06638   16 PSDTWEIIETIGKGTYGKVFKVLNKKNG----SKAAVKILDPIHDIDE--EIEAEYNILKALSdHPNVVKFYGMyykkdV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 543 TQEQPVCMLFEYMNQGDLHEFlimrsphsdvgcssdedgtVKSSLDHGD---------FLHIAIQiaaGMEYLSSHFFVH 613
Cdd:cd06638   90 KNGDQLWLVLELCNGGSVTDL-------------------VKGFLKRGErmeepiiayILHEALM---GLQHLHVNKTIH 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 614 KDLAARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSSlPIrWMPPEAI-----MYGKFSSDSDIWSFGVVLWEIfsf 688
Cdd:cd06638  148 RDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRRNTSVGT-PF-WMAPEVIaceqqLDSTYDARCDVWSLGITAIEL--- 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 223461072 689 glqpyyGFSNQEVIEMVRKRQLLPCSEDCPPRMYSlmTECWN 730
Cdd:cd06638  223 ------GDGDPPLADLHPMRALFKIPRNPPPTLHQ--PELWS 256
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
72-148 1.15e-09

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 55.96  E-value: 1.15e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223461072  72 GQTAELHCKVSGNPPPSIRWFKNDAPvVQEPRRISFRATNYGSR-LRIRNLDTTDTGYFQCVATNGKKVVSTTGVLFV 148
Cdd:cd05744   15 GRLCRFDCKVSGLPTPDLFWQLNGKP-VRPDSAHKMLVRENGRHsLIIEPVTKRDAGIYTCIARNRAGENSFNAELVV 91
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
500-724 1.34e-09

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: 60.42  E-value: 1.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 500 AQLVAIKTLkDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLheflimrsphsdvgcssdE 579
Cdd:cd06657   45 GKLVAVKKM-DLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL------------------T 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 580 DGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIySADYYRVQSKSSLPIrWM 659
Cdd:cd06657  106 DIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV-SKEVPRRKSLVGTPY-WM 183
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223461072 660 PPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRkrqllpcsEDCPPRMYSL 724
Cdd:cd06657  184 APELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYFNEPPLKAMKMIR--------DNLPPKLKNL 239
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
71-149 1.36e-09

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 55.73  E-value: 1.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  71 LGQTAELHCKVSGNPPPSIRWFKNDAPVVQE-PRRISFRATnyGSRLRIRNLDTTDTGYFQCVATNGKKVVSTTGVLFVK 149
Cdd:cd05736   14 PGVEASLRCHAEGIPLPRVQWLKNGMDINPKlSKQLTLIAN--GSELHISNVRYEDTGAYTCIAKNEGGVDEDISSLFVE 91
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
523-742 1.56e-09

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: 59.64  E-value: 1.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 523 EASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSPHSDVgcssdedgtvkssldhgDFLHIAIQIAAG 602
Cdd:cd13995   46 DVEIQACFRHENIAELYGALLWEETVHLFMEAGEGGSVLEKLESCGPMREF-----------------EIIWVTKHVLKG 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 603 MEYLSSHFFVHKDLAARNILIGEQLHVKIsDLGLSREIySADYYRVQSKSSLPIrWMPPEAIMYGKFSSDSDIWSFGVVL 682
Cdd:cd13995  109 LDFLHSKNIIHHDIKPSNIVFMSTKAVLV-DFGLSVQM-TEDVYVPKDLRGTEI-YMSPEVILCRGHNTKADIYSLGATI 185
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223461072 683 WEIFSfGLQPY---YGFSNQEVIEMVRKRQLLP---CSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd13995  186 IHMQT-GSPPWvrrYPRSAYPSYLYIIHKQAPPledIAQDCSPAMRELLEAALERNPNHRSSAAEL 250
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
514-687 1.91e-09

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: 59.55  E-value: 1.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 514 PQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSPHSDVgcssdedgTVKssldhgDFL 593
Cdd:cd14110   40 PEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPELLYNLAERNSYSEA--------EVT------DYL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 594 HiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGlSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDS 673
Cdd:cd14110  106 W---QILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLG-NAQPFNQGKVLMTDKKGDYVETMAPELLEGQGAGPQT 181
                        170
                 ....*....|....
gi 223461072 674 DIWSFGVVLWEIFS 687
Cdd:cd14110  182 DIWAIGVTAFIMLS 195
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
524-700 2.16e-09

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: 59.55  E-value: 2.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 524 ASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFlimrsphsdvgCSSDEDGTVKssldHGDFLHIAIQIAAGM 603
Cdd:cd14198   59 AVLELAKSNPRVVNLHEVYETTSEIILILEYAAGGEIFNL-----------CVPDLAEMVS----ENDIIRLIRQILEGV 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 604 EYLSSHFFVHKDLAARNIL---IGEQLHVKISDLGLSREIYSADYYRVQSKSSlpiRWMPPEAIMYGKFSSDSDIWSFGV 680
Cdd:cd14198  124 YYLHQNNIVHLDLKPQNILlssIYPLGDIKIVDFGMSRKIGHACELREIMGTP---EYLAPEILNYDPITTATDMWNIGV 200
                        170       180
                 ....*....|....*....|
gi 223461072 681 VLWEIFSfGLQPYYGFSNQE 700
Cdd:cd14198  201 IAYMLLT-HESPFVGEDNQE 219
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
503-724 2.73e-09

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: 59.28  E-value: 2.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 503 VAIKTLkDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLheflimrsphsdvgcssdEDGT 582
Cdd:cd06658   50 VAVKKM-DLRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGAL------------------TDIV 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 583 VKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIySADYYRVQSKSSLPIrWMPPE 662
Cdd:cd06658  111 THTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQV-SKEVPKRKSLVGTPY-WMAPE 188
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223461072 663 AIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYgfsNQEVIEMVRKrqllpCSEDCPPRMYSL 724
Cdd:cd06658  189 VISRLPYGTEVDIWSLGIMVIEMID-GEPPYF---NEPPLQAMRR-----IRDNLPPRVKDS 241
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
479-712 2.90e-09

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: 59.66  E-value: 2.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKghLYLPGMDhaQLVAIKTLKdyNNPQQWTEFQQEASLMAELHHPN-----IVCLLGAVTQEQPVCMLFE 553
Cdd:cd14229    8 LGRGTFGQVVK--CWKRGTN--EIVAVKILK--NHPSYARQGQIEVGILARLSNENadefnFVRAYECFQHRNHTCLVFE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 554 YMNQgDLHEFLIMRSphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNIL----IGEQLHV 629
Cdd:cd14229   82 MLEQ-NLYDFLKQNK---------------FSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMlvdpVRQPYRV 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 630 KISDLG----LSREIYS----ADYYRVqsksslpirwmpPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEV 701
Cdd:cd14229  146 KVIDFGsashVSKTVCStylqSRYYRA------------PEIILGLPFCEAIDMWSLGCVIAELF-LGWPLYPGALEYDQ 212
                        250
                 ....*....|.
gi 223461072 702 IEMVRKRQLLP 712
Cdd:cd14229  213 IRYISQTQGLP 223
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
503-739 3.00e-09

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


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 59.72  E-value: 3.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 503 VAIKTL-KDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTqeqPVCMLFEYMNQgdlheFLIMRSPHSDVgCSsdedg 581
Cdd:cd07874   45 VAIKKLsRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFT---PQKSLEEFQDV-----YLVMELMDANL-CQ----- 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 582 TVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSReiySADYYRVQSKSSLPIRWMPP 661
Cdd:cd07874  111 VIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR---TAGTSFMMTPYVVTRYYRAP 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 662 EAIMYGKFSSDSDIWSFGVVLWEIFSFG-LQPYYGFSNQ--EVIEMVrkrqllpcSEDCPPRMYSLMTECWNEIPSrRPR 738
Cdd:cd07874  188 EVILGMGYKENVDIWSVGCIMGEMVRHKiLFPGRDYIDQwnKVIEQL--------GTPCPEFMKKLQPTVRNYVEN-RPK 258

                 .
gi 223461072 739 F 739
Cdd:cd07874  259 Y 259
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
523-711 3.02e-09

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: 58.94  E-value: 3.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 523 EASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLImrsphsdvgcssdedGTVKSSLDHGDFlhIAIQIAAG 602
Cdd:cd14084   61 EIEILKKLSHPCIIKIEDFFDAEDDYYIVLELMEGGELFDRVV---------------SNKRLKEAICKL--YFYQMLLA 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 603 MEYLSSHFFVHKDLAARNILIG---EQLHVKISDLGLSREIYSADYYRVQSKSSLpirWMPPEAIMYG---KFSSDSDIW 676
Cdd:cd14084  124 VKYLHSNGIIHRDLKPENVLLSsqeEECLIKITDFGLSKILGETSLMKTLCGTPT---YLAPEVLRSFgteGYTRAVDCW 200
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 223461072 677 SFGVVLWEIFSfGLQPYygfsNQEVIEMVRKRQLL 711
Cdd:cd14084  201 SLGVILFICLS-GYPPF----SEEYTQMSLKEQIL 230
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
479-721 3.23e-09

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: 59.55  E-value: 3.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIY---------KGHLY-LPGMDHAQLVA-IKTLKDYNNPQQWTEFQQEASLMAELHHpnivcllgAVTQEQP 547
Cdd:cd05614    8 LGTGAYGKVFlvrkvsghdANKLYaMKVLRKAALVQkAKTVEHTRTERNVLEHVRQSPFLVTLHY--------AFQTDAK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 548 VCMLFEYMNQGDLHEFLIMRsphsdvgcssdedgtvksslDHgdFLHIAIQIAAG-----MEYLSSHFFVHKDLAARNIL 622
Cdd:cd05614   80 LHLILDYVSGGELFTHLYQR--------------------DH--FSEDEVRFYSGeiilaLEHLHKLGIVYRDIKLENIL 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 623 IGEQLHVKISDLGLSREIYSADYYRVQSKSSlPIRWMPPEAIM----YGKFssdSDIWSFGVVLWEIFSfGLQPYYGFSN 698
Cdd:cd05614  138 LDSEGHVVLTDFGLSKEFLTEEKERTYSFCG-TIEYMAPEIIRgksgHGKA---VDWWSLGILMFELLT-GASPFTLEGE 212
                        250       260
                 ....*....|....*....|...
gi 223461072 699 QEVIEMVRKRqLLPCSEDCPPRM 721
Cdd:cd05614  213 KNTQSEVSRR-ILKCDPPFPSFI 234
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
523-717 3.75e-09

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: 59.17  E-value: 3.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 523 EASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRsPHsdvGCSSDEDgtVKssldhgdFLhiAIQIAAG 602
Cdd:cd05574   51 EREILATLDHPFLPTLYASFQTSTHLCFVMDYCPGGELFRLLQKQ-PG---KRLPEEV--AR-------FY--AAEVLLA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 603 MEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSSLPIRWMP---------------------- 660
Cdd:cd05574  116 LEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKQSSVTPPPVRKSLRKGSRRSSVksieketfvaepsarsnsfvgt 195
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223461072 661 -----PEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVIEMVRKRQLL-----PCSEDC 717
Cdd:cd05574  196 eeyiaPEVIKGDGHGSAVDWWTLGILLYEML-YGTTPFKGSNRDETFSNILKKELTfpespPVSSEA 261
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
469-701 3.79e-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: 58.68  E-value: 3.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 469 PLSAVRFMEELGECTFGKIYKghlyLPGMDHAQLVAIKTLKdyNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPV 548
Cdd:cd14111    1 PQKPYTFLDEKARGRFGVIRR----CRENATGKNFPAKIVP--YQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 549 CMLFEYMNQGDLHEFLIMRSPHSdvgcssdEDgtvkssldhgDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLH 628
Cdd:cd14111   75 VLIAEFCSGKELLHSLIDRFRYS-------ED----------DVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNA 137
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223461072 629 VKISDLGlSREIYSADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEV 701
Cdd:cd14111  138 IKIVDFG-SAQSFNPLSLRQLGRRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLS-GRSPFEDQDPQET 208
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
513-694 3.85e-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: 58.83  E-value: 3.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 513 NPQQWTEFQQeaSLMAELH-------HPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLimrsphsdvgcssdedgTVKS 585
Cdd:cd14181   51 SPEQLEEVRS--STLKEIHilrqvsgHPSIITLIDSYESSTFIFLVFDLMRRGELFDYL-----------------TEKV 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 586 SLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSSlpiRWMPPEAIM 665
Cdd:cd14181  112 TLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHLEPGEKLRELCGTP---GYLAPEILK 188
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 223461072 666 ---------YGKfssDSDIWSFGVVLWEIFSfGLQPYY 694
Cdd:cd14181  189 csmdethpgYGK---EVDLWACGVILFTLLA-GSPPFW 222
IgI_1_Neogenin_like cd05722
First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of ...
60-148 4.03e-09

First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409387  Cd Length: 97  Bit Score: 54.79  E-value: 4.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  60 LDEPMNnITTSLGQTAELHCKVSGNPPPSIRWFKNDAPV--VQEPRRISFraTNyGSRLrIRNL-----DTTDTGYFQCV 132
Cdd:cd05722    5 LSEPSD-IVAMRGGPVVLNCSAESDPPPKIEWKKDGVLLnlVSDERRQQL--PN-GSLL-ITSVvhskhNKPDEGFYQCV 79
                         90
                 ....*....|....*...
gi 223461072 133 ATNGK--KVVSTTGVLFV 148
Cdd:cd05722   80 AQNESlgSIVSRTARVTV 97
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
503-637 4.27e-09

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: 58.50  E-value: 4.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 503 VAIKTLkDYNNPQQWTE--FQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLimrsphsdvgcssded 580
Cdd:cd14075   30 VAIKIL-DKTKLDQKTQrlLSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEYASGGELYTKI---------------- 92
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 223461072 581 gTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLS 637
Cdd:cd14075   93 -STEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFS 148
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
479-710 4.27e-09

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


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 58.72  E-value: 4.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLylpgMDHAQLVAIKTLKDYNNPQQWTEFQ--QEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMN 556
Cdd:cd14117   14 LGKGKFGNVYLARE----KQSKFIVALKVLFKSQIEKEGVEHQlrREIEIQSHLRHPNILRLYNYFHDRKRIYLILEYAP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLimrsphsDVGCSSDEDGTVKssldhgdflhIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGL 636
Cdd:cd14117   90 RGELYKEL-------QKHGRFDEQRTAT----------FMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGW 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223461072 637 SreIYSADYYRVQSKSSLPirWMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVIEMVRKRQL 710
Cdd:cd14117  153 S--VHAPSLRRRTMCGTLD--YLPPEMIEGRTHDEKVDLWCIGVLCYELL-VGMPPFESASHTETYRRIVKVDL 221
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
479-712 4.72e-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: 4.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIY---KGHlylpGMDHAQLVAIKTLKD---YNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLF 552
Cdd:cd05584    4 LGKGGYGKVFqvrKTT----GSDKGKIFAMKVLKKasiVRNQKDTAHTKAERNILEAVKHPFIVDLHYAFQTGGKLYLIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 EYMNQGDL-----HEFLIMRsphsDVGCssdedgtvkssldhgdfLHIAiQIAAGMEYLSSHFFVHKDLAARNILIGEQL 627
Cdd:cd05584   80 EYLSGGELfmhleREGIFME----DTAC-----------------FYLA-EITLALGHLHSLGIIYRDLKPENILLDAQG 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 628 HVKISDLGLSREIYSADyyRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRK 707
Cdd:cd05584  138 HVKLTDFGLCKESIHDG--TVTHTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLT-GAPPFTAENRKKTIDKILK 214

                 ....*.
gi 223461072 708 RQL-LP 712
Cdd:cd05584  215 GKLnLP 220
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
475-742 4.93e-09

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: 58.09  E-value: 4.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYKghlyLPGMDHAQLVAIKTLKD-YNNPQQWTEFQQEASLMAELH-HPNIVCLLGAVTQEQPVCMLF 552
Cdd:cd14050    5 ILSKLGEGSFGEVFK----VRSREDGKLYAVKRSRSrFRGEKDRKRKLEEVERHEKLGeHPNCVRFIKAWEEKGILYIQT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 EYMnQGDLHEFLimrsphsdVGCSSDEDGTVkssldhgdfLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKIS 632
Cdd:cd14050   81 ELC-DTSLQQYC--------EETHSLPESEV---------WNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLG 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 633 DLGLSREIYSADYYRVQSKSSlpiRWMPPEaIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEviemVRKRQL-L 711
Cdd:cd14050  143 DFGLVVELDKEDIHDAQEGDP---RYMAPE-LLQGSFTKAADIFSLGITILELACNLELPSGGDGWHQ----LRQGYLpE 214
                        250       260       270
                 ....*....|....*....|....*....|.
gi 223461072 712 PCSEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14050  215 EFTAGLSPELRSIIKLMMDPDPERRPTAEDL 245
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
501-712 5.03e-09

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: 58.96  E-value: 5.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 501 QLVAIKTL-KDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQE------QPVCMLFEYMNqGDLHEFLIMrsphsdv 573
Cdd:cd07850   26 QNVAIKKLsRPFQNVTHAKRAYRELVLMKLVNHKNIIGLLNVFTPQksleefQDVYLVMELMD-ANLCQVIQM------- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 574 gcssdedgtvksSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSA---------D 644
Cdd:cd07850   98 ------------DLDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSfmmtpyvvtR 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223461072 645 YYRVqsksslpirwmpPEAIMYGKFSSDSDIWSFGVVlweifsFGlqpyygfsnqeviEMVRKRQLLP 712
Cdd:cd07850  166 YYRA------------PEVILGMGYKENVDIWSVGCI------MG-------------EMIRGTVLFP 202
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
531-695 5.12e-09

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: 58.94  E-value: 5.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 531 HHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHeFLIMRSPhsdvgcssdedgtvKSSLDHGDFLhiAIQIAAGMEYLSSHF 610
Cdd:cd05592   54 QHPFLTHLFCTFQTESHLFFVMEYLNGGDLM-FHIQQSG--------------RFDEDRARFY--GAEIICGLQFLHSRG 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 611 FVHKDLAARNILIGEQLHVKISDLGLSREiysaDYYRVQSKSSL---PiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFs 687
Cdd:cd05592  117 IIYRDLKLDNVLLDREGHIKIADFGMCKE----NIYGENKASTFcgtP-DYIAPEILKGQKYNQSVDWWSFGVLLYEML- 190

                 ....*...
gi 223461072 688 FGLQPYYG 695
Cdd:cd05592  191 IGQSPFHG 198
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
575-737 5.60e-09

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: 58.05  E-value: 5.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 575 CSSDEDGTVKSSLDHGDFLHIAI-------QIAAGMEYLSSHFFVHKDLAARNILI-----GEQLHVKISDLGLSREIYS 642
Cdd:cd13982   77 CAASLQDLVESPRESKLFLRPGLepvrllrQIASGLAHLHSLNIVHRDLKPQNILIstpnaHGNVRAMISDFGLCKKLDV 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 643 ADY-YRVQSKSSLPIRWMPPEAIMYGKFSSDS---DIWSFGVVLWEIFSFGLQPYYG-FSNQEVIemVRKRQLLPCSED- 716
Cdd:cd13982  157 GRSsFSRRSGVAGTSGWIAPEMLSGSTKRRQTravDIFSLGCVFYYVLSGGSHPFGDkLEREANI--LKGKYSLDKLLSl 234
                        170       180
                 ....*....|....*....|...
gi 223461072 717 --CPPRMYSLMTECWNEIPSRRP 737
Cdd:cd13982  235 geHGPEAQDLIERMIDFDPEKRP 257
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
479-707 6.01e-09

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: 58.18  E-value: 6.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIY-------KGHLYLPGMDHAQLVAIKTLKDYNNpqqwtefqqEASLMAELHHPNIVCLLGAVTQEQPVCML 551
Cdd:cd14209    9 LGTGSFGRVMlvrhketGNYYAMKILDKQKVVKLKQVEHTLN---------EKRILQAINFPFLVKLEYSFKDNSNLYMV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMNQGDlhefliMRSPHSDVGcssdedgtvKSSLDHGDFLhiAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKI 631
Cdd:cd14209   80 MEYVPGGE------MFSHLRRIG---------RFSEPHARFY--AAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKV 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 632 SDLGLSReiysadyyRVQSKSS----LPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEiFSFGLQPyygFSNQEVIEMVRK 707
Cdd:cd14209  143 TDFGFAK--------RVKGRTWtlcgTP-EYLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPP---FFADQPIQIYEK 209
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
63-135 6.79e-09

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 53.73  E-value: 6.79e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223461072  63 PMNNITTSLGQTAELHCKVSGNPPPSIRWFKNDAPVVQEPRRISFratNYGSrLRIRNLDT-TDTGYFQCVATN 135
Cdd:cd20958    6 PMGNLTAVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNHRQRVF---PNGT-LVIENVQRsSDEGEYTCTARN 75
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
501-686 7.85e-09

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


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 58.34  E-value: 7.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 501 QLVAIKTLKD-YNNPQ--QWTeFQqEASLMAEL-HHPNIVCLLGAVTQE--QPVCMLFEYMnQGDLHEfLIMRSPHSDVg 574
Cdd:cd07852   33 EVVALKKIFDaFRNATdaQRT-FR-EIMFLQELnDHPNIIKLLNVIRAEndKDIYLVFEYM-ETDLHA-VIRANILEDI- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 575 cssdedgtvkssldHGDFlhIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSADYYrvqskSSL 654
Cdd:cd07852  108 --------------HKQY--IMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARSLSQLEED-----DEN 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 223461072 655 PI-------RWM-PPEaIMYG--KFSSDSDIWSFGVVLWEIF 686
Cdd:cd07852  167 PVltdyvatRWYrAPE-ILLGstRYTKGVDMWSVGCILGEML 207
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
479-687 8.00e-09

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: 57.78  E-value: 8.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHlylpGMDHAQLVAIKTLK-DYNNPQQWTE---FQQEASLMAELHHPNIVCLLGAVTQ--EQPVCMLF 552
Cdd:cd06651   15 LGQGAFGRVYLCY----DVDTGRELAAKQVQfDPESPETSKEvsaLECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 EYMNQGDLHEFLimrsphsdvgcssDEDGTVKSSLDHgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKIS 632
Cdd:cd06651   91 EYMPGGSVKDQL-------------KAYGALTESVTR----KYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLG 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 223461072 633 DLGLSREIYS--ADYYRVQSKSSLPIrWMPPEAIMYGKFSSDSDIWSFGVVLWEIFS 687
Cdd:cd06651  154 DFGASKRLQTicMSGTGIRSVTGTPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLT 209
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
505-694 8.53e-09

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: 57.75  E-value: 8.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 505 IKTLKDYNNPQQWTEFQQEAslMAELH-------HPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLimrsphsdvgcss 577
Cdd:cd14093   36 IDITGEKSSENEAEELREAT--RREIEilrqvsgHPNIIELHDVFESPTFIFLVFELCRKGELFDYL------------- 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 578 dedgTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSADYYRvqSKSSLPiR 657
Cdd:cd14093  101 ----TEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDEGEKLR--ELCGTP-G 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 223461072 658 WMPPEAI---MYGKFSSDS---DIWSFGVVLWEIFSfGLQPYY 694
Cdd:cd14093  174 YLAPEVLkcsMYDNAPGYGkevDMWACGVIMYTLLA-GCPPFW 215
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
472-686 8.89e-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: 57.94  E-value: 8.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 472 AVRF--MEELGECTFGKIYKGHlylpgmDH--AQLVAIKTLKdynNPQQWTefQQ---EASLMAEL------HHPNIVCL 538
Cdd:cd14210   12 AYRYevLSVLGKGSFGQVVKCL------DHktGQLVAIKIIR---NKKRFH--QQalvEVKILKHLndndpdDKHNIVRY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 539 LGAVTQEQPVCMLFEYMNQgDLHEFLIMRSPHsdvGCSSDedgTVKSsldhgdflhIAIQIAAGMEYLSSHFFVHKDLAA 618
Cdd:cd14210   81 KDSFIFRGHLCIVFELLSI-NLYELLKSNNFQ---GLSLS---LIRK---------FAKQILQALQFLHKLNIIHCDLKP 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223461072 619 RNILIGEQLH--VKISDLGLS----REIYS---ADYYRVqsksslpirwmpPEAIMYGKFSSDSDIWSFGVVLWEIF 686
Cdd:cd14210  145 ENILLKQPSKssIKVIDFGSScfegEKVYTyiqSRFYRA------------PEVILGLPYDTAIDMWSLGCILAELY 209
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
501-685 9.29e-09

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: 57.97  E-value: 9.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 501 QLVAIKTL-KDYNNPQQWTEFQQEASLMAELHHPNIVCLLGA-VTQEQPVCMLFEYMNQgDLHEFLIMRSPhsdvgcssd 578
Cdd:cd07856   36 QNVAVKKImKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIfISPLEDIYFVTELLGT-DLHRLLTSRPL--------- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 579 EDGTVKSsldhgdFLHiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSR-------EIYSADYYRVqsk 651
Cdd:cd07856  106 EKQFIQY------FLY---QILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARiqdpqmtGYVSTRYYRA--- 173
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 223461072 652 sslpirwmpPEAIM-YGKFSSDSDIWSFGVVLWEI 685
Cdd:cd07856  174 ---------PEIMLtWQKYDVEVDIWSAGCIFAEM 199
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
70-135 9.51e-09

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 53.37  E-value: 9.51e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223461072  70 SLGQTAELHCKVSGNPPPSIRWFKNDAPVVQEpRRISFRAtnygSRLRIRNLDTTDTGYFQCVATN 135
Cdd:cd05728   12 DIGSSLRWECKASGNPRPAYRWLKNGQPLASE-NRIEVEA----GDLRITKLSLSDSGMYQCVAEN 72
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
519-700 9.96e-09

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: 57.36  E-value: 9.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 519 EFQQE-ASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLimrsphsdvgcssDEDGtvksSLDHGDFLHIAI 597
Cdd:cd14106   53 EILHEiAVLELCKDCPRVVNLHEVYETRSELILILELAAGGELQTLL-------------DEEE----CLTEADVRRLMR 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 598 QIAAGMEYLSSHFFVHKDLAARNILI-GEQLH--VKISDLGLSREIysadyyrvqsKSSLPIR-------WMPPEAIMYG 667
Cdd:cd14106  116 QILEGVQYLHERNIVHLDLKPQNILLtSEFPLgdIKLCDFGISRVI----------GEGEEIReilgtpdYVAPEILSYE 185
                        170       180       190
                 ....*....|....*....|....*....|...
gi 223461072 668 KFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQE 700
Cdd:cd14106  186 PISLATDMWSIGVLTYVLLT-GHSPFGGDDKQE 217
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
72-149 1.06e-08

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 53.19  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  72 GQTAELHCKVSGNPPPSIRWFKNDAPV--VQEPRRISFRATNYGSRLRIRNLDTTDTGYFQCVATNGKKVVSTTGVLFVK 149
Cdd:cd20951   15 KSDAKLRVEVQGKPDPEVKWYKNGVPIdpSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEASSSASVVVE 94
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
503-715 1.08e-08

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: 58.13  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 503 VAIKTL-KDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPvcmLFEYMNQgdlheFLIMRSPHSDVgCSsdedg 581
Cdd:cd07875   52 VAIKKLsRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKS---LEEFQDV-----YIVMELMDANL-CQ----- 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 582 TVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSReiySADYYRVQSKSSLPIRWMPP 661
Cdd:cd07875  118 VIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR---TAGTSFMMTPYVVTRYYRAP 194
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 223461072 662 EAIMYGKFSSDSDIWSFGVVLWEIFSFG-LQPYYGFSNQ--EVIEMVRKrqllPCSE 715
Cdd:cd07875  195 EVILGMGYKENVDIWSVGCIMGEMIKGGvLFPGTDHIDQwnKVIEQLGT----PCPE 247
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
504-685 1.08e-08

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: 57.43  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 504 AIKTLK-DYNNPQQWTEFQQEASLMAELH---HPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLimrsphSDVGcssde 579
Cdd:cd14052   30 AVKKLKpNYAGAKDRLRRLEEVSILRELTldgHDNIVQLIDSWEYHGHLYIQTELCENGSLDVFL------SELG----- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 580 dgtVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSreiysadyyrvqskSSLPI--- 656
Cdd:cd14052   99 ---LLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMA--------------TVWPLirg 161
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 223461072 657 -------RWMPPEAIMYGKFSSDSDIWSFGVVLWEI 685
Cdd:cd14052  162 ieregdrEYIAPEILSEHMYDKPADIFSLGLILLEA 197
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
521-707 1.11e-08

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: 57.21  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 521 QQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLimrsphsdvgcsSDEDgtvkSSLDHGDFLHIAIQIA 600
Cdd:cd14114   47 RKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLSGGELFERI------------AAEH----YKMSEAEVINYMRQVC 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 601 AGMEYLSSHFFVHKDLAARNILIGEQ--LHVKISDLGLSREIYSADYYRVQSKSSlpiRWMPPEAIMYGKFSSDSDIWSF 678
Cdd:cd14114  111 EGLCHMHENNIVHLDIKPENIMCTTKrsNEVKLIDFGLATHLDPKESVKVTTGTA---EFAAPEIVEREPVGFYTDMWAV 187
                        170       180
                 ....*....|....*....|....*....
gi 223461072 679 GVVLWEIFSfGLQPYYGFSNQEVIEMVRK 707
Cdd:cd14114  188 GVLSYVLLS-GLSPFAGENDDETLRNVKS 215
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
443-705 1.17e-08

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: 58.12  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 443 PKPVRG-QNVEMSMLnayKPKSKakeLPLSAVRFMEELGECTFGKIY------KGHLYLPGMDHAQLVAIKtlkdynnpQ 515
Cdd:cd05594    2 PSDNSGaEEMEVSLT---KPKHK---VTMNDFEYLKLLGKGTFGKVIlvkekaTGRYYAMKILKKEVIVAK--------D 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 516 QWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSPHSDvgcssdedgtvksslDHGDFLhi 595
Cdd:cd05594   68 EVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSE---------------DRARFY-- 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 596 AIQIAAGMEYL-SSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSaDYYRVQSKSSLPiRWMPPEAIMYGKFSSDSD 674
Cdd:cd05594  131 GAEIVSALDYLhSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIK-DGATMKTFCGTP-EYLAPEVLEDNDYGRAVD 208
                        250       260       270
                 ....*....|....*....|....*....|.
gi 223461072 675 IWSFGVVLWEIFSfGLQPYYGFSNQEVIEMV 705
Cdd:cd05594  209 WWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 238
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
519-752 1.23e-08

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


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 57.55  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 519 EFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHeFLIMRspHSDVGCSSDEdgTVKSsldhgdflHIAIQ 598
Cdd:cd14094   51 DLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLC-FEIVK--RADAGFVYSE--AVAS--------HYMRQ 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 599 IAAGMEYLSSHFFVHKDLAARNILIGEQLH---VKISDLGLSR---EIYSADYYRVQSKsslpiRWMPPEAIMYGKFSSD 672
Cdd:cd14094  118 ILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIqlgESGLVAGGRVGTP-----HFMAPEVVKREPYGKP 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 673 SDIWSFGVVLWEIFSfGLQPYYGfSNQEVIEMVRKRQLlpcseDCPPRMYSLMTECWNEIpSRRPRFKDIHVRLRSWEGL 752
Cdd:cd14094  193 VDVWGCGVILFILLS-GCLPFYG-TKERLFEGIIKGKY-----KMNPRQWSHISESAKDL-VRRMLMLDPAERITVYEAL 264
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
522-685 1.26e-08

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: 57.76  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 522 QEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIM--RSPHSDVGcssdedgtvkssldhgdflHIAIQI 599
Cdd:cd06650   52 RELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKagRIPEQILG-------------------KVSIAV 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 600 AAGMEYL-SSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSAdyyrvQSKSSLPIR-WMPPEAIMYGKFSSDSDIWS 677
Cdd:cd06650  113 IKGLTYLrEKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDS-----MANSFVGTRsYMSPERLQGTHYSVQSDIWS 187

                 ....*...
gi 223461072 678 FGVVLWEI 685
Cdd:cd06650  188 MGLSLVEM 195
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
63-135 1.30e-08

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 53.01  E-value: 1.30e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223461072  63 PMNNITTSLGQTAELHCKVSGNPPPSIRWFKNDApVVQEPRRISFRATnyGSrLRIRNLDTTDTGYFQCVATN 135
Cdd:cd20968    5 PPTNVTIIEGLKAVLPCTTMGNPKPSVSWIKGDD-LIKENNRIAVLES--GS-LRIHNVQKEDAGQYRCVAKN 73
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
501-685 1.33e-08

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: 57.87  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 501 QLVAIKTLKD-YNNPQQWTEFQQEASLMAELHHPNIV----CLLGAVTQE-QPVCMLFEYMnQGDLHEFLimrsphsdvg 574
Cdd:cd07859   26 EKVAIKKINDvFEHVSDATRILREIKLLRLLRHPDIVeikhIMLPPSRREfKDIYVVFELM-ESDLHQVI---------- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 575 cSSDEDGTVKSsldHGDFLHiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSR--------EIYSADYy 646
Cdd:cd07859   95 -KANDDLTPEH---HQFFLY---QLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARvafndtptAIFWTDY- 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 223461072 647 rvqskssLPIRWM-PPE--AIMYGKFSSDSDIWSFGVVLWEI 685
Cdd:cd07859  167 -------VATRWYrAPElcGSFFSKYTPAIDIWSIGCIFAEV 201
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
503-685 1.36e-08

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: 57.73  E-value: 1.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 503 VAIKTL-KDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTqeqPVCMLFEYMNQgdlheFLIMRSPHSDVgCSsdedg 581
Cdd:cd07876   49 VAVKKLsRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFT---PQKSLEEFQDV-----YLVMELMDANL-CQ----- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 582 TVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSReiySADYYRVQSKSSLPIRWMPP 661
Cdd:cd07876  115 VIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR---TACTNFMMTPYVVTRYYRAP 191
                        170       180
                 ....*....|....*....|....
gi 223461072 662 EAIMYGKFSSDSDIWSFGVVLWEI 685
Cdd:cd07876  192 EVILGMGYKENVDIWSVGCIMGEL 215
IgI_2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; ...
73-135 1.39e-08

Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR. LAR belongs to the RPTP type IIa subfamily. Members of this subfamily are cell adhesion molecule-like proteins involved in central nervous system (CNS) development. They have large extracellular portions comprised of multiple Ig-like domains and two to nine fibronectin type III (FNIII) domains and a cytoplasmic portion having two tandem phosphatase domains.


Pssm-ID: 409400 [Multi-domain]  Cd Length: 91  Bit Score: 53.09  E-value: 1.39e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223461072  73 QTAELHCKVSGNPPPSIRWFKNDAPVVQEPRRISFRATNYGSrLRIRNLDTTDTGYFQCVATN 135
Cdd:cd05738   15 RTATMLCAASGNPDPEISWFKDFLPVDTATSNGRIKQLRSGA-LQIENSEESDQGKYECVATN 76
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
479-704 1.43e-08

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: 57.67  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGmdhaQLVAIKTLKD---YNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYM 555
Cdd:cd05603    3 IGKGSFGKVLLAKRKCDG----KFYAVKVLQKktiLKKKEQNHIMAERNVLLKNLKHPFLVGLHYSFQTSEKLYFVLDYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQGDLheFLIMRSPHsdvgCSSDEDGTVkssldhgdflhIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLG 635
Cdd:cd05603   79 NGGEL--FFHLQRER----CFLEPRARF-----------YAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFG 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223461072 636 LSREiySADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYgfsNQEVIEM 704
Cdd:cd05603  142 LCKE--GMEPEETTSTFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEML-YGLPPFY---SRDVSQM 204
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
532-694 1.45e-08

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: 57.41  E-value: 1.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 532 HPNIVCL--LGAVTQEQ-PVCMLFEYMNQGDLHEflIMRS--PHSDVGCSSdedgtvkssldhgdFLHiaiQIAAGMEYL 606
Cdd:cd07857   61 HKNITCLydMDIVFPGNfNELYLYEELMEADLHQ--IIRSgqPLTDAHFQS--------------FIY---QILCGLKYI 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 607 SSHFFVHKDLAARNILIGEQLHVKISDLGLSREiYSADYYRVQSKSS--LPIRWMPPEAIM--YGKFSSDSDIWSFGVVL 682
Cdd:cd07857  122 HSANVLHRDLKPGNLLVNADCELKICDFGLARG-FSENPGENAGFMTeyVATRWYRAPEIMlsFQSYTKAIDVWSVGCIL 200
                        170
                 ....*....|..
gi 223461072 683 WEIfsFGLQPYY 694
Cdd:cd07857  201 AEL--LGRKPVF 210
pknD PRK13184
serine/threonine-protein kinase PknD;
503-720 1.61e-08

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 58.63  E-value: 1.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 503 VAIKTLKD--YNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFL-------IMRSPHSDv 573
Cdd:PRK13184  30 VALKKIREdlSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYTMPYIEGYTLKSLLksvwqkeSLSKELAE- 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 574 gcssdedgtvKSSLdhGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSR-------EIYSADYY 646
Cdd:PRK13184 109 ----------KTSV--GAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAIfkkleeeDLLDIDVD 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 647 RVQSKSS---LP------IRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLqPYygfSNQEVIEMVRKRQLLPCSEDC 717
Cdd:PRK13184 177 ERNICYSsmtIPgkivgtPDYMAPERLLGVPASESTDIYALGVILYQMLTLSF-PY---RRKKGRKISYRDVILSPIEVA 252

                 ...
gi 223461072 718 PPR 720
Cdd:PRK13184 253 PYR 255
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
503-684 1.83e-08

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: 57.30  E-value: 1.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 503 VAIKTLkdyNNPQQWTEFQQ----EASLMAELHHPNIVCLLGAVTQEQP------VCMLFEYMNQgDLHEflIMRSPhsd 572
Cdd:cd07851   43 VAIKKL---SRPFQSAIHAKrtyrELRLLKHMKHENVIGLLDVFTPASSledfqdVYLVTHLMGA-DLNN--IVKCQ--- 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 573 vgcssdedgtvKSSLDHGDFLhiAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYS--ADYyrVQS 650
Cdd:cd07851  114 -----------KLSDDHIQFL--VYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHTDDemTGY--VAT 178
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 223461072 651 ksslpiRW-MPPEaIMY--GKFSSDSDIWSFGVVLWE 684
Cdd:cd07851  179 ------RWyRAPE-IMLnwMHYNQTVDIWSVGCIMAE 208
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
67-135 1.84e-08

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 52.59  E-value: 1.84e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  67 ITTSLGQTAELHCKVSGNPPPSIRWFKNDAPVVQEPR-RISFRATNYGSrLRIRNLDTTDTGYFQCVATN 135
Cdd:cd05737   11 VTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHcNLKVEAGRTVY-FTINGVSSEDSGKYGLVVKN 79
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
522-681 2.02e-08

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: 56.44  E-value: 2.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 522 QEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSphsdvgcsSDEDGTVKssldhgdfLHIAiQIAA 601
Cdd:cd14107   47 QERDILARLSHRRLTCLLDQFETRKTLILILELCSSEELLDRLFLKG--------VVTEAEVK--------LYIQ-QVLE 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 602 GMEYLSSHFFVHKDLAARNILI--GEQLHVKISDLGLSREIYSAdyyRVQ-SKSSLPiRWMPPEAIMYGKFSSDSDIWSF 678
Cdd:cd14107  110 GIGYLHGMNILHLDIKPDNILMvsPTREDIKICDFGFAQEITPS---EHQfSKYGSP-EFVAPEIVHQEPVSAATDIWAL 185

                 ...
gi 223461072 679 GVV 681
Cdd:cd14107  186 GVI 188
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
479-693 2.10e-08

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: 56.25  E-value: 2.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIY---KghlyLPGMDHAQLVAIKTLKDYNNPQQ-------WTEFQqeaSLMAELHHPNIVCLLGAVTQEQPV 548
Cdd:cd05583    2 LGTGAYGKVFlvrK----VGGHDAGKLYAMKVLKKATIVQKaktaehtMTERQ---VLEAVRQSPFLVTLHYAFQTDAKL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 549 CMLFEYMNQGDLHEFLIMRSPHsdvgcssDEDGtVKssldhgdfLHIAiQIAAGMEYLSSHFFVHKDLAARNILIGEQLH 628
Cdd:cd05583   75 HLILDYVNGGELFTHLYQREHF-------TESE-VR--------IYIG-EIVLALEHLHKLGIIYRDIKLENILLDSEGH 137
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223461072 629 VKISDLGLSREIYSADYYRVQSKSSlPIRWMPPEAIMYGKFSSDS--DIWSFGVVLWEIFSfGLQPY 693
Cdd:cd05583  138 VVLTDFGLSKEFLPGENDRAYSFCG-TIEYMAPEVVRGGSDGHDKavDWWSLGVLTYELLT-GASPF 202
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
498-705 2.17e-08

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: 56.94  E-value: 2.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 498 DHAQLVAIKTL--KDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRsphsdvgc 575
Cdd:cd05598   24 DTNALYAMKTLrkKDVLKRNQVAHVKAERDILAEADNEWVVKLYYSFQDKENLYFVMDYIPGGDLMSLLIKK-------- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 576 ssdedGTVKSSLDHgdfLHIAiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLS---REIYSADYYRVQSKS 652
Cdd:cd05598   96 -----GIFEEDLAR---FYIA-ELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfRWTHDSKYYLAHSLV 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 223461072 653 SLPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVIEMV 705
Cdd:cd05598  167 GTP-NYIAPEVLLRTGYTQLCDWWSVGVILYEML-VGQPPFLAQTPAETQLKV 217
IgI_1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; ...
61-151 2.30e-08

First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; The members here are composed of the first immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409356 [Multi-domain]  Cd Length: 96  Bit Score: 52.63  E-value: 2.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  61 DEPMNNI--TTSLGQTAELHCKVSGNPPPSIRWFKNDAPVVQEPrriSFRATNYGSRLRIRNLD-TTDTGYFQCVATNGK 137
Cdd:cd04967    6 EQPDDTIfpEDSDEKKVALNCRARANPVPSYRWLMNGTEIDLES---DYRYSLVDGTLVISNPSkAKDAGHYQCLATNTV 82
                         90
                 ....*....|....*
gi 223461072 138 -KVVSTTGVLfvKFG 151
Cdd:cd04967   83 gSVLSREATL--QFG 95
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
72-135 2.41e-08

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 52.22  E-value: 2.41e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223461072  72 GQTAELHCKVSGNPPPSIRWFKNDAPVVQEPRRISFRATNYGSRLRIRNLDTTDTGYFQCVATN 135
Cdd:cd05729   19 ANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGWSLIIERAIPRDKGKYTCIVEN 82
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
522-737 2.65e-08

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: 56.68  E-value: 2.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 522 QEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFL--IMRSPHSDVGcssdedgtvkssldhgdflHIAIQI 599
Cdd:cd06615   48 RELKVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLkkAGRIPENILG-------------------KISIAV 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 600 AAGMEYL-SSHFFVHKDLAARNILIGEQLHVKISDLGLSRE-IYSADYYRVQSKSslpirWMPPEAIMYGKFSSDSDIWS 677
Cdd:cd06615  109 LRGLTYLrEKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQlIDSMANSFVGTRS-----YMSPERLQGTHYTVQSDIWS 183
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223461072 678 FGVVLWEIF----------SFGLQPYYGFSNQEVIEMVRKRQLLPCSEDCPPRM--YSLMTECWNEIPSRRP 737
Cdd:cd06615  184 LGLSLVEMAigrypipppdAKELEAMFGRPVSEGEAKESHRPVSGHPPDSPRPMaiFELLDYIVNEPPPKLP 255
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
476-712 2.85e-08

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 57.02  E-value: 2.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKghLYLPGMDhaQLVAIKTLKdyNNPQQWTEFQQEASLMAELHHP-----NIVCLLGAVTQEQPVCM 550
Cdd:cd14227   20 LEFLGRGTFGQVVK--CWKRGTN--EIVAIKILK--NHPSYARQGQIEVSILARLSTEsaddyNFVRAYECFQHKNHTCL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 551 LFEYMNQgDLHEFLIMRSphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILI----GEQ 626
Cdd:cd14227   94 VFEMLEQ-NLYDFLKQNK---------------FSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvdpsRQP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 627 LHVKISDLGLSREIYSAdyyrVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVIEMVR 706
Cdd:cd14227  158 YRVKVIDFGSASHVSKA----VCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELF-LGWPLYPGASEYDQIRYIS 232

                 ....*.
gi 223461072 707 KRQLLP 712
Cdd:cd14227  233 QTQGLP 238
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
596-710 2.94e-08

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: 56.56  E-value: 2.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 596 AIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREiySADYYRVQSKSSLPIRWMPPEAIMYGKFSSDSDI 675
Cdd:cd05602  114 AAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKE--NIEPNGTTSTFCGTPEYLAPEVLHKQPYDRTVDW 191
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 223461072 676 WSFGVVLWEIFsFGLQPYYGFSNQEVIEMVRKRQL 710
Cdd:cd05602  192 WCLGAVLYEML-YGLPPFYSRNTAEMYDNILNKPL 225
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
598-716 3.07e-08

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


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 56.10  E-value: 3.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 598 QIAAGMEYLSSHFFVHKDLAARNILIGEQL---HVKISDLGLSREIYSADYYRVQSKSSlpiRWMPPEAIMYGKFSSDSD 674
Cdd:cd14197  119 QILEGVSFLHNNNVVHLDLKPQNILLTSESplgDIKIVDFGLSRILKNSEELREIMGTP---EYVAPEILSYEPISTATD 195
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 223461072 675 IWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRKRQLLPCSED 716
Cdd:cd14197  196 MWSIGVLAYVMLT-GISPFLGDDKQETFLNISQMNVSYSEEE 236
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
479-702 3.10e-08

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: 56.35  E-value: 3.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLgAVTQEQPV---CMLFEYM 555
Cdd:cd13988    1 LGQGATANVFRGRHKKTG----DLYAVKVFNNLSFMRPLDVQMREFEVLKKLNHKNIVKLF-AIEEELTTrhkVLVMELC 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQGDLheFLIMRSPHSDVGCSSDEdgtvkssldhgdFLHIAIQIAAGMEYLSSHFFVHKDLAARNIL--IGE--QLHVKI 631
Cdd:cd13988   76 PCGSL--YTVLEEPSNAYGLPESE------------FLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEdgQSVYKL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 632 SDLGLSREIYSADYYrvqskSSL--PIRWMPPEaiMY----------GKFSSDSDIWSFGVVLWEIFSfGLQPYYGFS-- 697
Cdd:cd13988  142 TDFGAARELEDDEQF-----VSLygTEEYLHPD--MYeravlrkdhqKKYGATVDLWSIGVTFYHAAT-GSLPFRPFEgp 213

                 ....*..
gi 223461072 698 --NQEVI 702
Cdd:cd13988  214 rrNKEVM 220
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
470-705 3.30e-08

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: 56.54  E-value: 3.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 470 LSAVRFMEELGECTFGKIYKGHLylPGMDhaQLVAIKTLKD----YNNPQQWTefQQEASLMAELHHPNIVCLLGAVTQE 545
Cdd:cd05615    9 LTDFNFLMVLGKGSFGKVMLAER--KGSD--ELYAIKILKKdvviQDDDVECT--MVEKRVLALQDKPPFLTQLHSCFQT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 546 -QPVCMLFEYMNQGDLHEFLimrsphSDVGcssdedgtvksSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIG 624
Cdd:cd05615   83 vDRLYFVMEYVNGGDLMYHI------QQVG-----------KFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLD 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 625 EQLHVKISDLGLSREiYSADYYRVQSKSSLPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEM 704
Cdd:cd05615  146 SEGHIKIADFGMCKE-HMVEGVTTRTFCGTP-DYIAPEIIAYQPYGRSVDWWAYGVLLYEMLA-GQPPFDGEDEDELFQS 222

                 .
gi 223461072 705 V 705
Cdd:cd05615  223 I 223
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
68-141 4.47e-08

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 51.79  E-value: 4.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  68 TTSLGQTAELHCKVSGNPPPSIRWFKNDAPVVQEPRrisFRATNYGSR-------LRIRNLDTTDTGYFQCVATNGKKVV 140
Cdd:cd20956   12 TLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPR---FRVGDYVTSdgdvvsyVNISSVRVEDGGEYTCTATNDVGSV 88

                 .
gi 223461072 141 S 141
Cdd:cd20956   89 S 89
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
59-136 4.87e-08

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 51.35  E-value: 4.87e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223461072  59 TLDEPMNNITTSLGQTAELHCKVSGNPPPSIRWFKNDAPVVQEPRRISFRATnyGSRLRIRNLDTTDTGYFQCVATNG 136
Cdd:cd20970    4 STPQPSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVREN--GTTLTIRNIRRSDMGIYLCIASNG 79
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
63-148 4.99e-08

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 51.47  E-value: 4.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  63 PMNnITTSLGQTAELHCKVSGNPPPSIRWFKN---DAPVVQEpRRISFRATNygSRLRIRNLDTTDTGYFQCVATNGKKV 139
Cdd:cd05763    6 PHD-ITIRAGSTARLECAATGHPTPQIAWQKDggtDFPAARE-RRMHVMPED--DVFFIVDVKIEDTGVYSCTAQNSAGS 81

                 ....*....
gi 223461072 140 VSTTGVLFV 148
Cdd:cd05763   82 ISANATLTV 90
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
522-742 5.09e-08

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: 55.11  E-value: 5.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 522 QEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFlIMRspHsdvGCSSDEDgTVKssldhgdflHIAIQIAA 601
Cdd:cd14074   51 QEVRCMKLVQHPNVVRLYEVIDTQTKLYLILELGDGGDMYDY-IMK--H---ENGLNED-LAR---------KYFRQIVS 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 602 GMEYLSSHFFVHKDLAARNILIGEQLH-VKISDLGLSREiYSADYYRVQSKSSLPirWMPPEaIMYGKfSSDS---DIWS 677
Cdd:cd14074  115 AISYCHKLHVVHRDLKPENVVFFEKQGlVKLTDFGFSNK-FQPGEKLETSCGSLA--YSAPE-ILLGD-EYDApavDIWS 189
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223461072 678 FGVVLWEIFSfGLQPYYGFSNQEVIEMVrkrqlLPCSEDCPPRmysLMTECWNEI-------PSRRPRFKDI 742
Cdd:cd14074  190 LGVILYMLVC-GQPPFQEANDSETLTMI-----MDCKYTVPAH---VSPECKDLIrrmlirdPKKRASLEEI 252
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
479-715 5.93e-08

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: 55.45  E-value: 5.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKG-HLYLPGMDHAQLVAI-KTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPV-CMLFEYM 555
Cdd:cd14040   14 LGRGGFSEVYKAfDLYEQRYAAVKIHQLnKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTfCTVLEYC 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQGDLHEFLIMRSPHSDVGCSSdedgtvkssldhgdflhIAIQIAAGMEYLSS--HFFVHKDLAARNILIGEQL---HVK 630
Cdd:cd14040   94 EGNDLDFYLKQHKLMSEKEARS-----------------IVMQIVNALRYLNEikPPIIHYDLKPGNILLVDGTacgEIK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 631 ISDLGLSR----EIYSADYYRVQSKSSLPIRWMPPEAIMYGK----FSSDSDIWSFGVVLWEIFsFGLQPYYgfSNQEVI 702
Cdd:cd14040  157 ITDFGLSKimddDSYGVDGMDLTSQGAGTYWYLPPECFVVGKeppkISNKVDVWSVGVIFFQCL-YGRKPFG--HNQSQQ 233
                        250
                 ....*....|...
gi 223461072 703 EMVRKRQLLPCSE 715
Cdd:cd14040  234 DILQENTILKATE 246
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
548-737 6.38e-08

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 56.42  E-value: 6.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 548 VCMLFEYMNQGDLHEFLIMRSPhsdvgcssdedgTVKSSLDHGDFLhIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQL 627
Cdd:PTZ00283 114 IALVLDYANAGDLRQEIKSRAK------------TNRTFREHEAGL-LFIQVLLAVHHVHSKHMIHRDIKSANILLCSNG 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 628 HVKISDLGLSReIYSADYYRVQSKS--SLPIrWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGlQPYYGFSNQEVIEMV 705
Cdd:PTZ00283 181 LVKLGDFGFSK-MYAATVSDDVGRTfcGTPY-YVAPEIWRRKPYSKKADMFSLGVLLYELLTLK-RPFDGENMEEVMHKT 257
                        170       180       190
                 ....*....|....*....|....*....|..
gi 223461072 706 RKRQLLPCSEDCPPRMYSLMTECWNEIPSRRP 737
Cdd:PTZ00283 258 LAGRYDPLPPSISPEMQEIVTALLSSDPKRRP 289
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
522-700 7.48e-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: 54.60  E-value: 7.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 522 QEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLimrsphsdVGCSSDEDGTVKSSLdhGDFLHiaiqiaa 601
Cdd:cd14113   52 HELGVLQSLQHPQLVGLLDTFETPTSYILVLEMADQGRLLDYV--------VRWGNLTEEKIRFYL--REILE------- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 602 GMEYLSSHFFVHKDLAARNILIGEQLH---VKISDLGLSREIYSAdYYRVQSKSSlpIRWMPPEAIMYGKFSSDSDIWSF 678
Cdd:cd14113  115 ALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFGDAVQLNTT-YYIHQLLGS--PEFAAPEIILGNPVSLTSDLWSI 191
                        170       180
                 ....*....|....*....|..
gi 223461072 679 GVVLWEIFSfGLQPYYGFSNQE 700
Cdd:cd14113  192 GVLTYVLLS-GVSPFLDESVEE 212
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
521-700 7.51e-08

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: 54.65  E-value: 7.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 521 QQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSPHsdvgcsSDEDGTVkssldhgdflhIAIQIA 600
Cdd:cd14184   47 ENEVSILRRVKHPNIIMLIEEMDTPAELYLVMELVKGGDLFDAITSSTKY------TERDASA-----------MVYNLA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 601 AGMEYLSSHFFVHKDLAARNILIGE----QLHVKISDLGLSrEIYSADYYRVQSKSSlpirWMPPEAIMYGKFSSDSDIW 676
Cdd:cd14184  110 SALKYLHGLCIVHRDIKPENLLVCEypdgTKSLKLGDFGLA-TVVEGPLYTVCGTPT----YVAPEIIAETGYGLKVDIW 184
                        170       180
                 ....*....|....*....|....*
gi 223461072 677 SFGVVLWeIFSFGLQPYYGFSN-QE 700
Cdd:cd14184  185 AAGVITY-ILLCGFPPFRSENNlQE 208
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
482-687 8.49e-08

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 55.06  E-value: 8.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 482 CTFGKIYKGHLYLPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQ--EQPVCMLFEYMNQGD 559
Cdd:cd07868   23 CKVGRGTYGHVYKAKRKDGKDDKDYALKQIEGTGISMSACREIALLRELKHPNVISLQKVFLShaDRKVWLLFDYAEHDL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 560 LHEFLIMRSPHSDVGCSSDEDGTVKSSLdhgdflhiaIQIAAGMEYLSSHFFVHKDLAARNILI----GEQLHVKISDLG 635
Cdd:cd07868  103 WHIIKFHRASKANKKPVQLPRGMVKSLL---------YQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMG 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 223461072 636 LSREIYSADYYRVQSKSSLPIRWM-PPEAIMYGK-FSSDSDIWSFGVVLWEIFS 687
Cdd:cd07868  174 FARLFNSPLKPLADLDPVVVTFWYrAPELLLGARhYTKAIDIWAIGCIFAELLT 227
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
68-146 9.16e-08

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 50.61  E-value: 9.16e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223461072  68 TTSLGQTAELHCKVSGNPPPSIRWFKNDAPVVQEPRrisfRATNYGSRLRIRNLDTTDTGYFQCVATNGKKVVSTTGVL 146
Cdd:cd20957   12 TVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSR----VQILSEDVLVIPSVKREDKGMYQCFVRNDGDSAQATAEL 86
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
63-143 9.16e-08

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 50.59  E-value: 9.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  63 PMNNITTSLGQTAELHCK-VSGNPPPSIRWFKNDAPV-VQEPRRISFRATNYGSRLRIRNLDTTDTGYFQCVATN--GKK 138
Cdd:cd05750    5 EMKSQTVQEGSKLVLKCEaTSENPSPRYRWFKDGKELnRKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENilGKD 84

                 ....*
gi 223461072 139 VVSTT 143
Cdd:cd05750   85 TVTGN 89
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
475-707 9.59e-08

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: 54.30  E-value: 9.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd14083    7 FKEVLGTGAFSEVVLAEDKATG----KLVAIKCIDKKALKGKEDSLENEIAVLRKIKHPNIVQLLDIYESKSHLYLVMEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQGDLHEFLIMRsphsdvGCSSDEDGTvkssldhgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILI---GEQLHVKI 631
Cdd:cd14083   83 VTGGELFDRIVEK------GSYTEKDAS-----------HLIRQVLEAVDYLHSLGIVHRDLKPENLLYyspDEDSKIMI 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223461072 632 SDLGLSREIYSAdyyrVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWeIFSFGLQPYYGFSNQEVIEMVRK 707
Cdd:cd14083  146 SDFGLSKMEDSG----VMSTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISY-ILLCGYPPFYDENDSKLFAQILK 216
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
72-135 1.01e-07

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 50.55  E-value: 1.01e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223461072  72 GQTAELHCKVSGNPPPSIRWFKNDAPVVQEPRRISFRATNYGSRLRIRNLDTTDTGYFQCVATN 135
Cdd:cd20975   15 GQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVN 78
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
67-135 1.02e-07

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including 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. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 50.41  E-value: 1.02e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  67 ITTSLGQTAELHCKVSGNPPPSIRWFKNDAPVVQEPRRIS-FRATNYGsrLRIRNLDTTDTGYFQCVATN 135
Cdd:cd20949    9 TTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSkYRILADG--LLINKVTQDDTGEYTCRAYQ 76
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
479-687 1.04e-07

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: 54.26  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHlylpGMDHAQLVAIKTLKDYNNPQQWTE----FQQEASLMAELHHPNIVCLLGAVT--QEQPVCMLF 552
Cdd:cd06653   10 LGRGAFGEVYLCY----DADTGRELAVKQVPFDPDSQETSKevnaLECEIQLLKNLRHDRIVQYYGCLRdpEEKKLSIFV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 553 EYMNQGDLHEFLIMRSPHSdvgcssdEDGTVKSSLdhgdflhiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKIS 632
Cdd:cd06653   86 EYMPGGSVKDQLKAYGALT-------ENVTRRYTR----------QILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLG 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 223461072 633 DLGLSREIYS--ADYYRVQSKSSLPIrWMPPEAIMYGKFSSDSDIWSFGVVLWEIFS 687
Cdd:cd06653  149 DFGASKRIQTicMSGTGIKSVTGTPY-WMSPEVISGEGYGRKADVWSVACTVVEMLT 204
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
476-712 1.06e-07

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 55.10  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYKGHlylpGMDHAQLVAIKTLKdyNNPQQWTEFQQEASLMAELHHPN-----IVCLLGAVTQEQPVCM 550
Cdd:cd14228   20 LEFLGRGTFGQVAKCW----KRSTKEIVAIKILK--NHPSYARQGQIEVSILSRLSSENadeynFVRSYECFQHKNHTCL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 551 LFEYMNQgDLHEFLIMRSphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNIL----IGEQ 626
Cdd:cd14228   94 VFEMLEQ-NLYDFLKQNK---------------FSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMlvdpVRQP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 627 LHVKISDLGLSREIYSAdyyrVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVIEMVR 706
Cdd:cd14228  158 YRVKVIDFGSASHVSKA----VCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELF-LGWPLYPGASEYDQIRYIS 232

                 ....*.
gi 223461072 707 KRQLLP 712
Cdd:cd14228  233 QTQGLP 238
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
521-737 1.17e-07

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


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 53.97  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 521 QQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSPHSdvgcssdedgtvkssLDHGDFLHIAIQIA 600
Cdd:cd08221   47 LNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGNLHDKIAQQKNQL---------------FPEEVVLWYLYQIV 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 601 AGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSReIYSADYYRVQSKSSLPIrWMPPEAIMYGKFSSDSDIWSFGV 680
Cdd:cd08221  112 SAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISK-VLDSESSMAESIVGTPY-YMSPELVQGVKYNFKSDIWAVGC 189
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223461072 681 VLWEIFSfgLQPYYGFSNQ-----EVIEMVRKRQLLPCSEDcpprMYSLMTECWNEIPSRRP 737
Cdd:cd08221  190 VLYELLT--LKRTFDATNPlrlavKIVQGEYEDIDEQYSEE----IIQLVHDCLHQDPEDRP 245
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
72-148 1.31e-07

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 50.18  E-value: 1.31e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223461072  72 GQTAELHCKVS-GNPPPSIRWFKNDAPVVQEpRRISFRATN-YGSRLRIRNLDTTDTGYFQCVATNGKKVVSTTGVLFV 148
Cdd:cd20959   17 GMRAQLHCGVPgGDLPLNIRWTLDGQPISDD-LGITVSRLGrRSSILSIDSLEASHAGNYTCHARNSAGSASYTAPLTV 94
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
63-136 1.43e-07

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 49.72  E-value: 1.43e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223461072  63 PMNNITTSLGQTAELHCKVSGNPPPSIRWFKNDAPVVqePRRISFRatNYGSRLRIRNLDTTDTGYFQCVATNG 136
Cdd:cd05731    1 SESSTMVLRGGVLLLECIAEGLPTPDIRWIKLGGELP--KGRTKFE--NFNKTLKIENVSEADSGEYQCTASNT 70
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
596-695 1.50e-07

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 54.32  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 596 AIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSADyyrVQSKS--SLPiRWMPPEAIMYGKFSSDS 673
Cdd:cd05587  103 AAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGG---KTTRTfcGTP-DYIAPEIIAYQPYGKSV 178
                         90       100
                 ....*....|....*....|..
gi 223461072 674 DIWSFGVVLWEIFSfGLQPYYG 695
Cdd:cd05587  179 DWWAYGVLLYEMLA-GQPPFDG 199
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
523-712 1.59e-07

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: 54.15  E-value: 1.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 523 EASLMAELHHPNIVCLLGAV---TQEQpVCMLFEYMNQgDLHEFL-IMRSPHSDvgcssdedGTVKSSLdhgdflhiaIQ 598
Cdd:cd07843   54 EINILLKLQHPNIVTVKEVVvgsNLDK-IYMVMEYVEH-DLKSLMeTMKQPFLQ--------SEVKCLM---------LQ 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 599 IAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSadyyrvqsksslPIRWM----------PPEaIMYG- 667
Cdd:cd07843  115 LLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREYGS------------PLKPYtqlvvtlwyrAPE-LLLGa 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 223461072 668 -KFSSDSDIWSFGVvlweIFSfglqpyygfsnqeviEMVRKRQLLP 712
Cdd:cd07843  182 kEYSTAIDMWSVGC----IFA---------------ELLTKKPLFP 208
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
479-687 1.64e-07

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: 53.97  E-value: 1.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKghlyLPGMDHAQLVAIKTLKDYNNPQQWTEFQ-QEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQ 557
Cdd:cd07846    9 VGEGSYGMVMK----CRHKETGQIVAIKKFLESEDDKMVKKIAmREIKMLKQLRHENLVNLIEVFRRKKRWYLVFEFVDH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 558 GDLHEflIMRSPHSdvgcssdedgtvkssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLS 637
Cdd:cd07846   85 TVLDD--LEKYPNG---------------LDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFA 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223461072 638 R------EIYSaDYyrvqskssLPIRWM-PPEAIM----YGKfssDSDIWSFGVVLWEIFS 687
Cdd:cd07846  148 RtlaapgEVYT-DY--------VATRWYrAPELLVgdtkYGK---AVDVWAVGCLVTEMLT 196
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
521-702 1.75e-07

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: 53.46  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 521 QQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSPHSDvgcsSDEDGTVKSsldhgdflhiaiqIA 600
Cdd:cd14183   52 QNEVSILRRVKHPNIVLLIEEMDMPTELYLVMELVKGGDLFDAITSTNKYTE----RDASGMLYN-------------LA 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 601 AGMEYLSSHFFVHKDLAARNILIGEQL----HVKISDLGLSrEIYSADYYRVQSKSSlpirWMPPEAIMYGKFSSDSDIW 676
Cdd:cd14183  115 SAIKYLHSLNIVHRDIKPENLLVYEHQdgskSLKLGDFGLA-TVVDGPLYTVCGTPT----YVAPEIIAETGYGLKVDIW 189
                        170       180
                 ....*....|....*....|....*..
gi 223461072 677 SFGVVLWeIFSFGLQPYYGFS-NQEVI 702
Cdd:cd14183  190 AAGVITY-ILLCGFPPFRGSGdDQEVL 215
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
477-692 1.82e-07

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: 53.47  E-value: 1.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 477 EELGECTFGKIYKGHLylpgmdHAQlVAIKTLK-DYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVtqeqpvcmlfeym 555
Cdd:cd14153    6 ELIGKGRFGQVYHGRW------HGE-VAIRLIDiERDNEEQLKAFKREVMAYRQTRHENVVLFMGAC------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 nqgdlhefliMRSPHSDVGCSSDEDGTV-------KSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIgEQLH 628
Cdd:cd14153   66 ----------MSPPHLAIITSLCKGRTLysvvrdaKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGK 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 629 VKISDLGL----------SREiysaDYYRVQSK-----SSLPIRWMPPEAIMYG-KFSSDSDIWSFGVVLWEI----FSF 688
Cdd:cd14153  135 VVITDFGLftisgvlqagRRE----DKLRIQSGwlchlAPEIIRQLSPETEEDKlPFSKHSDVFAFGTIWYELhareWPF 210

                 ....
gi 223461072 689 GLQP 692
Cdd:cd14153  211 KTQP 214
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
522-706 1.89e-07

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: 53.37  E-value: 1.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 522 QEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYmnqgdLHEFLIMRSPHSDVGCSSDedgtVKSsldhgdflhIAIQIAA 601
Cdd:cd14108   47 RELALLAELDHKSIVRFHDAFEKRRVVIIVTEL-----CHEELLERITKRPTVCESE----VRS---------YMRQLLE 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 602 GMEYLSSHFFVHKDLAARNILIGEQL--HVKISDLGLSREIYSADyyRVQSKSSLPiRWMPPEAIMYGKFSSDSDIWSFG 679
Cdd:cd14108  109 GIEYLHQNDVLHLDLKPENLLMADQKtdQVRICDFGNAQELTPNE--PQYCKYGTP-EFVAPEIVNQSPVSKVTDIWPVG 185
                        170       180
                 ....*....|....*....|....*..
gi 223461072 680 VVLWEIFSfGLQPYYGFSNQEVIEMVR 706
Cdd:cd14108  186 VIAYLCLT-GISPFVGENDRTTLMNIR 211
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
469-742 1.92e-07

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


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 53.40  E-value: 1.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 469 PLSAVRFMEE--LGECTFGKIYKghlyLPGMDHAQLVAIKTLKD--YNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQ 544
Cdd:cd14187    3 PRTRRRYVRGrfLGKGGFAKCYE----ITDADTKEVFAGKIVPKslLLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFED 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 545 EQPVCMLFEYMNQGDLHEFLIMRSphsdvgcssdedgtvksSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIG 624
Cdd:cd14187   79 NDFVYVVLELCRRRSLLELHKRRK-----------------ALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLN 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 625 EQLHVKISDLGLSREIySADYYRVQSKSSLPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVIEM 704
Cdd:cd14187  142 DDMEVKIGDFGLATKV-EYDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDIWSIGCIMYTLL-VGKPPFETSCLKETYLR 218
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 223461072 705 VRKRQL-LPcsEDCPPRMYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14187  219 IKKNEYsIP--KHINPVAASLIQKMLQTDPTARPTINEL 255
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
522-685 1.98e-07

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: 53.90  E-value: 1.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 522 QEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFL--IMRSPHSDVGcssdedgtvkssldhgdflHIAIQI 599
Cdd:cd06649   52 RELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLkeAKRIPEEILG-------------------KVSIAV 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 600 AAGMEYL-SSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSAdyyrvQSKSSLPIR-WMPPEAIMYGKFSSDSDIWS 677
Cdd:cd06649  113 LRGLAYLrEKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDS-----MANSFVGTRsYMSPERLQGTHYSVQSDIWS 187

                 ....*...
gi 223461072 678 FGVVLWEI 685
Cdd:cd06649  188 MGLSLVEL 195
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
72-137 2.20e-07

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 49.47  E-value: 2.20e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223461072  72 GQTAELHCKVSGNPPPSIRWFKNDAPvvQEPRRISFRAtnyGSRLRIRNLDTTDTGYFQCVATNGK 137
Cdd:cd04968   16 GQTVTLECFALGNPVPQIKWRKVDGS--PSSQWEITTS---EPVLEIPNVQFEDEGTYECEAENSR 76
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
498-719 2.28e-07

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 54.85  E-value: 2.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072   498 DHAQLVAIKTLKD--YNNPQQWTEFQQEASLMAELHHPNIVCLL-GAVTQEQPVCMLFEYMNQGDLHEFLIMRSPhsdvg 574
Cdd:TIGR03903    1 MTGHEVAIKLLRTdaPEEEHQRARFRRETALCARLYHPNIVALLdSGEAPPGLLFAVFEYVPGRTLREVLAADGA----- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072   575 cssdedgtvkssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILI---GEQLHVKISDLGLS------REIYSADY 645
Cdd:TIGR03903   76 ------------LPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVsqtGVRPHAKVLDFGIGtllpgvRDADVATL 143
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223461072   646 YRVQSKSSLPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEmvrkRQLLPCSEDCPP 719
Cdd:TIGR03903  144 TRTTEVLGTP-TYCAPEQLRGEPVTPNSDLYAWGLIFLECLT-GQRVVQGASVAEILY----QQLSPVDVSLPP 211
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
598-742 2.53e-07

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: 53.01  E-value: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 598 QIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSADyYRVQSKSSLPiRWMPPEAIMYGKFSSDSDIWS 677
Cdd:cd14189  109 QIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPE-QRKKTICGTP-NYLAPEVLLRQGHGPESDVWS 186
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223461072 678 FGVVLWEIFSfGLQPYYGFSNQEVIEMVRK-RQLLPCSEDCPPRmySLMTECWNEIPSRRPRFKDI 742
Cdd:cd14189  187 LGCVMYTLLC-GNPPFETLDLKETYRCIKQvKYTLPASLSLPAR--HLLAGILKRNPGDRLTLDQI 249
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
67-148 2.56e-07

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 49.76  E-value: 2.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072   67 ITTSLGQTAELHCKVSG---NPPPSIRW---------------FKNDAPVVQEPRRISFRA-TNYGS-RLRIRNLDTTDT 126
Cdd:pfam07686   6 VTVALGGSVTLPCTYSSsmsEASTSVYWyrqppgkgptfliayYSNGSEEGVKKGRFSGRGdPSNGDgSLTIQNLTLSDS 85
                          90       100
                  ....*....|....*....|...
gi 223461072  127 GYFQCVATNGKKVVSTTGV-LFV 148
Cdd:pfam07686  86 GTYTCAVIPSGEGVFGKGTrLTV 108
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
60-138 2.67e-07

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 49.28  E-value: 2.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  60 LDEPmNNITTSLGQTAELHCKVSGNPPPSIRWFKNDAPVVQEpRRISFRATNYGSRLRIRNLDTTDTGYFQCVATN--GK 137
Cdd:cd05747    7 LTKP-RSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSS-QRHQITSTEYKSTFEISKVQMSDEGNYTVVVENseGK 84

                 .
gi 223461072 138 K 138
Cdd:cd05747   85 Q 85
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
486-737 2.70e-07

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


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 53.09  E-value: 2.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 486 KIYKGHlylpGMDHAQLVAI-----KTLKDYNNP--QQWTE-FQQEASLMAELHHPNIVCLLgAVTQEQPVCMLFEYmnq 557
Cdd:cd14011   11 KIYNGS----KKSTKQEVSVfvfekKQLEEYSKRdrEQILElLKRGVKQLTRLRHPRILTVQ-HPLEESRESLAFAT--- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 558 gdlhEFlIMRSPHSDVGCSSDEDGTVKSSLDHGdfLHIAI------QIAAGMEYLssHF---FVHKDLAARNILIGEQLH 628
Cdd:cd14011   83 ----EP-VFASLANVLGERDNMPSPPPELQDYK--LYDVEikygllQISEALSFL--HNdvkLVHGNICPESVVINSNGE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 629 VKISDLGLSREIYSA---DYYRVQSKSSLPI------RWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQ 699
Cdd:cd14011  154 WKLAGFDFCISSEQAtdqFPYFREYDPNLPPlaqpnlNYLAPEYILSKTCDPASDMFSLGVLIYAIYNKGKPLFDCVNNL 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 223461072 700 ---EVIEMVRKRQLLPCSEDCPPRMYSLMTECWNEIPSRRP 737
Cdd:cd14011  234 lsyKKNSNQLRQLSLSLLEKVPEELRDHVKTLLNVTPEVRP 274
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
59-149 2.75e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 49.27  E-value: 2.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  59 TLDEPMNNITTSLGQTAELHCKVSGNPPPSIRWFKnDAPVVQEPR----RISFRATNygSRLRIRNLDTTDTGYFQCVAT 134
Cdd:cd20974    2 VFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFR-DGQVISTSTlpgvQISFSDGR--AKLSIPAVTKANSGRYSLTAT 78
                         90
                 ....*....|....*
gi 223461072 135 NGKKVVSTTGVLFVK 149
Cdd:cd20974   79 NGSGQATSTAELLVL 93
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
476-685 2.77e-07

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: 52.89  E-value: 2.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGKIYkghLYLPGMDHAQLVaIKTLK-DYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd08218    5 IKKIGEGSFGKAL---LVKSKEDGKQYV-IKEINiSKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQGDLHEFLimrspHSDVGCSSDEDgtvkssldhgDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDL 634
Cdd:cd08218   81 CDGGDLYKRI-----NAQRGVLFPED----------QILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDF 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223461072 635 GLSREIYSA----------DYYrvqsksslpirwMPPEAIMYGKFSSDSDIWSFGVVLWEI 685
Cdd:cd08218  146 GIARVLNSTvelartcigtPYY------------LSPEICENKPYNNKSDIWALGCVLYEM 194
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
520-697 2.89e-07

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: 53.86  E-value: 2.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 520 FQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLheflimrsphsdVGCSSDEDGTVKSSLDHgdflhiAIQI 599
Cdd:cd05622  120 FWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL------------VNLMSNYDVPEKWARFY------TAEV 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 600 AAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSSLPiRWMPPEAIMY----GKFSSDSDI 675
Cdd:cd05622  182 VLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTP-DYISPEVLKSqggdGYYGRECDW 260
                        170       180
                 ....*....|....*....|..
gi 223461072 676 WSFGVVLWEIFsFGLQPYYGFS 697
Cdd:cd05622  261 WSVGVFLYEML-VGDTPFYADS 281
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
79-148 3.19e-07

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 49.00  E-value: 3.19e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072  79 CKVSGNPPPSIRWFKNDAPVVQEPRrISFraTNYGSrLRIRNLDTTDTGYFQCVATNGKKVVSTTGVLFV 148
Cdd:cd04969   24 CKPKASPKPTISWSKGTELLTNSSR-ICI--LPDGS-LKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
478-687 3.23e-07

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. 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 CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 53.15  E-value: 3.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 478 ELGECTFGKIYKGHLYlPGMDHAQLvaikTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQ--EQPVCMLFEYM 555
Cdd:cd07867    9 KVGRGTYGHVYKAKRK-DGKDEKEY----ALKQIEGTGISMSACREIALLRELKHPNVIALQKVFLShsDRKVWLLFDYA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 556 NQGDLHEFLIMRSPHSDVGCSSDEDGTVKSSLdhgdflhiaIQIAAGMEYLSSHFFVHKDLAARNILI----GEQLHVKI 631
Cdd:cd07867   84 EHDLWHIIKFHRASKANKKPMQLPRSMVKSLL---------YQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKI 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 223461072 632 SDLGLSREIYSADYYRVQSKSSLPIRWM-PPEAIMYGK-FSSDSDIWSFGVVLWEIFS 687
Cdd:cd07867  155 ADMGFARLFNSPLKPLADLDPVVVTFWYrAPELLLGARhYTKAIDIWAIGCIFAELLT 212
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
452-693 3.35e-07

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


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 53.50  E-value: 3.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 452 EMSMLNAYKPKSKAKELPLSAVRFMEELGECTFGKIYKGHLYLPGMDHAQLVAIKTLKDYNNPQQWTefQQEASLMAEL- 530
Cdd:cd05618    1 EKEAMNSRESGKASSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWV--QTEKHVFEQAs 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 531 HHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHeFLIMRSPhsdvgcssdedgtvKSSLDHGDFlhIAIQIAAGMEYLSSHF 610
Cdd:cd05618   79 NHPFLVGLHSCFQTESRLFFVIEYVNGGDLM-FHMQRQR--------------KLPEEHARF--YSAEISLALNYLHERG 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 611 FVHKDLAARNILIGEQLHVKISDLGLSRE-IYSADyyrVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfG 689
Cdd:cd05618  142 IIYRDLKLDNVLLDSEGHIKLTDYGMCKEgLRPGD---TTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMA-G 217

                 ....
gi 223461072 690 LQPY 693
Cdd:cd05618  218 RSPF 221
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
594-750 3.81e-07

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: 52.76  E-value: 3.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 594 HIAIQIAAGMEYL-SSHFFVHKDLAARNILIGEQLHVKISDLGLS-REIYSadyyRVQSKSSLPIRWMPPEAI---MYGK 668
Cdd:cd06618  118 KMTVSIVKALHYLkEKHGVIHRDVKPSNILLDESGNVKLCDFGISgRLVDS----KAKTRSAGCAAYMAPERIdppDNPK 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 669 FSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQ-EVIEMVRKRQL--LPCSEDCPPRMYSLMTECWNEIPSRRPRFKDI--H 743
Cdd:cd06618  194 YDIRADVWSLGISLVELAT-GQFPYRNCKTEfEVLTKILNEEPpsLPPNEGFSPDFCSFVDLCLTKDHRYRPKYRELlqH 272

                 ....*..
gi 223461072 744 VRLRSWE 750
Cdd:cd06618  273 PFIRRYE 279
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
72-140 3.98e-07

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.


Pssm-ID: 143220  Cd Length: 78  Bit Score: 48.25  E-value: 3.98e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223461072  72 GQTAELHCKVSGNPPPSIRWFKNDAPVVQEPRRISFRATNYGSrLRIRNLDTTDTGYFQCVATNGKKVV 140
Cdd:cd05743    1 GETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEGGYGT-LTIRDVKESDQGAYTCEAINTRGMV 68
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
443-697 4.42e-07

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: 53.08  E-value: 4.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 443 PKPVRGQNVEmSMLNAY-KPKSKAKELPLSAVRF--MEELGECTFGKIYkghlyLPGMDHAQLV-AIKTLKDYNNPQQWT 518
Cdd:cd05621   22 PALRKNKNID-NFLNRYeKIVNKIRELQMKAEDYdvVKVIGRGAFGEVQ-----LVRHKASQKVyAMKLLSKFEMIKRSD 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 519 E--FQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLheflimrsphsdVGCSSDEDGTVKSSLDHgdflhiA 596
Cdd:cd05621   96 SafFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEYMPGGDL------------VNLMSNYDVPEKWAKFY------T 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 597 IQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSSLPiRWMPPEAIMY----GKFSSD 672
Cdd:cd05621  158 AEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKMDETGMVHCDTAVGTP-DYISPEVLKSqggdGYYGRE 236
                        250       260
                 ....*....|....*....|....*
gi 223461072 673 SDIWSFGVVLWEIFsFGLQPYYGFS 697
Cdd:cd05621  237 CDWWSVGVFLFEML-VGDTPFYADS 260
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
476-742 4.65e-07

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: 52.00  E-value: 4.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 476 MEELGECTFGK----IYKGHLYLpgmdhaqlVAIK-TLKDYNNPQQWTEFQQ------EASLMAELH---HPNIVCLLGa 541
Cdd:cd14004    5 LKEMGEGAYGQvnlaIYKSKGKE--------VVIKfIFKERILVDTWVRDRKlgtvplEIHILDTLNkrsHPNIVKLLD- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 542 vtqeqpvcmLFEymnqGDLHEFLIMrSPHsdvGCSSDEDGTV--KSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAAR 619
Cdd:cd14004   76 ---------FFE----DDEFYYLVM-EKH---GSGMDLFDFIerKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDE 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 620 NILIGEQLHVKISDLGlsreiySADYYRVQSKSSL--PIRWMPPEAIMYGKF-SSDSDIWSFGVVLWEIFsFGLQPYYgf 696
Cdd:cd14004  139 NVILDGNGTIKLIDFG------SAAYIKSGPFDTFvgTIDYAAPEVLRGNPYgGKEQDIWALGVLLYTLV-FKENPFY-- 209
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 223461072 697 snqEVIEMVRKRQLLP--CSEDCpprmYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14004  210 ---NIEEILEADLRIPyaVSEDL----IDLISRMLNRDVGDRPTIEEL 250
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
479-742 4.74e-07

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 52.16  E-value: 4.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDyNNPQQWTEFQQ------EASLMAEL----HHPNIVCLLGAVTQEQPV 548
Cdd:cd14101    8 LGKGGFGTVYAGHRISDG----LQVAIKQISR-NRVQQWSKLPGvnpvpnEVALLQSVgggpGHRGVIRLLDWFEIPEGF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 549 CMLFEY-MNQGDLHEFLImrsphsdvgcssdEDGTVKSSLDHGDFLhiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQL 627
Cdd:cd14101   83 LLVLERpQHCQDLFDYIT-------------ERGALDESLARRFFK----QVVEAVQHCHSKGVVHRDIKDENILVDLRT 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 628 -HVKISDLG----LSREIYSA-DYYRVQSksslpirwmPPEAIMYGKFSS-DSDIWSFGVVLWEIFSfGLQPyygFSNQE 700
Cdd:cd14101  146 gDIKLIDFGsgatLKDSMYTDfDGTRVYS---------PPEWILYHQYHAlPATVWSLGILLYDMVC-GDIP---FERDT 212
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 223461072 701 VIEMVRKRQLLPCSEDCpprmYSLMTECWNEIPSRRPRFKDI 742
Cdd:cd14101  213 DILKAKPSFNKRVSNDC----RSLIRSCLAYNPSDRPSLEQI 250
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
532-737 4.94e-07

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 52.50  E-value: 4.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 532 HPNIVCLLGAVTQEQPVC---------MLFEYMNQGDLHE----FLIMRS-PHSDVG--CSSDEDGTVKSSldhgdflhI 595
Cdd:cd14018   72 HPNIIRVQRAFTDSVPLLpgaiedypdVLPARLNPSGLGHnrtlFLVMKNyPCTLRQylWVNTPSYRLARV--------M 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 596 AIQIAAGMEYLSSHFFVHKDLAARNILIGEQL----HVKISDLG--LSREI------YSADYYRVQSKSSLpirwMPPEA 663
Cdd:cd14018  144 ILQLLEGVDHLVRHGIAHRDLKSDNILLELDFdgcpWLVIADFGccLADDSiglqlpFSSWYVDRGGNACL----MAPEV 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 664 I--MYGKFS----SDSDIWSFGVVLWEIFSFGlQPYYGFSNQEVIEM-VRKRQLLPCSEDCPPRMYSLMTECWNEIPSRR 736
Cdd:cd14018  220 StaVPGPGVvinySKADAWAVGAIAYEIFGLS-NPFYGLGDTMLESRsYQESQLPALPSAVPPDVRQVVKDLLQRDPNKR 298

                 .
gi 223461072 737 P 737
Cdd:cd14018  299 V 299
Ig4_NrCAM cd05868
Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); The ...
63-135 5.29e-07

Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); The members here are composed of the fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule). NrCAM belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six IG-like domains and five fibronectin type III domains, a transmembrane region, and an intracellular domain. NrCAM is primarily expressed in the nervous system.


Pssm-ID: 409454  Cd Length: 89  Bit Score: 48.44  E-value: 5.29e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223461072  63 PMNNITTSLGQTAELHCKVSGNPPPSIRWFKNDAPVVQEPRRISFRATnyGSRLRIRNLDTTDTGYFQCVATN 135
Cdd:cd05868    5 APTNLVLSPGEDGTLICRANGNPKPSISWLTNGVPIEIAPTDPSRKVD--GDTIIFSKVQERSSAVYQCNASN 75
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
479-720 5.87e-07

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: 52.37  E-value: 5.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHlylpGMDHAQLVAIK------TLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQE-QPVCML 551
Cdd:cd14041   14 LGRGGFSEVYKAF----DLTEQRYVAVKihqlnkNWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDtDSFCTV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 552 FEYMNQGDLHEFLIMRSPHSDVGCSSdedgtvkssldhgdflhIAIQIAAGMEYLSS--HFFVHKDLAARNILI------ 623
Cdd:cd14041   90 LEYCEGNDLDFYLKQHKLMSEKEARS-----------------IIMQIVNALKYLNEikPPIIHYDLKPGNILLvngtac 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 624 GEqlhVKISDLGLSREIYSADYYRVQ-----SKSSLPIRWMPPEAIMYGK----FSSDSDIWSFGVVLWEIFsFGLQPYY 694
Cdd:cd14041  153 GE---IKITDFGLSKIMDDDSYNSVDgmeltSQGAGTYWYLPPECFVVGKeppkISNKVDVWSVGVIFYQCL-YGRKPFG 228
                        250       260
                 ....*....|....*....|....*..
gi 223461072 695 gfSNQEVIEMVRKRQLLPCSE-DCPPR 720
Cdd:cd14041  229 --HNQSQQDILQENTILKATEvQFPPK 253
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
72-135 6.60e-07

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 48.31  E-value: 6.60e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223461072  72 GQTAELHCKVSGNPPPSIRWFKNDAPVVQEPRRISFRATNYGSRLRIRNLDTTDTGYFQCVATN 135
Cdd:cd05857   19 ANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVEN 82
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
479-736 6.93e-07

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: 52.19  E-value: 6.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIykghLYLPGMDHAQLVAIKTLKDYN--NPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMN 556
Cdd:cd05585    2 IGKGSFGKV----MQVRKKDTSRIYALKTIRKAHivSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFIN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 557 QGDLHEFLiMRSPHSDVGCSSdedgtvkssldhgdfLHIAiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGL 636
Cdd:cd05585   78 GGELFHHL-QREGRFDLSRAR---------------FYTA-ELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 637 SReIYSADYYRVQSKSSLPiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYgfsNQEVIEMVRK--RQLLPCS 714
Cdd:cd05585  141 CK-LNMKDDDKTNTFCGTP-EYLAPELLLGHGYTKAVDWWTLGVLLYEMLT-GLPPFY---DENTNEMYRKilQEPLRFP 214
                        250       260
                 ....*....|....*....|..
gi 223461072 715 EDCPPRMYSLMTECWNEIPSRR 736
Cdd:cd05585  215 DGFDRDAKDLLIGLLNRDPTKR 236
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
498-708 7.26e-07

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: 51.91  E-value: 7.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 498 DHAQLVAIKTLKDYNNPQQWTEFQQEASlmaelHHPNIVCLLGavtqeqpvcmLFEYMNQGDLHEFLIMRSPH-----SD 572
Cdd:cd14172   27 RTGQKCALKLLYDSPKARREVEHHWRAS-----GGPHIVHILD----------VYENMHHGKRCLLIIMECMEggelfSR 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 573 VGCSSDEDGTVKSSLDhgdflhIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQ---LHVKISDLGLSREiySADYYRVQ 649
Cdd:cd14172   92 IQERGDQAFTEREASE------IMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKekdAVLKLTDFGFAKE--TTVQNALQ 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 223461072 650 SKSSLPIrWMPPEAIMYGKFSSDSDIWSFGVVLWeIFSFGLQPYYGFSNQEVIEMVRKR 708
Cdd:cd14172  164 TPCYTPY-YVAPEVLGPEKYDKSCDMWSLGVIMY-ILLCGFPPFYSNTGQAISPGMKRR 220
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
531-693 7.33e-07

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: 51.94  E-value: 7.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 531 HHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSphsdvgCSSDEDGTVkssldhgdflhIAIQIAAGMEYLSSHF 610
Cdd:cd14178   55 QHPNIITLKDVYDDGKFVYLVMELMRGGELLDRILRQK------CFSEREASA-----------VLCTITKTVEYLHSQG 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 611 FVHKDLAARNILI----GEQLHVKISDLGLSREIYSADyyRVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIF 686
Cdd:cd14178  118 VVHRDLKPSNILYmdesGNPESIRICDFGFAKQLRAEN--GLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGILLYTML 195

                 ....*..
gi 223461072 687 SfGLQPY 693
Cdd:cd14178  196 A-GFTPF 201
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
520-694 8.26e-07

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: 51.75  E-value: 8.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 520 FQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSPHSDvgcsSDEDGTVKssldhgdflhiaiQI 599
Cdd:cd14085   45 VRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGGELFDRIVEKGYYSE----RDAADAVK-------------QI 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 600 AAGMEYLSSHFFVHKDLAARNIL---IGEQLHVKISDLGLSREIysADYYRVQSKSSLPiRWMPPEAIMYGKFSSDSDIW 676
Cdd:cd14085  108 LEAVAYLHENGIVHRDLKPENLLyatPAPDAPLKIADFGLSKIV--DQQVTMKTVCGTP-GYCAPEILRGCAYGPEVDMW 184
                        170
                 ....*....|....*...
gi 223461072 677 SFGVVLWeIFSFGLQPYY 694
Cdd:cd14085  185 SVGVITY-ILLCGFEPFY 201
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
520-687 8.40e-07

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 51.86  E-value: 8.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 520 FQQEASLMAELH-HPNIVCLLGAVTQEQPV-----CMLFEYMNQgDLHEFLIMRSPHsdvGCSSdedgtvkssldhGDFL 593
Cdd:cd14020   50 FAKERAALEQLQgHRNIVTLYGVFTNHYSAnvpsrCLLLELLDV-SVSELLLRSSNQ---GCSM------------WMIQ 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 594 HIAIQIAAGMEYLSSHFFVHKDLAARNIL-IGEQLHVKISDLGLSREIYSADYYRVQSKSslpirWMPPEA-----IMYG 667
Cdd:cd14020  114 HCARDVLEALAFLHHEGYVHADLKPRNILwSAEDECFKLIDFGLSFKEGNQDVKYIQTDG-----YRAPEAelqncLAQA 188
                        170       180
                 ....*....|....*....|....*.
gi 223461072 668 KFSSDS------DIWSFGVVLWEIFS 687
Cdd:cd14020  189 GLQSETectsavDLWSLGIVLLEMFS 214
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
72-137 8.83e-07

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 47.39  E-value: 8.83e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223461072   72 GQTAELHCKVSGNPPPSIRWFKNDAPVvqeprrisfratNYGSRLRIRNLDTTDTGYFQCVATNGK 137
Cdd:pfam13895  14 GEPVTLTCSAPGNPPPSYTWYKDGSAI------------SSSPNFFTLSVSAEDSGTYTCVARNGR 67
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
523-706 9.69e-07

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


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 51.36  E-value: 9.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 523 EASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLhefLIMRSPHSDVGCSSDEDgtvkssldhgdFLHIAIQIAAG 602
Cdd:cd14109   46 EVDIHNSLDHPNIVQMHDAYDDEKLAVTVIDNLASTIE---LVRDNLLPGKDYYTERQ-----------VAVFVRQLLLA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 603 MEYLSSHFFVHKDLAARNILIGEQlHVKISDLGLSREIysadyyrVQSKSSLPIRWMP----PEAIMYGKFSSDSDIWSF 678
Cdd:cd14109  112 LKHMHDLGIAHLDLRPEDILLQDD-KLKLADFGQSRRL-------LRGKLTTLIYGSPefvsPEIVNSYPVTLATDMWSV 183
                        170       180
                 ....*....|....*....|....*...
gi 223461072 679 GVVLWEIFSfGLQPYYGFSNQEVIEMVR 706
Cdd:cd14109  184 GVLTYVLLG-GISPFLGDNDRETLTNVR 210
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
501-685 9.86e-07

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: 51.54  E-value: 9.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 501 QLVAIKTLKDYNNPQQWTEFQ-QEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHefLIMRSPHsdvGCSSDE 579
Cdd:cd07848   27 EIVAIKKFKDSEENEEVKETTlRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEKNMLE--LLEEMPN---GVPPEK 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 580 dgtVKSSLdhgdflhiaIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSR---EIYSADYyrvqsKSSLPI 656
Cdd:cd07848  102 ---VRSYI---------YQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARnlsEGSNANY-----TEYVAT 164
                        170       180       190
                 ....*....|....*....|....*....|
gi 223461072 657 RWM-PPEAIMYGKFSSDSDIWSFGVVLWEI 685
Cdd:cd07848  165 RWYrSPELLLGAPYGKAVDMWSVGCILGEL 194
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
475-707 1.10e-06

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


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 51.59  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 475 FMEELGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEY 554
Cdd:cd14168   14 FKEVLGTGAFSEVVLAEERATG----KLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 555 MNQGDLHEFLIMRSPHSDvgcsSDEDGTVKSSLDHGDFLHiaiqiaagmeylsSHFFVHKDLAARNILI---GEQLHVKI 631
Cdd:cd14168   90 VSGGELFDRIVEKGFYTE----KDASTLIRQVLDAVYYLH-------------RMGIVHRDLKPENLLYfsqDEESKIMI 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223461072 632 SDLGLSREIYSADyyrVQSKSSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWeIFSFGLQPYYGFSNQEVIEMVRK 707
Cdd:cd14168  153 SDFGLSKMEGKGD---VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQILK 224
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
501-687 1.11e-06

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: 51.54  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 501 QLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLL-----GAVTQEQPVCMLFEYMnQGDLHEfLIMRSPHSDvgc 575
Cdd:cd07849   31 QKVAIKKISPFEHQTYCLRTLREIKILLRFKHENIIGILdiqrpPTFESFKDVYIVQELM-ETDLYK-LIKTQHLSN--- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 576 ssdedgtvksslDHGD-FLHiaiQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSREIYSADYYRVQSKSSL 654
Cdd:cd07849  106 ------------DHIQyFLY---QILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARIADPEHDHTGFLTEYV 170
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 223461072 655 PIRWM-PPEaIM--YGKFSSDSDIWSFGVVLWEIFS 687
Cdd:cd07849  171 ATRWYrAPE-IMlnSKGYTKAIDIWSVGCILAEMLS 205
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
479-639 1.13e-06

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


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 51.22  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 479 LGECTFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQG 558
Cdd:cd14046   14 LGKGAFGQVVKVRNKLDG----RYYAIKKIKLRSESKNNSRILREVMLLSRLNHQHVVRYYQAWIERANLYIQMEYCEKS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 559 DLHEfLIMRSPHSDVgcssdedgtvkssldhgDFL-HIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLS 637
Cdd:cd14046   90 TLRD-LIDSGLFQDT-----------------DRLwRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLA 151

                 ..
gi 223461072 638 RE 639
Cdd:cd14046  152 TS 153
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
496-693 1.15e-06

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: 51.56  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 496 GMDHAQLVAIKTLKDynnPQQWTEFqqeasLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSPHSDVGC 575
Cdd:cd14176   44 NMEFAVKIIDKSKRD---PTEEIEI-----LLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 576 SSdedgtvkssldhgdflhIAIQIAAGMEYLSSHFFVHKDLAARNILI----GEQLHVKISDLGLSREIYSADyyRVQSK 651
Cdd:cd14176  116 SA-----------------VLFTITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAKQLRAEN--GLLMT 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 223461072 652 SSLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPY 693
Cdd:cd14176  177 PCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLT-GYTPF 217
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
497-693 1.15e-06

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: 51.18  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 497 MDHAQLVAIKTLKDynnPQQWTEFqqeasLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRSPHSDVGCS 576
Cdd:cd14175   27 MEYAVKVIDKSKRD---PSEEIEI-----LLRYGQHPNIITLKDVYDDGKHVYLVTELMRGGELLDKILRQKFFSEREAS 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 577 SdedgtvkssldhgdFLHiaiQIAAGMEYLSSHFFVHKDLAARNILI----GEQLHVKISDLGLSREI-----------Y 641
Cdd:cd14175   99 S--------------VLH---TICKTVEYLHSQGVVHRDLKPSNILYvdesGNPESLRICDFGFAKQLraengllmtpcY 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 223461072 642 SADYyrvqsksslpirwMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPY 693
Cdd:cd14175  162 TANF-------------VAPEVLKRQGYDEGCDIWSLGILLYTMLA-GYTPF 199
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
532-705 1.35e-06

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: 51.07  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 532 HPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLimrsphsdvgcssdedgTVKSSLDHGDFLHIAIQIAAGMEYLSSHFF 611
Cdd:cd14182   69 HPNIIQLKDTYETNTFFFLVFDLMKKGELFDYL-----------------TEKVTLSEKETRKIMRALLEVICALHKLNI 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 612 VHKDLAARNILIGEQLHVKISDLGLSREIYSADyyRVQSKSSLPiRWMPPEAIM---------YGKfssDSDIWSFGVVL 682
Cdd:cd14182  132 VHRDLKPENILLDDDMNIKLTDFGFSCQLDPGE--KLREVCGTP-GYLAPEIIEcsmddnhpgYGK---EVDMWSTGVIM 205
                        170       180
                 ....*....|....*....|...
gi 223461072 683 WEIFSfGLQPYYGFSNQEVIEMV 705
Cdd:cd14182  206 YTLLA-GSPPFWHRKQMLMLRMI 227
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
523-685 1.41e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 51.53  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 523 EASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMnQGDLHEFLimrsphsdvgcssdedgTVKSSLDHGDFLHIAIQIAAG 602
Cdd:PHA03212 133 EAHILRAINHPSIIQLKGTFTYNKFTCLILPRY-KTDLYCYL-----------------AAKRNIAICDILAIERSVLRA 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 603 MEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLS---REIYSADYYRVQSKsslpIRWMPPEAIMYGKFSSDSDIWSFG 679
Cdd:PHA03212 195 IQYLHENRIIHRDIKAENIFINHPGDVCLGDFGAAcfpVDINANKYYGWAGT----IATNAPELLARDPYGPAVDIWSAG 270

                 ....*.
gi 223461072 680 VVLWEI 685
Cdd:PHA03212 271 IVLFEM 276
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
72-148 1.43e-06

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 46.86  E-value: 1.43e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223461072  72 GQTAELHCKVSGNPPPSIRWFKNDAPVVQEPRRISFRAtnygSRLRIRNLDTTDTGYFQCVATNGKKVVSTTGVLFV 148
Cdd:cd05745    2 GQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLSS----GTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
71-137 1.68e-06

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 143259  Cd Length: 88  Bit Score: 46.94  E-value: 1.68e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223461072  71 LGQTAELHCKVSGNPPPSIRWFKndapvVQEPRRISFRATNYGSRLRIRNLDTTDTGYFQCVATNGK 137
Cdd:cd05851   15 KGQNVTLECFALGNPVPVIRWRK-----ILEPMPATAEISMSGAVLKIFNIQPEDEGTYECEAENIK 76
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
501-693 1.69e-06

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: 50.61  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 501 QLVAIKTL-KDYNNPQQWtefQQEASLMAELHHPNIVCLLGAVTQEQPVCMLFEYMNQGDLHEFLIMRsphsdvGCSSDE 579
Cdd:cd14087   27 QPYAIKMIeTKCRGREVC---ESELNVLRRVRHTNIIQLIEVFETKERVYMVMELATGGELFDRIIAK------GSFTER 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 580 DGTvkssldhgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILI---GEQLHVKISDLGLSREIYSADYYRVQSKSSLPi 656
Cdd:cd14087   98 DAT-----------RVLQMVLDGVKYLHGLGITHRDLKPENLLYyhpGPDSKIMITDFGLASTRKKGPNCLMKTTCGTP- 165
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 223461072 657 RWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPY 693
Cdd:cd14087  166 EYIAPEILLRKPYTQSVDMWAVGVIAYILLS-GTMPF 201
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
537-683 1.75e-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: 51.02  E-value: 1.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 537 CLLGAVT--QEQPVCMLF--EYMNQGDLHEFLIMRSPHSDVGCSsdedgtvkssldhgdFLhiaIQIAAGMEYLSSHFFV 612
Cdd:cd13977   95 SLKGERCfdPRSACYLWFvmEFCDGGDMNEYLLSRRPDRQTNTS---------------FM---LQLSSALAFLHRNQIV 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223461072 613 HKDLAARNILIGEQLH---VKISDLGLSR----------EIYSADYYRVQSKSSLPIrWMPPEaIMYGKFSSDSDIWSFG 679
Cdd:cd13977  157 HRDLKPDNILISHKRGepiLKVADFGLSKvcsgsglnpeEPANVNKHFLSSACGSDF-YMAPE-VWEGHYTAKADIFALG 234

                 ....
gi 223461072 680 VVLW 683
Cdd:cd13977  235 IIIW 238
 
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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